Author: "Richard J. Reece" - Searchworks@Jio Institute Digital Library Search Results

Your search keyword '"Richard J. Reece"' showing total 223 results

Start Over Author "Richard J. Reece"

223 results on '"Richard J. Reece"'

1. Analysis of Genes and Genomes

Author: Richard J. Reece
Published: 2004

2. Interplay of a Ligand Sensor and an Enzyme in Controlling Expression of the Saccharomyces cerevisiae GAL Genes

Author: Christopher Page, Richard J. Reece, Dariusz Abramczyk, and Stacey Holden
Subjects: Saccharomyces cerevisiae Proteins, Transcription, Genetic, Saccharomyces cerevisiae, Biology, Microbiology, Galactokinase, Bacterial Proteins, Genes, Reporter, Gene Expression Regulation, Fungal, Gene expression, Transcriptional regulation, gal operon, Molecular Biology, Gene, Transcription factor, Cell Nucleus, Galactose, Articles, General Medicine, Ligand (biochemistry), biology.organism_classification, Luminescent Proteins, Biochemistry, Protein Binding, Signal Transduction, Transcription Factors
Abstract: The regulation of the Saccharomyces cerevisiae GAL genes in response to galactose as a source of carbon has served as a paradigm for eukaryotic transcriptional control over the last 50 years. Three proteins—a transcriptional activator (Gal4p), an inhibitor (Gal80p), and a ligand sensor (Gal3p)—control the switch between inert and active gene expression. The molecular mechanism by which the recognition of galactose within the cell is converted into a transcriptional response has been the subject of considerable debate. In this study, using a novel and powerful method of localizing active transcription factors within the nuclei of cells, we show that a short-lived complex between Gal4p, Gal80p, and Gal3p occurs soon after the addition of galactose to cells to activate GAL gene expression. Gal3p is subsequently replaced in this complex by Gal1p, and a Gal4p-Gal80p-Gal1p complex is responsible for the continued expression of the GAL genes. The transient role of the ligand sensor indicates that current models for the induction and continued expression of the yeast GAL genes need to be reevaluated.
Published: 2012

3. Localization and Interaction of the Proteins Constituting the GAL Genetic Switch in Saccharomyces cerevisiae

Author: Rachel Bell, Raymond Wightman, and Richard J. Reece
Subjects: Cell Nucleus, Cytoplasm, Saccharomyces cerevisiae Proteins, biology, Saccharomyces cerevisiae, Galactose, Articles, General Medicine, biology.organism_classification, Microbiology, DNA-binding protein, DNA-Binding Proteins, Repressor Proteins, Protein Transport, Biochemistry, Gene expression, Transcriptional regulation, gal operon, Molecular Biology, Gene, Cellular localization, Protein Binding, Transcription Factors
Abstract: In Saccharomyces cerevisiae , the GAL genes encode the enzymes required for galactose metabolism. Regulation of these genes has served as the paradigm for eukaryotic transcriptional control over the last 50 years. The switch between inert and active gene expression is dependent upon three proteins—the transcriptional activator Gal4p, the inhibitor Gal80p, and the ligand sensor Gal3p. Here, we present a detailed spatial analysis of the three GAL regulatory proteins produced from their native genomic loci. Using a novel application of photobleaching, we demonstrate, for the first time, that the Gal3p ligand sensor enters the nucleus of yeast cells in the presence of galactose. Additionally, using Förster resonance energy transfer, we show that the interaction between Gal3p and Gal80p occurs throughout the yeast cell. Taken together, these data challenge existing models for the cellular localization of the regulatory proteins during the induction of GAL gene expression by galactose and suggest a mechanism for the induction of the GAL genes in which galactose-bound Gal3p moves from the cytoplasm to the nucleus to interact with the transcriptional inhibitor Gal80p.
Published: 2008

4. The Interaction between an Acidic Transcriptional Activator and Its Inhibitor

Author: Louise A. Ryan, James B. Thoden, Richard J. Reece, and Hazel M. Holden
Subjects: Activator (genetics), Repressor, Cell Biology, Plasma protein binding, Biology, Biochemistry, DNA-binding protein, Cell biology, Transactivation, Gene expression, Binding site, Molecular Biology, Peptide sequence
Abstract: The GAL genes, which encode the enzymes required for normal galactose metabolism in yeast, are transcriptionally regulated by three proteins: Gal4p, an activator; Gal80p, an inhibitor; and Gal3p, a galactose sensor. These proteins control the switch between inert and active gene expression. The transcriptional activation function of Gal4p is rendered inactive in the presence of Gal80p. Here we present the three-dimensional structure of a complex between the acidic activation domain of Gal4p and Gal80p. The transactivation domain initiates with an extended region of polypeptide chain followed by two turns of an amphipathic α-helix. It fits into and across a deep cleft within the Gal80p dimer with the protein-protein interface defined primarily by hydrophobic interactions. A disordered loop in the apo-Gal80p structure (Asp-309 to Ser-316) becomes well-defined upon binding of the transactivation domain. This investigation provides a new molecular scaffold for understanding previous biochemical and genetic studies.
Published: 2008

5. Metabolic control of transcription: paradigms and lessons from Saccharomyces cerevisiae

Author: Robert N. Campbell, Michael K. Leverentz, Richard J. Reece, and Louise A. Ryan
Subjects: Genetics, Saccharomyces cerevisiae Proteins, Transcription, Genetic, biology, Saccharomyces cerevisiae, Galactose, Cell Biology, Computational biology, biology.organism_classification, Models, Biological, Biochemistry, Protein Structure, Secondary, chemistry.chemical_compound, chemistry, Transcription (biology), Gene Expression Regulation, Fungal, Metabolic control analysis, Gene expression, Eukaryote, Molecular Biology, Gene, Organism
Abstract: The comparatively simple eukaryote Saccharomyces cerevisiae is composed of some 6000 individual genes. Specific sets of these genes can be transcribed co-ordinately in response to particular metabolic signals. The resultant integrated response to nutrient challenge allows the organism to survive and flourish in a variety of environmental conditions while minimal energy is expended upon the production of unnecessary proteins. The Zn(II)2Cys6 family of transcriptional regulators is composed of some 46 members in S. cerevisiae and many of these have been implicated in mediating transcriptional responses to specific nutrients. Gal4p, the archetypical member of this family, is responsible for the expression of the GAL genes when galactose is utilized as a carbon source. The regulation of Gal4p activity has been studied for many years, but we are still uncovering both nuances and fundamental control mechanisms that impinge on its function. In the present review, we describe the latest developments in the regulation of GAL gene expression and compare the mechanisms employed here with the molecular control of other Zn(II)2Cys6 transcriptional regulators. This reveals a wide array of protein–protein, protein–DNA and protein–nutrient interactions that are employed by this family of regulators.
Published: 2008

6. Understanding a Transcriptional Paradigm at the Molecular Level

Author: Christopher A. Sellick, James B. Thoden, Richard J. Reece, and Hazel M. Holden
Subjects: Kluyveromyces lactis, chemistry.chemical_classification, biology, Activator (genetics), Repressor, Cell Biology, biology.organism_classification, Biochemistry, chemistry.chemical_compound, chemistry, Oxidoreductase, Galactose, Gene expression, Transcriptional regulation, Molecular Biology, Gene
Abstract: In yeast, the GAL genes encode the enzymes required for normal galactose metabolism. Regulation of these genes in response to the organism being challenged with galactose has served as a paradigm for eukaryotic transcriptional control over the last 50 years. Three proteins, the activator Gal4p, the repressor Gal80p, and the ligand sensor Gal3p, control the switch between inert and active gene expression. Gal80p, the focus of this investigation, plays a pivotal role both in terms of repressing the activity of Gal4p and allowing the GAL switch to respond to galactose. Here we present the three-dimensional structure of Gal80p from Kluyveromyces lactis and show that it is structurally homologous to glucose-fructose oxidoreductase, an enzyme in the sorbitol-gluconate pathway. Our results clearly define the overall tertiary and quaternary structure of Gal80p and suggest that Gal4p and Gal3p bind to Gal80p at distinct but overlapping sites. In addition to providing a molecular basis for previous biochemical and genetic studies, our structure demonstrates that much of the enzymatic scaffold of the oxidoreductase has been maintained in Gal80p, but it is utilized in a very different manner to facilitate transcriptional regulation.
Published: 2007

7. Phosphorylation of Zn(II)2Cys6 proteins: a cause or effect of transcriptional activation?

Author: Michael K. Leverentz and Richard J. Reece
Subjects: Saccharomyces cerevisiae Proteins, Monosaccharide Transport Proteins, Transcription, Genetic, Chemistry, Membrane Proteins, Saccharomyces cerevisiae, Biochemistry, DNA-Binding Proteins, Gene Expression Regulation, Trans-Activators, Transcriptional regulation, Phosphorylation, sense organs, Transcription Factors
Abstract: Many Zn(II)2Cys6 transcriptional regulators exhibit changes in phosphorylation that are coincident with their roles in transcriptional activation. It is, however, unclear whether these changes occur as a cause of, or as a result of, transcriptional activation. In this paper, we explore the relationship between these two events and collate data available on the phosphorylation state of those transcriptional regulators where the relationship has not been clearly identified.
Published: 2006

8. Eukaryotic transcription factors as direct nutrient sensors

Author: Richard J. Reece and Christopher A. Sellick
Subjects: Saccharomyces cerevisiae Proteins, Proline, Metabolite, RNA polymerase II, Saccharomyces cerevisiae, Biology, Models, Biological, Biochemistry, chemistry.chemical_compound, Transcription (biology), Transcriptional regulation, Nutritional Physiological Phenomena, Molecular Biology, Gene, Genetics, Molecular Structure, General transcription factor, Eukaryotic transcription, Hedgehog signaling pathway, Cell biology, Eukaryotic Cells, chemistry, Trans-Activators, biology.protein, sense organs, Signal Transduction, Transcription Factors
Abstract: The recognition of changes in environmental conditions, and the ability to adapt to these changes, is essential for the viability of cells. There are numerous well-characterized systems by which the presence or absence of an individual metabolite can be recognized by a cell. The recognition of a metabolite is, however, just one step of a process that often results in changes in the expression of sets of genes required to respond to that metabolite. The signalling pathway between metabolite recognition and transcriptional control is often complex. However, recent evidence from yeast suggests that complex signalling pathways might be circumvented via the direct interaction between individual metabolites and regulators of RNA polymerase II transcription.
Published: 2005

9. Molecular Structure of Human Galactokinase

Author: James B. Thoden, Richard J. Reece, Hazel M. Holden, and David J. Timson
Subjects: biology, Chemistry, Stereochemistry, Galactosemia, Active site, Cell Biology, medicine.disease, Biochemistry, Galactokinase, Leloir pathway, chemistry.chemical_compound, Protein structure, Galactose, medicine, biology.protein, Transferase, Binding site, Molecular Biology
Abstract: Galactokinase functions in the Leloir pathway for galactose metabolism by catalyzing the MgATP-dependent phosphorylation of the C-1 hydroxyl group of alpha-D-galactose. The enzyme is known to belong to the GHMP superfamily of small molecule kinases and has attracted significant research attention for well over 40 years. Approximately 20 mutations have now been identified in human galactokinase, which result in the diseased state referred to as Type II galactosemia. Here we report the three-dimensional architecture of human galactokinase with bound alpha-D-galactose and Mg-AMPPNP. The overall fold of the molecule can be described in terms of two domains with the active site wedged between them. The N-terminal domain is dominated by a six-stranded mixed beta-sheet whereas the C-terminal motif contains six alpha-helices and two layers of anti-parallel beta-sheet. Those residues specifically involved in sugar binding include Arg37, Glu43, His44, Asp46, Gly183, Asp186, and Tyr236. The C-1 hydroxyl group of alpha-D-galactose sits within 3.3 A of the gamma-phosphorus of the nucleotide and 3.4 A of the guanidinium group of Arg37. The carboxylate side chain of Asp186 lies within approximately 3.2 A of the C-2 hydroxyl group of alpha-D-galactose and the guanidinium group of Arg37. Both Arg37 and Asp186 are strictly conserved among both prokaryotic and eukaryotic galactokinases. In addition to providing molecular insight into the active site geometry of the enzyme, the model also provides a structural framework upon which to more fully understand the consequences of the those mutations known to give rise to Type II galactosemia.
Published: 2005

10. Molecular Structure of Human Galactose Mutarotase

Author: David J. Timson, James B. Thoden, Richard J. Reece, and Hazel M. Holden
Subjects: Models, Molecular, Protein Conformation, Stereochemistry, Isomerase, Plasma protein binding, Biology, Crystallography, X-Ray, Biochemistry, Catalysis, chemistry.chemical_compound, Protein structure, Humans, Binding site, education, Molecular Biology, education.field_of_study, Binding Sites, Molecular Structure, Lactococcus lactis, Cell Biology, biology.organism_classification, Ligand (biochemistry), chemistry, Galactose, Galactose mutarotase, Carbohydrate Epimerases, Protein Binding
Abstract: Galactose mutarotase catalyzes the conversion of beta-d-galactose to alpha-d-galactose during normal galactose metabolism. The enzyme has been isolated from bacteria, plants, and animals and is present in the cytoplasm of most cells. Here we report the x-ray crystallographic analysis of human galactose mutarotase both in the apoform and complexed with its substrate, beta-d-galactose. The polypeptide chain folds into an intricate array of 29 beta-strands, 25 classical reverse turns, and 2 small alpha-helices. There are two cis-peptide bonds at Arg-78 and Pro-103. The sugar ligand sits in a shallow cleft and is surrounded by Asn-81, Arg-82, His-107, His-176, Asp-243, Gln-279, and Glu-307. Both the side chains of Glu-307 and His-176 are in the proper location to act as a catalytic base and a catalytic acid, respectively. These residues are absolutely conserved among galactose mutarotases. To date, x-ray models for three mutarotases have now been reported, namely that described here and those from Lactococcus lactis and Caenorhabditis elegans. The molecular architectures of these enzymes differ primarily in the loop regions connecting the first two beta-strands. In the human protein, there are six extra residues in the loop compared with the bacterial protein for an approximate longer length of 9 A. In the C. elegans protein, the first 17 residues are missing, thereby reducing the total number of beta-strands by one.
Published: 2004

11. Substrate Specificity and Mechanism from the Structure of Pyrococcus furiosus Galactokinase

Author: Steven E. Glynn, David W. Rice, Corné H. Verhees, Daniel de Geus, A. Hartley, David J. Timson, V.V. Barynin, Richard J. Reece, Patrick J. Baker, Svetlana E. Sedelnikova, and John van der Oost
Subjects: Models, Molecular, Protein Folding, Protein Conformation, Crystallography, X-Ray, Substrate Specificity, chemistry.chemical_compound, Microbiologie, Structural Biology, Catalytic Domain, Transferase, Genetics, biology, Galactosemia, deficiency, molscript, Galactokinase, Galactokinase deficiency, Adenosine Diphosphate, Pyrococcus furiosus, Leloir pathway, Biochemistry, cataracts, Galactosemias, Saccharomyces cerevisiae Proteins, Molecular Sequence Data, Static Electricity, galactose, Saccharomyces cerevisiae, ghmp kinase superfamily, Microbiology, medicine, Humans, Amino Acid Sequence, Molecular Biology, VLAG, Binding Sites, Sequence Homology, Amino Acid, mevalonate kinase, Active site, mutations, medicine.disease, biology.organism_classification, chemistry, Galactose, Mutation, biology.protein, identification, sugar kinases, activation, Transcription Factors
Abstract: Galactokinase (GaIK) catalyses the first step of the Leloir pathway of galactose metabolism, the ATP-dependent phosphorylation of galactose to galactose-l-phosphate. In man, defects in galactose metabolism can result in disorders with severe clinical consequences, and deficiencies in galactokinase have been linked with the development of cataracts within the first few months of life. The crystal structure of GalK from Pyrococcus furiosus in complex with MgADP and galactose has been determined to 2.9 Angstrom resolution to provide insights into the substrate specificity and catalytic mechanism of the enzyme. The structure consists of two domains with the active site in a cleft at the domain interface. Inspection of the substrate binding pocket identifies the amino acid residues involved in galactose and nucleotide binding and points to both structural and mechanistic similarities with other enzymes of the GHMP kinase superfamily to which GalK belongs. Comparison of the sequence of the Gal3p inducer protein, which is related to GalK and which forms part of the transcriptional activation of the GAL gene cluster in the yeast Saccharomyces cerevisiae, has led to an understanding of the molecular basis of galactose and nucleotide recognition. Finally, the structure has enabled us to further our understanding on the functional consequences of mutations in human GalK which cause galactosemia. (C) 2004 Elsevier Ltd. All rights reserved.
Published: 2004

12. Cell Cycle-Regulated Transcription through the FHA Domain of Fkh2p and the Coactivator Ndd1p

Author: Andrew D. Sharrocks, Marco Geymonat, Adonis Spanos, Joanna Boros, Brian A. Morgan, Aline Pic-Taylor, Steven G. Sedgwick, Zoulfia Darieva, and Richard J. Reece
Subjects: Saccharomyces cerevisiae Proteins, Transcription, Genetic, Blotting, Western, Saccharomyces cerevisiae, Cell Cycle Proteins, Cyclin B, Models, Biological, General Biochemistry, Genetics and Molecular Biology, 03 medical and health sciences, 0302 clinical medicine, Transcription (biology), Coactivator, Transcriptional regulation, Phosphorylation, Cell Cycle Protein, Transcription factor, 030304 developmental biology, 0303 health sciences, Agricultural and Biological Sciences(all), biology, Biochemistry, Genetics and Molecular Biology(all), Cell Cycle, Forkhead Transcription Factors, Cell cycle, biology.organism_classification, Molecular biology, Protein Structure, Tertiary, Cell biology, Gene Components, Electrophoresis, Polyacrylamide Gel, General Agricultural and Biological Sciences, CDC28 Protein Kinase, S cerevisiae, 030217 neurology & neurosurgery, Transcription Factors
Abstract: Recent studies in Saccharomyces cerevisiae by using global approaches have significantly enhanced our knowledge of the components involved in the transcriptional regulation of the cell cycle [1–3]. The Mcm1p-Fkh2p complex, in combination with the coactivator Ndd1p, plays an important role in the cell cycle-dependent expression of the CLB2 gene cluster during the G2 and M phases ([4–7]; see [8–10] for reviews). Fkh2p is phosphorylated in a cell cycle-dependent manner, and peak phosphorylation occurs coincidentally with maximal expression of Mcm1p-Fkh2p-dependent gene expression [6]. However, the mechanism by which this complex is activated in a cell cycle-dependent manner is unknown. Here, we demonstrate that the forkhead-associated (FHA) domain of Fkh2p directs cell cycle-regulated transcription and that the activity of this domain is dependent on the coactivator Ndd1p. Ndd1p was found to be phosphorylated in a cell cycle-dependent manner by Cdc28p-Clb2p, and, importantly, this phosphorylation event promotes interactions between Ndd1p and the FHA domain of Fkh2p. Furthermore, mutation of the FHA domain blocks these phosphorylation-dependent interactions and abolishes transcriptional activity. Our data therefore link the transcriptional activity of the FHA domain with cell cycle-dependent phosphorylation of the coactivator Ndd1p and reveal a mechanism that permits precise temporal activation of the Mcm1p-Fkh2p complex.
Published: 2003

13. Identification and characterisation of human aldose 1-epimerase

Author: Richard J. Reece and David J. Timson
Subjects: Mutarotase, Recombinant Fusion Proteins, Molecular Sequence Data, Biophysics, Carbohydrate metabolism, Biology, Biochemistry, Substrate Specificity, Leloir pathway, chemistry.chemical_compound, Structural Biology, Catalytic Domain, Genetics, medicine, Humans, Hexose, Amino Acid Sequence, Cloning, Molecular, education, Molecular Biology, chemistry.chemical_classification, education.field_of_study, Galactosemia, Galactose, Cell Biology, medicine.disease, Molecular biology, Enzyme assay, Kinetics, Glucose, Enzyme, chemistry, Aldose, biology.protein, Galactose mutarotase, Carbohydrate Epimerases, Sequence Alignment
Abstract: Aldose 1-epimerase or mutarotase (EC 5.1.3.3) is a key enzyme of carbohydrate metabolism catalysing the interconversion of the α- and β-anomers of hexose sugars such as glucose and galactose. We identified an open reading frame in the human genome (BC014916) which has high sequence similarity to previously identified bacterial aldose 1-epimerases. This sequence was cloned into a bacterial expression vector, and expressed and purified from this source. Enzyme assays show that the protein has aldose 1-epimerase activity and exhibits a preference for galactose over glucose. Site-directed mutagenesis confirmed the involvement of three residues involved in catalysis and substrate binding.
Published: 2003

14. Functional analysis of disease-causing mutations in human galactokinase

Author: David J. Timson and Richard J. Reece
Subjects: Galactosemias, Mutant, Mutation, Missense, medicine.disease_cause, Biochemistry, Cataract, Galactokinase, chemistry.chemical_compound, Escherichia coli, medicine, Humans, Point Mutation, Cloning, Molecular, chemistry.chemical_classification, Chemistry, Point mutation, Galactosemia, medicine.disease, Recombinant Proteins, Kinetics, Enzyme, Amino Acid Substitution, Product inhibition, Galactose, Mutagenesis, Site-Directed
Abstract: Galactokinase (EC 2.7.1.6) catalyzes the first committed step in the catabolism of galactose. The sugar is phosphorylated at position 1 at the expense of ATP. Lack of fully functional galactokinase is one cause of the inherited disease galactosemia, the main clinical manifestation of which is early onset cataracts. Human galactokinase (GALK1) was expressed in and purified from Escherichia coli. The recombinant enzyme was both soluble and active. Product inhibition studies showed that the most likely kinetic mechanism of the enzyme was an ordered ternary complex one in which ATP is the first substrate to bind. The lack of a solvent kinetic isotope effect suggests that proton transfer is unlikely to be involved in the rate determining step of catalysis. Ten mutations that are known to cause galactosemia were constructed and expressed in E. coli. Of these, five (P28T, V32M, G36R, T288M and A384P) were insoluble following induction and could not be studied further. Four of the remainder (H44Y, R68C, G346S and G349S) were all less active than the wild-type enzyme. One mutant (A198V) had kinetic properties that were essentially wild-type. These results are discussed both in terms of galactokinase structure-function relationships and how these functional changes may relate to the causes of galactosemia.
Published: 2003

15. Accreditation of biology degrees: Who needs it, and why now?

Author: Richard J. Reece
Subjects: ComputingMilieux_COMPUTERSANDEDUCATION, ComputerApplications_COMPUTERSINOTHERSYSTEMS, Engineering ethics, General Biochemistry, Genetics and Molecular Biology, Accreditation
Abstract: Are the skills of a student graduating from a biochemistry programme at university X equivalent to those graduating from the same programme at university Y? Probably not, but this is not an easy question to answer. Although minimum specifications for all biochemistry degree programmes are, in part, outlined by the Quality Assurance Agency (QAA), different universities have different entry requirements, can focus the degree they offer in a variety of different ways depending on their own expertise and can afford their students a whole host of different experiences – not necessarily better or worse experiences, but different. Additionally, of course, not all students are equal. Differences between individuals aside, graduate employers, from both academia and industry, are increasingly keen to know what they are likely to expect from a ‘typical’ graduate from a particular programme. Those of us working in the university sector know only too well how difficult it can be to find a PhD student who can hit the ground running on their project work. Can the accreditation of UK biology degrees help?
Published: 2012

16. Gal3p and Gal1p interact with the transcriptional repressor Gal80p to form a complex of 1:1 stoichiometry

Author: David J. TIMSON, Helen C. ROSS, and Richard J. REECE
Subjects: Cell Biology, Molecular Biology, Biochemistry
Abstract: The genes encoding the enzymes required for galactose metabolism in Saccharomyces cerevisiae are controlled at the level of transcription by a genetic switch consisting of three proteins: a transcriptional activator, Gal4p; a transcriptional repressor, Gal80p; and a ligand sensor, Gal3p. The switch is turned on in the presence of two small molecule ligands, galactose and ATP. Gal3p shows a high degree of sequence identity with Gal1p, the yeast galactokinase. We have mapped the interaction between Gal80p and Gal3p, which only occurs in the presence of both ligands, using protease protection experiments and have shown that this involves amino acid residue 331 of Gal80p. Gel-filtration experiments indicate that Gal3p, or the galactokinase Gal1p, interact directly with Gal80p to form a complex with 1:1 stoichiometry.
Published: 2002

17. Molecular basis of nutrient-controlled gene expression in Saccharomyces cerevisiae

Author: Richard J. Reece
Subjects: Pharmacology, Genetics, Regulation of gene expression, biology, Saccharomyces cerevisiae, Cell Biology, biology.organism_classification, Unicellular organism, Culture Media, Cell biology, Cellular and Molecular Neuroscience, Transcription (biology), Gene Expression Regulation, Fungal, Gene expression, Transcriptional regulation, Molecular Medicine, Molecular Biology, Gene, Transcription factor, Transcription Factors
Abstract: The ability of a unicellular organism to alter patterns of gene expression in response to nutrient availability is essential to its survival in a changing environment. How is the cell able to identify individual metabolites amongst a myriad of other similar molecules, and convert the information of its presence into a concerted change in the transcription of the genes required for the response to that metabolite? There is increasing evidence that the activity of transcription factors can be influenced directly by interaction with metabolites. A variety of mechanisms have been identified by which this type of gene regulation by small molecules can occur.
Published: 2000

18. Activation of Transcription by Metabolic Intermediates of the Pyrimidine Biosynthetic Pathway

Author: Richard J. Reece and Paul J. Flynn
Subjects: Transcriptional Activation, Orotic acid, Saccharomyces cerevisiae Proteins, Pyrimidine, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Biology, Cell Line, Fungal Proteins, chemistry.chemical_compound, Biosynthesis, Aspartic acid, Carbamoyl phosphate, medicine, Animals, Molecular Biology, Transcriptional Regulation, Orotic Acid, chemistry.chemical_classification, Binding Sites, DNA, Cell Biology, Amino acid, DNA-Binding Proteins, Glutamine, Pyrimidines, Biochemistry, chemistry, Pyrimidine metabolism, Transcription Factors, medicine.drug
Abstract: Saccharomyces cerevisiae responds to pyrimidine starvation by increasing the expression of four URA genes, encoding the enzymes of de novo pyrimidine biosynthesis, three- to eightfold. The increase in gene expression is dependent on a transcriptional activator protein, Ppr1p. Here, we investigate the mechanism by which the transcriptional activity of Ppr1p responds to the level of pyrimidine biosynthetic intermediates. We find that purified Ppr1p is unable to promote activation of transcription in an in vitro system. Transcriptional activation by Ppr1p can be observed, however, if either dihydroorotic acid (DHO) or orotic acid (OA) is included in the transcription reactions. The transcriptional activation function and the DHO/OA-responsive element of Ppr1p localize to the carboxyl-terminal 134 amino acids of the protein. Thus, Ppr1p directly senses the level of early pyrimidine biosynthetic intermediates within the cell and activates the expression of genes encoding proteins required later in the pathway. These results are discussed in terms of (i) regulation of the pyrimidine biosynthetic pathway and (ii) a novel mechanism of regulating gene expression. In Saccharomyces cerevisiae, the biosynthesis of pyrimidines involves the de novo synthesis of UMP from glutamine (Fig. 1). Carbamoyl phosphate, derived from glutamine, undergoes a condensation reaction with aspartic acid, resulting in the formation of N-carbamoyl aspartic acid. Both the formation and subsequent condensation of carbamoyl phosphate are performed by Ura2p. The pyrimidine ring of N-carbamoyl aspartic acid is closed by the elimination of water to form dihydroorotic
Published: 1999

19. A transcriptional activating region with two contrasting modes of protein interaction

Author: Richard J. Reece, Aseem Z. Ansari, and Mark Ptashne
Subjects: Transcriptional Activation, chemistry.chemical_classification, Binding Sites, Multidisciplinary, Transcription, Genetic, Activator (genetics), TATA-Box Binding Protein, Membrane Proteins, Saccharomyces cerevisiae, Plasma protein binding, Biological Sciences, Biology, DNA-binding protein, Amino acid, Amino Acid Substitution, Bacterial Proteins, Biochemistry, chemistry, Mutagenesis, Biophysics, Binding site, Protein secondary structure, Protein Binding, Cysteine
Abstract: A C-terminal segment of the yeast activator Gal4 manifests two functions: When tethered to DNA, it elicits gene activation, and it binds the inhibitor Gal80. Here we examine the effects on these two functions of cysteine and proline substitutions. We find that, although certain cysteine substitutions diminish interaction with Gal80, those substitutions have little effect on the activating function in vivo and interaction with TATA box-binding protein (TBP) in vitro . Proline substitutions introduced near residues critical for Gal80 binding abolish that interaction but once again have no effect on the activating function. Crosslinking experiments show that a defined position in the activating peptide is in close proximity to TBP and Gal80 in the two separate reactions and show that binding of the inhibitor blocks binding to TBP. Thus, the same stretch of amino acids are involved in two quite different protein–protein interactions: binding to Gal80, which depends on a precise sequence and the formation of a defined secondary structure, or interactions with the transcriptional machinery in vivo , which are not impaired by perturbations of either sequence or structure.
Published: 1998

20. The yeast galactose genetic switch is mediated by the formation of a Gal4p–Gal80p–Gal3p complex

Author: Richard J. Reece and Adam Platt
Subjects: Transcriptional Activation, Saccharomyces cerevisiae Proteins, Saccharomyces cerevisiae, Repressor, DNA-binding protein, General Biochemistry, Genetics and Molecular Biology, Fungal Proteins, Galactokinase, chemistry.chemical_compound, Adenosine Triphosphate, Gene Expression Regulation, Fungal, gal operon, RNA, Messenger, DNA, Fungal, Molecular Biology, General Immunology and Microbiology, biology, Activator (genetics), General Neuroscience, Galactose, RNA, Fungal, biology.organism_classification, DNA-Binding Proteins, Repressor Proteins, Leloir pathway, chemistry, Biochemistry, Transcription Factors, Research Article
Abstract: Saccharomyces cerevisiae responds to galactose as the sole source of carbon by activating the GAL genes encoding the enzymes of the Leloir pathway. Here, we show in vitro that the switch from repressed to activated gene expression involves the interplay of three proteins [an activator (Gal4p), a repressor (Gal80p) and an inducer (Gal3p)] and two small molecules (galactose and ATP). We also show that the galactose- and ATP-dependent interaction between Gal3p and Gal80p occurs without disruption of the Gal80p-Gal4p interaction. Thus, Gal3p-mediated activation of transcription occurs via the formation of a tripartite protein complex.
Published: 1998

21. Crystal structure of a PUT3–DNA complex reveals a novel mechanism for DMA recognition by a protein containing a Zn2Cys6 binuclear cluster

Author: Ronen Marmorstein, Richard J. Reece, Paul J. Flynn, and Kunchithapadam Swaminathan
Subjects: Models, Molecular, Saccharomyces cerevisiae Proteins, HMG-box, Protein Conformation, Base pair, Molecular Sequence Data, Biology, Crystallography, X-Ray, Biochemistry, Fungal Proteins, Structural Biology, Genetics, Protein–DNA interaction, Amino Acid Sequence, Cysteine, chemistry.chemical_classification, DNA ligase, Binding Sites, DNA clamp, Circular bacterial chromosome, DNA, DNA-binding domain, DNA binding site, Zinc, Crystallography, chemistry, Trans-Activators, Nucleic Acid Conformation, Dimerization, Transcription Factors
Abstract: PUT3 is a member of a family of at least 79 fungal transcription factors that contain a six-cysteine, two-zinc domain called a 'Zn2Cys6 binuclear cluster'. We have determined the crystal structure of the DNA binding region from the PUT3 protein bound to its cognate DNA target. The structure reveals that the PUT3 homodimer is bound asymmetrically to the DNA site. This asymmetry orients a beta-strand from one protein subunit into the minor groove of the DNA resulting in a partial amino acid-base pair intercalation and extensive direct and water-mediated protein interactions with the minor groove of the DNA. These interactions facilitate a sequence dependent kink at the centre of the DNA site and specify the intervening base pairs separating two DNA half-sites that are contacted in the DNA major groove. A comparison with the GAL4-DNA and PPR1-DNA complexes shows how a family of related DNA binding proteins can use a diverse set of mechanisms to discriminate between the base pairs separating conserved DNA half-sites.
Published: 1997

22. Quantitation of putative activator-target affinities predicts transcriptional activating potentials

Author: Richard J. Reece, Y Wu, and Mark Ptashne
Subjects: chemistry.chemical_classification, General Immunology and Microbiology, biology, Activator (genetics), General Neuroscience, DNA-binding protein, Molecular biology, General Biochemistry, Genetics and Molecular Biology, Activating transcription factor 2, Yeast, Cell biology, Amino acid, enzymes and coenzymes (carbohydrates), chemistry, Transcription (biology), biology.protein, Molecular Biology, Transcription factor II B, Peptide sequence
Abstract: We quantitate the 'activating potentials' of deletion and point mutation variants of a 42 amino acid yeast transcriptional activating region excised from the yeast activator GAL4 and, using surface plasmon resonance, we measure the relative affinities of these molecules for a variety of proteins, including plausible target proteins as well as GAL80, a specific inhibitor of GAL4. We find a remarkable correlation between the relative activating potentials of the derivatives and their relative affinities for yeast TBP and for yeast TFIIB; other tested proteins interacted significantly more weakly, if at all. These results provide an especially strong argument that TBP and TFIIB are activating region targets. We also show, using one set of yeast activating region mutants, that activator-target interactions are strongly correlated with the length of the activating region, that the effect of point mutants is highly dependent on the length of the activating region mutated and that, unlike interactions with TBP and TFIIB, interaction with the specific inhibitor GAL80 is destroyed by deletion of certain critical residues in the C-terminal half of the 42 amino acid activating region.
Published: 1996

23. Isolation of compensatory inhibitor domain mutants to novel activation domain variants using the split-ubiquitin screen

Author: Robert N. Campbell, Frederick G. Westhorpe, and Richard J. Reece
Subjects: Saccharomyces cerevisiae Proteins, Mutant, Saccharomyces cerevisiae, Bioengineering, Applied Microbiology and Biotechnology, Biochemistry, Ubiquitin, Transcription (biology), Protein Interaction Mapping, Genetics, Transcriptional regulation, Protein Interaction Domains and Motifs, Single amino acid, Transcription factor, biology, biology.organism_classification, Yeast, Protein Structure, Tertiary, DNA-Binding Proteins, Repressor Proteins, Mutation, biology.protein, Biotechnology, Protein Binding, Transcription Factors
Abstract: The control of transcription factor function plays an important role in the development of many processes in eukaryotes, such as drug resistance in fungi and human tumours undergoing chemotherapy. Detailed molecular mapping of the interactions between transcription factors and their protein partners can give important information about their mechanisms of action and reveal potential therapeutic targets. We devised a genetic screening system for mapping the interaction site between the Saccharomyces cerevisiae transcription factor-inhibitor pair Gal4p and Gal80p. A novel Gal4p activation domain mutant, L868K, was produced, which prevented it interacting with Gal80p. The split-ubiquitin system was used with a mutant GAL80 library in order to screen for compensatory mutants in Gal80p which would restore binding with L868K. Five single amino acid residue compensatory mutations in Gal80p which restored the interaction with Gal4p(L868K) were isolated. These compensatory mutations were specific to L868K as they were unable to restore the interaction with two other Gal4p mutants that were incapable of interacting with Gal80p. Mutations within Gal80p that were capable of compensating for Gal4p (L868K) clustered inside a Gal80p surface cleft, supporting the idea that this area is important for Gal4p binding. Our data suggest a way to generate information about interaction sites that should be applicable to any transcription factor. Copyright © 2011 John Wiley & Sons, Ltd.
Published: 2011

24. Zebrafish ultraviolet visual pigment: absorption spectrum, sequence, and localization

Author: Ferenc I. Harosi, John E. Dowling, Ellen A. Schmitt, Richard J. Reece, and Judith Robinson
Subjects: education.field_of_study, Opsin, Multidisciplinary, genetic structures, biology, Population, Retinal binding, Protein primary structure, Anatomy, biology.organism_classification, Biochemistry, Rhodopsin, Complementary DNA, biology.protein, sense organs, education, Zebrafish, Peptide sequence
Abstract: In many vertebrates, UV-sensitive photoreceptors have been identified by microspectrophotometry and UV-visual sensitivity has been identified by behavioral studies, but as yet no vertebrate UV-sensitive pigment gene has been isolated. We have sequenced a cDNA clone that hybridizes to short single cone cells in the zebrafish (Brachydanio rerio). These cells, which make up 25% of the cone population in zebrafish retinae, are UV-sensitive (lambda max approximately 360 nm). The visual pigment encoded by this gene is unusual in that its amino acid sequence is more homologous to the rod pigment rhodopsin (up to 89%) than to other cone pigments (35-83%). Like all other vertebrate visual pigments, it contains a lysine residue at position 296, the presumptive retinal binding site, and a glutamate residue at position 113. However, it is unique in possessing a lysine residue at position 126, which may account for the UV-sensitivity of the pigment.
Published: 1993

25. Mutation of a Phosphorylatable Residue in Put3p Affects the Magnitude of Rapamycin-induced PUT1 Activation in a Gat1p-dependent Manner*

Author: Michael K. Leverentz, Robert N. Campbell, Anthony D. Whetton, Richard J. Reece, and Yvonne Connolly
Subjects: Antifungal Agents, Saccharomyces cerevisiae Proteins, Proline, Transcription, Genetic, Saccharomyces cerevisiae, Biology, Biochemistry, GATA Transcription Factors, Gene Expression Regulation, Fungal, Proline Oxidase, Transcription, Chromatin, and Epigenetics, Phosphorylation, Molecular Biology, Transcription factor, chemistry.chemical_classification, Sirolimus, Proline oxidase, Cell Biology, biology.organism_classification, Amino acid, Glutamine, chemistry, Mutation, GATA transcription factor, Transcription Factors
Abstract: Saccharomyces cerevisiae can utilize high quality (e.g. glutamine and ammonia) as well as low quality (e.g. gamma-amino butyric acid and proline) nitrogen sources. The transcriptional activator Put3p allows yeast cells to utilize proline as a nitrogen source through expression of the PUT1 and PUT2 genes. Put3p activates high level transcription of these genes by binding proline directly. However, Put3p also responds to other lower quality nitrogen sources. As nitrogen quality decreases, Put3p exhibits an increase in phosphorylation concurrent with an increase in PUT gene expression. The proline-independent activation of the PUT genes requires both Put3p and the positively acting GATA factors, Gln3p and Gat1p. Conversely, the phosphorylation of Put3p is not dependent on GATA factor activity. Here, we find that the mutation of Put3p at amino acid Tyr-788 modulates the proline-independent activation of PUT1 through Gat1p. The phosphorylation of Put3p appears to influence the association of Gat1p, but not Gln3p, to the PUT1 promoter. Combined, our findings suggest that this may represent a mechanism through which yeast cells rapidly adapt to use proline as a nitrogen source under nitrogen limiting conditions.
Published: 2009

26. Giant Cell Thyroiditis

Author: David J. Timson, Richard J. Reece, James B. Thoden, Hazel M. Holden, Andrea L. Utz, Beverly M. K. Biller, Eugen-Matthias Strehle, Markus Böhm, Thomas A. Luger, Alexander K. C. Leung, Andrew L. Wong, Markus G. Donner, Dieter Häussinger, Nirmal S. Mann, Marcus Schmitt, William Lane M. Robson, Manisha Balwani, Ainu Prakash-Cheng, Robert J. Desnick, Holger Lerche, Ingrid E. Scheffer, Samuel F. Berkovic, Brigitte M. Lobnig, Peter L. M. Jansen, Siegfried Waldegger, Florian Lang, Hugo ten Cate, Hagen Thieme, Michael Weller, Bärbel Schütte, Ronnie Fass, Hideki Kato, Masaomi Nangaku, Anthony Chang, Pradeep V. Kadambi, Jessy J. Alexander, Pierre Ronco, Hanna Debiec, Christian Hugo, John-John B. Schnog, Victor E. A. Gerdes, Jean Francis, David S. Geller, Knut Brockmann, Dong Wang, Darryl C. Vivo, Stefan Kölker, Elardus Erasmus, Lodewyk J. Mienie, John Vissing, Arnold Reuser, Catherine E. Correia, David A. Weinstein, Joseph I. Wolfsdorf, Yoon S. Shin, Reinout P. Hesselink, Maarten R. Drost, Anton J. M. Wagenmakers, Ger J. Vusse, Stefan Kiechl, Jonas Denecke, Ute Schepers, Thomas Kolter, Konrad Sandhoff, Dianna C. Martin, Barbara L. Triggs-Raine, Seda Sancak, Ralf Paschke, Dorin-Bogdan Borza, Sonja Ständer, Heiko Traupe, Michael A. Becker, Hanneke M. Straaten, Leo F. Verdonck, Hugo Ten Cate, Martin Mempel, Dietrich Abeck, Ismat Ghanem, Samer El Hage, Johannes G. Bode, Thomas A. Fleisher, Steven M. Holland, Bennett Myers, David Herrmann, Zaki Kraiem, Yaron Tomer, Terry F. Davies, James G. White, Sylvia Stöckler-Ipsiroglu, Guido Stoll, Klaus V. Toyka, Valéria Lamounier-Zepter, and Klaus Ruether
Published: 2009

27. Glycogenosis Type IX

Author: David J. Timson, Richard J. Reece, James B. Thoden, Hazel M. Holden, Andrea L. Utz, Beverly M. K. Biller, Eugen-Matthias Strehle, Markus Böhm, Thomas A. Luger, Alexander K. C. Leung, Andrew L. Wong, Markus G. Donner, Dieter Häussinger, Nirmal S. Mann, Marcus Schmitt, William Lane M. Robson, Manisha Balwani, Ainu Prakash-Cheng, Robert J. Desnick, Holger Lerche, Ingrid E. Scheffer, Samuel F. Berkovic, Brigitte M. Lobnig, Peter L. M. Jansen, Siegfried Waldegger, Florian Lang, Hugo ten Cate, Hagen Thieme, Michael Weller, Bärbel Schütte, Ronnie Fass, Hideki Kato, Masaomi Nangaku, Anthony Chang, Pradeep V. Kadambi, Jessy J. Alexander, Pierre Ronco, Hanna Debiec, Christian Hugo, John-John B. Schnog, Victor E. A. Gerdes, Jean Francis, David S. Geller, Knut Brockmann, Dong Wang, Darryl C. Vivo, Stefan Kölker, Elardus Erasmus, Lodewyk J. Mienie, John Vissing, Arnold Reuser, Catherine E. Correia, David A. Weinstein, Joseph I. Wolfsdorf, Yoon S. Shin, Reinout P. Hesselink, Maarten R. Drost, Anton J. M. Wagenmakers, Ger J. Vusse, Stefan Kiechl, Jonas Denecke, Ute Schepers, Thomas Kolter, Konrad Sandhoff, Dianna C. Martin, Barbara L. Triggs-Raine, Seda Sancak, Ralf Paschke, Dorin-Bogdan Borza, Sonja Ständer, Heiko Traupe, Michael A. Becker, Hanneke M. Straaten, Leo F. Verdonck, Hugo Ten Cate, Martin Mempel, Dietrich Abeck, Ismat Ghanem, Samer El Hage, Johannes G. Bode, Thomas A. Fleisher, Steven M. Holland, Bennett Myers, David Herrmann, Zaki Kraiem, Yaron Tomer, Terry F. Davies, James G. White, Sylvia Stöckler-Ipsiroglu, Guido Stoll, Klaus V. Toyka, Valéria Lamounier-Zepter, and Klaus Ruether
Published: 2009

28. Glomus Tumors

Author: David J. Timson, Richard J. Reece, James B. Thoden, Hazel M. Holden, Andrea L. Utz, Beverly M. K. Biller, Eugen-Matthias Strehle, Markus Böhm, Thomas A. Luger, Alexander K. C. Leung, Andrew L. Wong, Markus G. Donner, Dieter Häussinger, Nirmal S. Mann, Marcus Schmitt, William Lane M. Robson, Manisha Balwani, Ainu Prakash-Cheng, Robert J. Desnick, Holger Lerche, Ingrid E. Scheffer, Samuel F. Berkovic, Brigitte M. Lobnig, Peter L. M. Jansen, Siegfried Waldegger, Florian Lang, Hugo ten Cate, Hagen Thieme, Michael Weller, Bärbel Schütte, Ronnie Fass, Hideki Kato, Masaomi Nangaku, Anthony Chang, Pradeep V. Kadambi, Jessy J. Alexander, Pierre Ronco, Hanna Debiec, Christian Hugo, John-John B. Schnog, Victor E. A. Gerdes, Jean Francis, David S. Geller, Knut Brockmann, Dong Wang, Darryl C. Vivo, Stefan Kölker, Elardus Erasmus, Lodewyk J. Mienie, John Vissing, Arnold Reuser, Catherine E. Correia, David A. Weinstein, Joseph I. Wolfsdorf, Yoon S. Shin, Reinout P. Hesselink, Maarten R. Drost, Anton J. M. Wagenmakers, Ger J. Vusse, Stefan Kiechl, Jonas Denecke, Ute Schepers, Thomas Kolter, Konrad Sandhoff, Dianna C. Martin, Barbara L. Triggs-Raine, Seda Sancak, Ralf Paschke, Dorin-Bogdan Borza, Sonja Ständer, Heiko Traupe, Michael A. Becker, Hanneke M. Straaten, Leo F. Verdonck, Hugo Ten Cate, Martin Mempel, Dietrich Abeck, Ismat Ghanem, Samer El Hage, Johannes G. Bode, Thomas A. Fleisher, Steven M. Holland, Bennett Myers, David Herrmann, Zaki Kraiem, Yaron Tomer, Terry F. Davies, James G. White, Sylvia Stöckler-Ipsiroglu, Guido Stoll, Klaus V. Toyka, Valéria Lamounier-Zepter, and Klaus Ruether
Published: 2009

29. Granular Nuclear Inclusion Body Disease

Author: David J. Timson, Richard J. Reece, James B. Thoden, Hazel M. Holden, Andrea L. Utz, Beverly M. K. Biller, Eugen-Matthias Strehle, Markus Böhm, Thomas A. Luger, Alexander K. C. Leung, Andrew L. Wong, Markus G. Donner, Dieter Häussinger, Nirmal S. Mann, Marcus Schmitt, William Lane M. Robson, Manisha Balwani, Ainu Prakash-Cheng, Robert J. Desnick, Holger Lerche, Ingrid E. Scheffer, Samuel F. Berkovic, Brigitte M. Lobnig, Peter L. M. Jansen, Siegfried Waldegger, Florian Lang, Hugo ten Cate, Hagen Thieme, Michael Weller, Bärbel Schütte, Ronnie Fass, Hideki Kato, Masaomi Nangaku, Anthony Chang, Pradeep V. Kadambi, Jessy J. Alexander, Pierre Ronco, Hanna Debiec, Christian Hugo, John-John B. Schnog, Victor E. A. Gerdes, Jean Francis, David S. Geller, Knut Brockmann, Dong Wang, Darryl C. Vivo, Stefan Kölker, Elardus Erasmus, Lodewyk J. Mienie, John Vissing, Arnold Reuser, Catherine E. Correia, David A. Weinstein, Joseph I. Wolfsdorf, Yoon S. Shin, Reinout P. Hesselink, Maarten R. Drost, Anton J. M. Wagenmakers, Ger J. Vusse, Stefan Kiechl, Jonas Denecke, Ute Schepers, Thomas Kolter, Konrad Sandhoff, Dianna C. Martin, Barbara L. Triggs-Raine, Seda Sancak, Ralf Paschke, Dorin-Bogdan Borza, Sonja Ständer, Heiko Traupe, Michael A. Becker, Hanneke M. Straaten, Leo F. Verdonck, Hugo Ten Cate, Martin Mempel, Dietrich Abeck, Ismat Ghanem, Samer El Hage, Johannes G. Bode, Thomas A. Fleisher, Steven M. Holland, Bennett Myers, David Herrmann, Zaki Kraiem, Yaron Tomer, Terry F. Davies, James G. White, Sylvia Stöckler-Ipsiroglu, Guido Stoll, Klaus V. Toyka, Valéria Lamounier-Zepter, and Klaus Ruether
Published: 2009

30. Gangliosidosis, Pseudo AB Variant

Author: David J. Timson, Richard J. Reece, James B. Thoden, Hazel M. Holden, Andrea L. Utz, Beverly M. K. Biller, Eugen-Matthias Strehle, Markus Böhm, Thomas A. Luger, Alexander K. C. Leung, Andrew L. Wong, Markus G. Donner, Dieter Häussinger, Nirmal S. Mann, Marcus Schmitt, William Lane M. Robson, Manisha Balwani, Ainu Prakash-Cheng, Robert J. Desnick, Holger Lerche, Ingrid E. Scheffer, Samuel F. Berkovic, Brigitte M. Lobnig, Peter L. M. Jansen, Siegfried Waldegger, Florian Lang, Hugo ten Cate, Hagen Thieme, Michael Weller, Bärbel Schütte, Ronnie Fass, Hideki Kato, Masaomi Nangaku, Anthony Chang, Pradeep V. Kadambi, Jessy J. Alexander, Pierre Ronco, Hanna Debiec, Christian Hugo, John-John B. Schnog, Victor E. A. Gerdes, Jean Francis, David S. Geller, Knut Brockmann, Dong Wang, Darryl C. Vivo, Stefan Kölker, Elardus Erasmus, Lodewyk J. Mienie, John Vissing, Arnold Reuser, Catherine E. Correia, David A. Weinstein, Joseph I. Wolfsdorf, Yoon S. Shin, Reinout P. Hesselink, Maarten R. Drost, Anton J. M. Wagenmakers, Ger J. Vusse, Stefan Kiechl, Jonas Denecke, Ute Schepers, Thomas Kolter, Konrad Sandhoff, Dianna C. Martin, Barbara L. Triggs-Raine, Seda Sancak, Ralf Paschke, Dorin-Bogdan Borza, Sonja Ständer, Heiko Traupe, Michael A. Becker, Hanneke M. Straaten, Leo F. Verdonck, Hugo Ten Cate, Martin Mempel, Dietrich Abeck, Ismat Ghanem, Samer El Hage, Johannes G. Bode, Thomas A. Fleisher, Steven M. Holland, Bennett Myers, David Herrmann, Zaki Kraiem, Yaron Tomer, Terry F. Davies, James G. White, Sylvia Stöckler-Ipsiroglu, Guido Stoll, Klaus V. Toyka, Valéria Lamounier-Zepter, and Klaus Ruether
Published: 2009

31. Gaucher Activator Deficiency

Author: David J. Timson, Richard J. Reece, James B. Thoden, Hazel M. Holden, Andrea L. Utz, Beverly M. K. Biller, Eugen-Matthias Strehle, Markus Böhm, Thomas A. Luger, Alexander K. C. Leung, Andrew L. Wong, Markus G. Donner, Dieter Häussinger, Nirmal S. Mann, Marcus Schmitt, William Lane M. Robson, Manisha Balwani, Ainu Prakash-Cheng, Robert J. Desnick, Holger Lerche, Ingrid E. Scheffer, Samuel F. Berkovic, Brigitte M. Lobnig, Peter L. M. Jansen, Siegfried Waldegger, Florian Lang, Hugo ten Cate, Hagen Thieme, Michael Weller, Bärbel Schütte, Ronnie Fass, Hideki Kato, Masaomi Nangaku, Anthony Chang, Pradeep V. Kadambi, Jessy J. Alexander, Pierre Ronco, Hanna Debiec, Christian Hugo, John-John B. Schnog, Victor E. A. Gerdes, Jean Francis, David S. Geller, Knut Brockmann, Dong Wang, Darryl C. Vivo, Stefan Kölker, Elardus Erasmus, Lodewyk J. Mienie, John Vissing, Arnold Reuser, Catherine E. Correia, David A. Weinstein, Joseph I. Wolfsdorf, Yoon S. Shin, Reinout P. Hesselink, Maarten R. Drost, Anton J. M. Wagenmakers, Ger J. Vusse, Stefan Kiechl, Jonas Denecke, Ute Schepers, Thomas Kolter, Konrad Sandhoff, Dianna C. Martin, Barbara L. Triggs-Raine, Seda Sancak, Ralf Paschke, Dorin-Bogdan Borza, Sonja Ständer, Heiko Traupe, Michael A. Becker, Hanneke M. Straaten, Leo F. Verdonck, Hugo Ten Cate, Martin Mempel, Dietrich Abeck, Ismat Ghanem, Samer El Hage, Johannes G. Bode, Thomas A. Fleisher, Steven M. Holland, Bennett Myers, David Herrmann, Zaki Kraiem, Yaron Tomer, Terry F. Davies, James G. White, Sylvia Stöckler-Ipsiroglu, Guido Stoll, Klaus V. Toyka, Valéria Lamounier-Zepter, and Klaus Ruether
Published: 2009

32. Gorlin-Goltz Syndrome

Author: David J. Timson, Richard J. Reece, James B. Thoden, Hazel M. Holden, Andrea L. Utz, Beverly M. K. Biller, Eugen-Matthias Strehle, Markus Böhm, Thomas A. Luger, Alexander K. C. Leung, Andrew L. Wong, Markus G. Donner, Dieter Häussinger, Nirmal S. Mann, Marcus Schmitt, William Lane M. Robson, Manisha Balwani, Ainu Prakash-Cheng, Robert J. Desnick, Holger Lerche, Ingrid E. Scheffer, Samuel F. Berkovic, Brigitte M. Lobnig, Peter L. M. Jansen, Siegfried Waldegger, Florian Lang, Hugo ten Cate, Hagen Thieme, Michael Weller, Bärbel Schütte, Ronnie Fass, Hideki Kato, Masaomi Nangaku, Anthony Chang, Pradeep V. Kadambi, Jessy J. Alexander, Pierre Ronco, Hanna Debiec, Christian Hugo, John-John B. Schnog, Victor E. A. Gerdes, Jean Francis, David S. Geller, Knut Brockmann, Dong Wang, Darryl C. Vivo, Stefan Kölker, Elardus Erasmus, Lodewyk J. Mienie, John Vissing, Arnold Reuser, Catherine E. Correia, David A. Weinstein, Joseph I. Wolfsdorf, Yoon S. Shin, Reinout P. Hesselink, Maarten R. Drost, Anton J. M. Wagenmakers, Ger J. Vusse, Stefan Kiechl, Jonas Denecke, Ute Schepers, Thomas Kolter, Konrad Sandhoff, Dianna C. Martin, Barbara L. Triggs-Raine, Seda Sancak, Ralf Paschke, Dorin-Bogdan Borza, Sonja Ständer, Heiko Traupe, Michael A. Becker, Hanneke M. Straaten, Leo F. Verdonck, Hugo Ten Cate, Martin Mempel, Dietrich Abeck, Ismat Ghanem, Samer El Hage, Johannes G. Bode, Thomas A. Fleisher, Steven M. Holland, Bennett Myers, David Herrmann, Zaki Kraiem, Yaron Tomer, Terry F. Davies, James G. White, Sylvia Stöckler-Ipsiroglu, Guido Stoll, Klaus V. Toyka, Valéria Lamounier-Zepter, and Klaus Ruether
Published: 2009

33. Glomerulonephritis, Membranous

Author: David J. Timson, Richard J. Reece, James B. Thoden, Hazel M. Holden, Andrea L. Utz, Beverly M. K. Biller, Eugen-Matthias Strehle, Markus Böhm, Thomas A. Luger, Alexander K. C. Leung, Andrew L. Wong, Markus G. Donner, Dieter Häussinger, Nirmal S. Mann, Marcus Schmitt, William Lane M. Robson, Manisha Balwani, Ainu Prakash-Cheng, Robert J. Desnick, Holger Lerche, Ingrid E. Scheffer, Samuel F. Berkovic, Brigitte M. Lobnig, Peter L. M. Jansen, Siegfried Waldegger, Florian Lang, Hugo ten Cate, Hagen Thieme, Michael Weller, Bärbel Schütte, Ronnie Fass, Hideki Kato, Masaomi Nangaku, Anthony Chang, Pradeep V. Kadambi, Jessy J. Alexander, Pierre Ronco, Hanna Debiec, Christian Hugo, John-John B. Schnog, Victor E. A. Gerdes, Jean Francis, David S. Geller, Knut Brockmann, Dong Wang, Darryl C. Vivo, Stefan Kölker, Elardus Erasmus, Lodewyk J. Mienie, John Vissing, Arnold Reuser, Catherine E. Correia, David A. Weinstein, Joseph I. Wolfsdorf, Yoon S. Shin, Reinout P. Hesselink, Maarten R. Drost, Anton J. M. Wagenmakers, Ger J. Vusse, Stefan Kiechl, Jonas Denecke, Ute Schepers, Thomas Kolter, Konrad Sandhoff, Dianna C. Martin, Barbara L. Triggs-Raine, Seda Sancak, Ralf Paschke, Dorin-Bogdan Borza, Sonja Ständer, Heiko Traupe, Michael A. Becker, Hanneke M. Straaten, Leo F. Verdonck, Hugo Ten Cate, Martin Mempel, Dietrich Abeck, Ismat Ghanem, Samer El Hage, Johannes G. Bode, Thomas A. Fleisher, Steven M. Holland, Bennett Myers, David Herrmann, Zaki Kraiem, Yaron Tomer, Terry F. Davies, James G. White, Sylvia Stöckler-Ipsiroglu, Guido Stoll, Klaus V. Toyka, Valéria Lamounier-Zepter, and Klaus Ruether
Published: 2009

34. Glycoprotein Ib, Platelet, Deficiency of

Author: David J. Timson, Richard J. Reece, James B. Thoden, Hazel M. Holden, Andrea L. Utz, Beverly M. K. Biller, Eugen-Matthias Strehle, Markus Böhm, Thomas A. Luger, Alexander K. C. Leung, Andrew L. Wong, Markus G. Donner, Dieter Häussinger, Nirmal S. Mann, Marcus Schmitt, William Lane M. Robson, Manisha Balwani, Ainu Prakash-Cheng, Robert J. Desnick, Holger Lerche, Ingrid E. Scheffer, Samuel F. Berkovic, Brigitte M. Lobnig, Peter L. M. Jansen, Siegfried Waldegger, Florian Lang, Hugo ten Cate, Hagen Thieme, Michael Weller, Bärbel Schütte, Ronnie Fass, Hideki Kato, Masaomi Nangaku, Anthony Chang, Pradeep V. Kadambi, Jessy J. Alexander, Pierre Ronco, Hanna Debiec, Christian Hugo, John-John B. Schnog, Victor E. A. Gerdes, Jean Francis, David S. Geller, Knut Brockmann, Dong Wang, Darryl C. Vivo, Stefan Kölker, Elardus Erasmus, Lodewyk J. Mienie, John Vissing, Arnold Reuser, Catherine E. Correia, David A. Weinstein, Joseph I. Wolfsdorf, Yoon S. Shin, Reinout P. Hesselink, Maarten R. Drost, Anton J. M. Wagenmakers, Ger J. Vusse, Stefan Kiechl, Jonas Denecke, Ute Schepers, Thomas Kolter, Konrad Sandhoff, Dianna C. Martin, Barbara L. Triggs-Raine, Seda Sancak, Ralf Paschke, Dorin-Bogdan Borza, Sonja Ständer, Heiko Traupe, Michael A. Becker, Hanneke M. Straaten, Leo F. Verdonck, Hugo Ten Cate, Martin Mempel, Dietrich Abeck, Ismat Ghanem, Samer El Hage, Johannes G. Bode, Thomas A. Fleisher, Steven M. Holland, Bennett Myers, David Herrmann, Zaki Kraiem, Yaron Tomer, Terry F. Davies, James G. White, Sylvia Stöckler-Ipsiroglu, Guido Stoll, Klaus V. Toyka, Valéria Lamounier-Zepter, and Klaus Ruether
Published: 2009

35. Gigantism

Author: David J. Timson, Richard J. Reece, James B. Thoden, Hazel M. Holden, Andrea L. Utz, Beverly M. K. Biller, Eugen-Matthias Strehle, Markus Böhm, Thomas A. Luger, Alexander K. C. Leung, Andrew L. Wong, Markus G. Donner, Dieter Häussinger, Nirmal S. Mann, Marcus Schmitt, William Lane M. Robson, Manisha Balwani, Ainu Prakash-Cheng, Robert J. Desnick, Holger Lerche, Ingrid E. Scheffer, Samuel F. Berkovic, Brigitte M. Lobnig, Peter L. M. Jansen, Siegfried Waldegger, Florian Lang, Hugo ten Cate, Hagen Thieme, Michael Weller, Bärbel Schütte, Ronnie Fass, Hideki Kato, Masaomi Nangaku, Anthony Chang, Pradeep V. Kadambi, Jessy J. Alexander, Pierre Ronco, Hanna Debiec, Christian Hugo, John-John B. Schnog, Victor E. A. Gerdes, Jean Francis, David S. Geller, Knut Brockmann, Dong Wang, Darryl C. Vivo, Stefan Kölker, Elardus Erasmus, Lodewyk J. Mienie, John Vissing, Arnold Reuser, Catherine E. Correia, David A. Weinstein, Joseph I. Wolfsdorf, Yoon S. Shin, Reinout P. Hesselink, Maarten R. Drost, Anton J. M. Wagenmakers, Ger J. Vusse, Stefan Kiechl, Jonas Denecke, Ute Schepers, Thomas Kolter, Konrad Sandhoff, Dianna C. Martin, Barbara L. Triggs-Raine, Seda Sancak, Ralf Paschke, Dorin-Bogdan Borza, Sonja Ständer, Heiko Traupe, Michael A. Becker, Hanneke M. Straaten, Leo F. Verdonck, Hugo Ten Cate, Martin Mempel, Dietrich Abeck, Ismat Ghanem, Samer El Hage, Johannes G. Bode, Thomas A. Fleisher, Steven M. Holland, Bennett Myers, David Herrmann, Zaki Kraiem, Yaron Tomer, Terry F. Davies, James G. White, Sylvia Stöckler-Ipsiroglu, Guido Stoll, Klaus V. Toyka, Valéria Lamounier-Zepter, and Klaus Ruether
Published: 2009

36. Glycogen Storage Disease Type II

Author: David J. Timson, Richard J. Reece, James B. Thoden, Hazel M. Holden, Andrea L. Utz, Beverly M. K. Biller, Eugen-Matthias Strehle, Markus Böhm, Thomas A. Luger, Alexander K. C. Leung, Andrew L. Wong, Markus G. Donner, Dieter Häussinger, Nirmal S. Mann, Marcus Schmitt, William Lane M. Robson, Manisha Balwani, Ainu Prakash-Cheng, Robert J. Desnick, Holger Lerche, Ingrid E. Scheffer, Samuel F. Berkovic, Brigitte M. Lobnig, Peter L. M. Jansen, Siegfried Waldegger, Florian Lang, Hugo ten Cate, Hagen Thieme, Michael Weller, Bärbel Schütte, Ronnie Fass, Hideki Kato, Masaomi Nangaku, Anthony Chang, Pradeep V. Kadambi, Jessy J. Alexander, Pierre Ronco, Hanna Debiec, Christian Hugo, John-John B. Schnog, Victor E. A. Gerdes, Jean Francis, David S. Geller, Knut Brockmann, Dong Wang, Darryl C. Vivo, Stefan Kölker, Elardus Erasmus, Lodewyk J. Mienie, John Vissing, Arnold Reuser, Catherine E. Correia, David A. Weinstein, Joseph I. Wolfsdorf, Yoon S. Shin, Reinout P. Hesselink, Maarten R. Drost, Anton J. M. Wagenmakers, Ger J. Vusse, Stefan Kiechl, Jonas Denecke, Ute Schepers, Thomas Kolter, Konrad Sandhoff, Dianna C. Martin, Barbara L. Triggs-Raine, Seda Sancak, Ralf Paschke, Dorin-Bogdan Borza, Sonja Ständer, Heiko Traupe, Michael A. Becker, Hanneke M. Straaten, Leo F. Verdonck, Hugo Ten Cate, Martin Mempel, Dietrich Abeck, Ismat Ghanem, Samer El Hage, Johannes G. Bode, Thomas A. Fleisher, Steven M. Holland, Bennett Myers, David Herrmann, Zaki Kraiem, Yaron Tomer, Terry F. Davies, James G. White, Sylvia Stöckler-Ipsiroglu, Guido Stoll, Klaus V. Toyka, Valéria Lamounier-Zepter, and Klaus Ruether
Published: 2009

37. Glycogen Branching Enzyme Deficiency

Author: David J. Timson, Richard J. Reece, James B. Thoden, Hazel M. Holden, Andrea L. Utz, Beverly M. K. Biller, Eugen-Matthias Strehle, Markus Böhm, Thomas A. Luger, Alexander K. C. Leung, Andrew L. Wong, Markus G. Donner, Dieter Häussinger, Nirmal S. Mann, Marcus Schmitt, William Lane M. Robson, Manisha Balwani, Ainu Prakash-Cheng, Robert J. Desnick, Holger Lerche, Ingrid E. Scheffer, Samuel F. Berkovic, Brigitte M. Lobnig, Peter L. M. Jansen, Siegfried Waldegger, Florian Lang, Hugo ten Cate, Hagen Thieme, Michael Weller, Bärbel Schütte, Ronnie Fass, Hideki Kato, Masaomi Nangaku, Anthony Chang, Pradeep V. Kadambi, Jessy J. Alexander, Pierre Ronco, Hanna Debiec, Christian Hugo, John-John B. Schnog, Victor E. A. Gerdes, Jean Francis, David S. Geller, Knut Brockmann, Dong Wang, Darryl C. Vivo, Stefan Kölker, Elardus Erasmus, Lodewyk J. Mienie, John Vissing, Arnold Reuser, Catherine E. Correia, David A. Weinstein, Joseph I. Wolfsdorf, Yoon S. Shin, Reinout P. Hesselink, Maarten R. Drost, Anton J. M. Wagenmakers, Ger J. Vusse, Stefan Kiechl, Jonas Denecke, Ute Schepers, Thomas Kolter, Konrad Sandhoff, Dianna C. Martin, Barbara L. Triggs-Raine, Seda Sancak, Ralf Paschke, Dorin-Bogdan Borza, Sonja Ständer, Heiko Traupe, Michael A. Becker, Hanneke M. Straaten, Leo F. Verdonck, Hugo Ten Cate, Martin Mempel, Dietrich Abeck, Ismat Ghanem, Samer El Hage, Johannes G. Bode, Thomas A. Fleisher, Steven M. Holland, Bennett Myers, David Herrmann, Zaki Kraiem, Yaron Tomer, Terry F. Davies, James G. White, Sylvia Stöckler-Ipsiroglu, Guido Stoll, Klaus V. Toyka, Valéria Lamounier-Zepter, and Klaus Ruether
Published: 2009

38. Generalized Acantholytic Epidermal Nevus

Author: David J. Timson, Richard J. Reece, James B. Thoden, Hazel M. Holden, Andrea L. Utz, Beverly M. K. Biller, Eugen-Matthias Strehle, Markus Böhm, Thomas A. Luger, Alexander K. C. Leung, Andrew L. Wong, Markus G. Donner, Dieter Häussinger, Nirmal S. Mann, Marcus Schmitt, William Lane M. Robson, Manisha Balwani, Ainu Prakash-Cheng, Robert J. Desnick, Holger Lerche, Ingrid E. Scheffer, Samuel F. Berkovic, Brigitte M. Lobnig, Peter L. M. Jansen, Siegfried Waldegger, Florian Lang, Hugo ten Cate, Hagen Thieme, Michael Weller, Bärbel Schütte, Ronnie Fass, Hideki Kato, Masaomi Nangaku, Anthony Chang, Pradeep V. Kadambi, Jessy J. Alexander, Pierre Ronco, Hanna Debiec, Christian Hugo, John-John B. Schnog, Victor E. A. Gerdes, Jean Francis, David S. Geller, Knut Brockmann, Dong Wang, Darryl C. Vivo, Stefan Kölker, Elardus Erasmus, Lodewyk J. Mienie, John Vissing, Arnold Reuser, Catherine E. Correia, David A. Weinstein, Joseph I. Wolfsdorf, Yoon S. Shin, Reinout P. Hesselink, Maarten R. Drost, Anton J. M. Wagenmakers, Ger J. Vusse, Stefan Kiechl, Jonas Denecke, Ute Schepers, Thomas Kolter, Konrad Sandhoff, Dianna C. Martin, Barbara L. Triggs-Raine, Seda Sancak, Ralf Paschke, Dorin-Bogdan Borza, Sonja Ständer, Heiko Traupe, Michael A. Becker, Hanneke M. Straaten, Leo F. Verdonck, Hugo Ten Cate, Martin Mempel, Dietrich Abeck, Ismat Ghanem, Samer El Hage, Johannes G. Bode, Thomas A. Fleisher, Steven M. Holland, Bennett Myers, David Herrmann, Zaki Kraiem, Yaron Tomer, Terry F. Davies, James G. White, Sylvia Stöckler-Ipsiroglu, Guido Stoll, Klaus V. Toyka, Valéria Lamounier-Zepter, and Klaus Ruether
Published: 2009

39. 1,4-α-D-Glucan 6-α-D-[1,4-D-Glucano] Transferase Deficiency

Author: David J. Timson, Richard J. Reece, James B. Thoden, Hazel M. Holden, Andrea L. Utz, Beverly M. K. Biller, Eugen-Matthias Strehle, Markus Böhm, Thomas A. Luger, Alexander K. C. Leung, Andrew L. Wong, Markus G. Donner, Dieter Häussinger, Nirmal S. Mann, Marcus Schmitt, William Lane M. Robson, Manisha Balwani, Ainu Prakash-Cheng, Robert J. Desnick, Holger Lerche, Ingrid E. Scheffer, Samuel F. Berkovic, Brigitte M. Lobnig, Peter L. M. Jansen, Siegfried Waldegger, Florian Lang, Hugo ten Cate, Hagen Thieme, Michael Weller, Bärbel Schütte, Ronnie Fass, Hideki Kato, Masaomi Nangaku, Anthony Chang, Pradeep V. Kadambi, Jessy J. Alexander, Pierre Ronco, Hanna Debiec, Christian Hugo, John-John B. Schnog, Victor E. A. Gerdes, Jean Francis, David S. Geller, Knut Brockmann, Dong Wang, Darryl C. Vivo, Stefan Kölker, Elardus Erasmus, Lodewyk J. Mienie, John Vissing, Arnold Reuser, Catherine E. Correia, David A. Weinstein, Joseph I. Wolfsdorf, Yoon S. Shin, Reinout P. Hesselink, Maarten R. Drost, Anton J. M. Wagenmakers, Ger J. Vusse, Stefan Kiechl, Jonas Denecke, Ute Schepers, Thomas Kolter, Konrad Sandhoff, Dianna C. Martin, Barbara L. Triggs-Raine, Seda Sancak, Ralf Paschke, Dorin-Bogdan Borza, Sonja Ständer, Heiko Traupe, Michael A. Becker, Hanneke M. Straaten, Leo F. Verdonck, Hugo Ten Cate, Martin Mempel, Dietrich Abeck, Ismat Ghanem, Samer El Hage, Johannes G. Bode, Thomas A. Fleisher, Steven M. Holland, Bennett Myers, David Herrmann, Zaki Kraiem, Yaron Tomer, Terry F. Davies, James G. White, Sylvia Stöckler-Ipsiroglu, Guido Stoll, Klaus V. Toyka, Valéria Lamounier-Zepter, and Klaus Ruether
Published: 2009

40. Genetic Emphysema

Author: David J. Timson, Richard J. Reece, James B. Thoden, Hazel M. Holden, Andrea L. Utz, Beverly M. K. Biller, Eugen-Matthias Strehle, Markus Böhm, Thomas A. Luger, Alexander K. C. Leung, Andrew L. Wong, Markus G. Donner, Dieter Häussinger, Nirmal S. Mann, Marcus Schmitt, William Lane M. Robson, Manisha Balwani, Ainu Prakash-Cheng, Robert J. Desnick, Holger Lerche, Ingrid E. Scheffer, Samuel F. Berkovic, Brigitte M. Lobnig, Peter L. M. Jansen, Siegfried Waldegger, Florian Lang, Hugo ten Cate, Hagen Thieme, Michael Weller, Bärbel Schütte, Ronnie Fass, Hideki Kato, Masaomi Nangaku, Anthony Chang, Pradeep V. Kadambi, Jessy J. Alexander, Pierre Ronco, Hanna Debiec, Christian Hugo, John-John B. Schnog, Victor E. A. Gerdes, Jean Francis, David S. Geller, Knut Brockmann, Dong Wang, Darryl C. Vivo, Stefan Kölker, Elardus Erasmus, Lodewyk J. Mienie, John Vissing, Arnold Reuser, Catherine E. Correia, David A. Weinstein, Joseph I. Wolfsdorf, Yoon S. Shin, Reinout P. Hesselink, Maarten R. Drost, Anton J. M. Wagenmakers, Ger J. Vusse, Stefan Kiechl, Jonas Denecke, Ute Schepers, Thomas Kolter, Konrad Sandhoff, Dianna C. Martin, Barbara L. Triggs-Raine, Seda Sancak, Ralf Paschke, Dorin-Bogdan Borza, Sonja Ständer, Heiko Traupe, Michael A. Becker, Hanneke M. Straaten, Leo F. Verdonck, Hugo Ten Cate, Martin Mempel, Dietrich Abeck, Ismat Ghanem, Samer El Hage, Johannes G. Bode, Thomas A. Fleisher, Steven M. Holland, Bennett Myers, David Herrmann, Zaki Kraiem, Yaron Tomer, Terry F. Davies, James G. White, Sylvia Stöckler-Ipsiroglu, Guido Stoll, Klaus V. Toyka, Valéria Lamounier-Zepter, and Klaus Ruether
Published: 2009

41. GSD-Ia

Author: David J. Timson, Richard J. Reece, James B. Thoden, Hazel M. Holden, Andrea L. Utz, Beverly M. K. Biller, Eugen-Matthias Strehle, Markus Böhm, Thomas A. Luger, Alexander K. C. Leung, Andrew L. Wong, Markus G. Donner, Dieter Häussinger, Nirmal S. Mann, Marcus Schmitt, William Lane M. Robson, Manisha Balwani, Ainu Prakash-Cheng, Robert J. Desnick, Holger Lerche, Ingrid E. Scheffer, Samuel F. Berkovic, Brigitte M. Lobnig, Peter L. M. Jansen, Siegfried Waldegger, Florian Lang, Hugo ten Cate, Hagen Thieme, Michael Weller, Bärbel Schütte, Ronnie Fass, Hideki Kato, Masaomi Nangaku, Anthony Chang, Pradeep V. Kadambi, Jessy J. Alexander, Pierre Ronco, Hanna Debiec, Christian Hugo, John-John B. Schnog, Victor E. A. Gerdes, Jean Francis, David S. Geller, Knut Brockmann, Dong Wang, Darryl C. Vivo, Stefan Kölker, Elardus Erasmus, Lodewyk J. Mienie, John Vissing, Arnold Reuser, Catherine E. Correia, David A. Weinstein, Joseph I. Wolfsdorf, Yoon S. Shin, Reinout P. Hesselink, Maarten R. Drost, Anton J. M. Wagenmakers, Ger J. Vusse, Stefan Kiechl, Jonas Denecke, Ute Schepers, Thomas Kolter, Konrad Sandhoff, Dianna C. Martin, Barbara L. Triggs-Raine, Seda Sancak, Ralf Paschke, Dorin-Bogdan Borza, Sonja Ständer, Heiko Traupe, Michael A. Becker, Hanneke M. Straaten, Leo F. Verdonck, Hugo Ten Cate, Martin Mempel, Dietrich Abeck, Ismat Ghanem, Samer El Hage, Johannes G. Bode, Thomas A. Fleisher, Steven M. Holland, Bennett Myers, David Herrmann, Zaki Kraiem, Yaron Tomer, Terry F. Davies, James G. White, Sylvia Stöckler-Ipsiroglu, Guido Stoll, Klaus V. Toyka, Valéria Lamounier-Zepter, and Klaus Ruether
Published: 2009

42. GTP Cyclohydrolase I [arGTPCH] Deficiency

Author: David J. Timson, Richard J. Reece, James B. Thoden, Hazel M. Holden, Andrea L. Utz, Beverly M. K. Biller, Eugen-Matthias Strehle, Markus Böhm, Thomas A. Luger, Alexander K. C. Leung, Andrew L. Wong, Markus G. Donner, Dieter Häussinger, Nirmal S. Mann, Marcus Schmitt, William Lane M. Robson, Manisha Balwani, Ainu Prakash-Cheng, Robert J. Desnick, Holger Lerche, Ingrid E. Scheffer, Samuel F. Berkovic, Brigitte M. Lobnig, Peter L. M. Jansen, Siegfried Waldegger, Florian Lang, Hugo ten Cate, Hagen Thieme, Michael Weller, Bärbel Schütte, Ronnie Fass, Hideki Kato, Masaomi Nangaku, Anthony Chang, Pradeep V. Kadambi, Jessy J. Alexander, Pierre Ronco, Hanna Debiec, Christian Hugo, John-John B. Schnog, Victor E. A. Gerdes, Jean Francis, David S. Geller, Knut Brockmann, Dong Wang, Darryl C. Vivo, Stefan Kölker, Elardus Erasmus, Lodewyk J. Mienie, John Vissing, Arnold Reuser, Catherine E. Correia, David A. Weinstein, Joseph I. Wolfsdorf, Yoon S. Shin, Reinout P. Hesselink, Maarten R. Drost, Anton J. M. Wagenmakers, Ger J. Vusse, Stefan Kiechl, Jonas Denecke, Ute Schepers, Thomas Kolter, Konrad Sandhoff, Dianna C. Martin, Barbara L. Triggs-Raine, Seda Sancak, Ralf Paschke, Dorin-Bogdan Borza, Sonja Ständer, Heiko Traupe, Michael A. Becker, Hanneke M. Straaten, Leo F. Verdonck, Hugo Ten Cate, Martin Mempel, Dietrich Abeck, Ismat Ghanem, Samer El Hage, Johannes G. Bode, Thomas A. Fleisher, Steven M. Holland, Bennett Myers, David Herrmann, Zaki Kraiem, Yaron Tomer, Terry F. Davies, James G. White, Sylvia Stöckler-Ipsiroglu, Guido Stoll, Klaus V. Toyka, Valéria Lamounier-Zepter, and Klaus Ruether
Published: 2009

43. Gordon's Syndrome

Author: David J. Timson, Richard J. Reece, James B. Thoden, Hazel M. Holden, Andrea L. Utz, Beverly M. K. Biller, Eugen-Matthias Strehle, Markus Böhm, Thomas A. Luger, Alexander K. C. Leung, Andrew L. Wong, Markus G. Donner, Dieter Häussinger, Nirmal S. Mann, Marcus Schmitt, William Lane M. Robson, Manisha Balwani, Ainu Prakash-Cheng, Robert J. Desnick, Holger Lerche, Ingrid E. Scheffer, Samuel F. Berkovic, Brigitte M. Lobnig, Peter L. M. Jansen, Siegfried Waldegger, Florian Lang, Hugo ten Cate, Hagen Thieme, Michael Weller, Bärbel Schütte, Ronnie Fass, Hideki Kato, Masaomi Nangaku, Anthony Chang, Pradeep V. Kadambi, Jessy J. Alexander, Pierre Ronco, Hanna Debiec, Christian Hugo, John-John B. Schnog, Victor E. A. Gerdes, Jean Francis, David S. Geller, Knut Brockmann, Dong Wang, Darryl C. Vivo, Stefan Kölker, Elardus Erasmus, Lodewyk J. Mienie, John Vissing, Arnold Reuser, Catherine E. Correia, David A. Weinstein, Joseph I. Wolfsdorf, Yoon S. Shin, Reinout P. Hesselink, Maarten R. Drost, Anton J. M. Wagenmakers, Ger J. Vusse, Stefan Kiechl, Jonas Denecke, Ute Schepers, Thomas Kolter, Konrad Sandhoff, Dianna C. Martin, Barbara L. Triggs-Raine, Seda Sancak, Ralf Paschke, Dorin-Bogdan Borza, Sonja Ständer, Heiko Traupe, Michael A. Becker, Hanneke M. Straaten, Leo F. Verdonck, Hugo Ten Cate, Martin Mempel, Dietrich Abeck, Ismat Ghanem, Samer El Hage, Johannes G. Bode, Thomas A. Fleisher, Steven M. Holland, Bennett Myers, David Herrmann, Zaki Kraiem, Yaron Tomer, Terry F. Davies, James G. White, Sylvia Stöckler-Ipsiroglu, Guido Stoll, Klaus V. Toyka, Valéria Lamounier-Zepter, and Klaus Ruether
Published: 2009

44. Glomerulonephritis, Focal Proliferative

Author: David J. Timson, Richard J. Reece, James B. Thoden, Hazel M. Holden, Andrea L. Utz, Beverly M. K. Biller, Eugen-Matthias Strehle, Markus Böhm, Thomas A. Luger, Alexander K. C. Leung, Andrew L. Wong, Markus G. Donner, Dieter Häussinger, Nirmal S. Mann, Marcus Schmitt, William Lane M. Robson, Manisha Balwani, Ainu Prakash-Cheng, Robert J. Desnick, Holger Lerche, Ingrid E. Scheffer, Samuel F. Berkovic, Brigitte M. Lobnig, Peter L. M. Jansen, Siegfried Waldegger, Florian Lang, Hugo ten Cate, Hagen Thieme, Michael Weller, Bärbel Schütte, Ronnie Fass, Hideki Kato, Masaomi Nangaku, Anthony Chang, Pradeep V. Kadambi, Jessy J. Alexander, Pierre Ronco, Hanna Debiec, Christian Hugo, John-John B. Schnog, Victor E. A. Gerdes, Jean Francis, David S. Geller, Knut Brockmann, Dong Wang, Darryl C. Vivo, Stefan Kölker, Elardus Erasmus, Lodewyk J. Mienie, John Vissing, Arnold Reuser, Catherine E. Correia, David A. Weinstein, Joseph I. Wolfsdorf, Yoon S. Shin, Reinout P. Hesselink, Maarten R. Drost, Anton J. M. Wagenmakers, Ger J. Vusse, Stefan Kiechl, Jonas Denecke, Ute Schepers, Thomas Kolter, Konrad Sandhoff, Dianna C. Martin, Barbara L. Triggs-Raine, Seda Sancak, Ralf Paschke, Dorin-Bogdan Borza, Sonja Ständer, Heiko Traupe, Michael A. Becker, Hanneke M. Straaten, Leo F. Verdonck, Hugo Ten Cate, Martin Mempel, Dietrich Abeck, Ismat Ghanem, Samer El Hage, Johannes G. Bode, Thomas A. Fleisher, Steven M. Holland, Bennett Myers, David Herrmann, Zaki Kraiem, Yaron Tomer, Terry F. Davies, James G. White, Sylvia Stöckler-Ipsiroglu, Guido Stoll, Klaus V. Toyka, Valéria Lamounier-Zepter, and Klaus Ruether
Published: 2009

45. Giant Hypertrophic Gastritis

Author: David J. Timson, Richard J. Reece, James B. Thoden, Hazel M. Holden, Andrea L. Utz, Beverly M. K. Biller, Eugen-Matthias Strehle, Markus Böhm, Thomas A. Luger, Alexander K. C. Leung, Andrew L. Wong, Markus G. Donner, Dieter Häussinger, Nirmal S. Mann, Marcus Schmitt, William Lane M. Robson, Manisha Balwani, Ainu Prakash-Cheng, Robert J. Desnick, Holger Lerche, Ingrid E. Scheffer, Samuel F. Berkovic, Brigitte M. Lobnig, Peter L. M. Jansen, Siegfried Waldegger, Florian Lang, Hugo ten Cate, Hagen Thieme, Michael Weller, Bärbel Schütte, Ronnie Fass, Hideki Kato, Masaomi Nangaku, Anthony Chang, Pradeep V. Kadambi, Jessy J. Alexander, Pierre Ronco, Hanna Debiec, Christian Hugo, John-John B. Schnog, Victor E. A. Gerdes, Jean Francis, David S. Geller, Knut Brockmann, Dong Wang, Darryl C. Vivo, Stefan Kölker, Elardus Erasmus, Lodewyk J. Mienie, John Vissing, Arnold Reuser, Catherine E. Correia, David A. Weinstein, Joseph I. Wolfsdorf, Yoon S. Shin, Reinout P. Hesselink, Maarten R. Drost, Anton J. M. Wagenmakers, Ger J. Vusse, Stefan Kiechl, Jonas Denecke, Ute Schepers, Thomas Kolter, Konrad Sandhoff, Dianna C. Martin, Barbara L. Triggs-Raine, Seda Sancak, Ralf Paschke, Dorin-Bogdan Borza, Sonja Ständer, Heiko Traupe, Michael A. Becker, Hanneke M. Straaten, Leo F. Verdonck, Hugo Ten Cate, Martin Mempel, Dietrich Abeck, Ismat Ghanem, Samer El Hage, Johannes G. Bode, Thomas A. Fleisher, Steven M. Holland, Bennett Myers, David Herrmann, Zaki Kraiem, Yaron Tomer, Terry F. Davies, James G. White, Sylvia Stöckler-Ipsiroglu, Guido Stoll, Klaus V. Toyka, Valéria Lamounier-Zepter, and Klaus Ruether
Published: 2009

46. Gray Platelet Syndrome

Author: David J. Timson, Richard J. Reece, James B. Thoden, Hazel M. Holden, Andrea L. Utz, Beverly M. K. Biller, Eugen-Matthias Strehle, Markus Böhm, Thomas A. Luger, Alexander K. C. Leung, Andrew L. Wong, Markus G. Donner, Dieter Häussinger, Nirmal S. Mann, Marcus Schmitt, William Lane M. Robson, Manisha Balwani, Ainu Prakash-Cheng, Robert J. Desnick, Holger Lerche, Ingrid E. Scheffer, Samuel F. Berkovic, Brigitte M. Lobnig, Peter L. M. Jansen, Siegfried Waldegger, Florian Lang, Hugo ten Cate, Hagen Thieme, Michael Weller, Bärbel Schütte, Ronnie Fass, Hideki Kato, Masaomi Nangaku, Anthony Chang, Pradeep V. Kadambi, Jessy J. Alexander, Pierre Ronco, Hanna Debiec, Christian Hugo, John-John B. Schnog, Victor E. A. Gerdes, Jean Francis, David S. Geller, Knut Brockmann, Dong Wang, Darryl C. Vivo, Stefan Kölker, Elardus Erasmus, Lodewyk J. Mienie, John Vissing, Arnold Reuser, Catherine E. Correia, David A. Weinstein, Joseph I. Wolfsdorf, Yoon S. Shin, Reinout P. Hesselink, Maarten R. Drost, Anton J. M. Wagenmakers, Ger J. Vusse, Stefan Kiechl, Jonas Denecke, Ute Schepers, Thomas Kolter, Konrad Sandhoff, Dianna C. Martin, Barbara L. Triggs-Raine, Seda Sancak, Ralf Paschke, Dorin-Bogdan Borza, Sonja Ständer, Heiko Traupe, Michael A. Becker, Hanneke M. Straaten, Leo F. Verdonck, Hugo Ten Cate, Martin Mempel, Dietrich Abeck, Ismat Ghanem, Samer El Hage, Johannes G. Bode, Thomas A. Fleisher, Steven M. Holland, Bennett Myers, David Herrmann, Zaki Kraiem, Yaron Tomer, Terry F. Davies, James G. White, Sylvia Stöckler-Ipsiroglu, Guido Stoll, Klaus V. Toyka, Valéria Lamounier-Zepter, and Klaus Ruether
Published: 2009

47. Glucagon Deficiency Syndromes

Author: David J. Timson, Richard J. Reece, James B. Thoden, Hazel M. Holden, Andrea L. Utz, Beverly M. K. Biller, Eugen-Matthias Strehle, Markus Böhm, Thomas A. Luger, Alexander K. C. Leung, Andrew L. Wong, Markus G. Donner, Dieter Häussinger, Nirmal S. Mann, Marcus Schmitt, William Lane M. Robson, Manisha Balwani, Ainu Prakash-Cheng, Robert J. Desnick, Holger Lerche, Ingrid E. Scheffer, Samuel F. Berkovic, Brigitte M. Lobnig, Peter L. M. Jansen, Siegfried Waldegger, Florian Lang, Hugo ten Cate, Hagen Thieme, Michael Weller, Bärbel Schütte, Ronnie Fass, Hideki Kato, Masaomi Nangaku, Anthony Chang, Pradeep V. Kadambi, Jessy J. Alexander, Pierre Ronco, Hanna Debiec, Christian Hugo, John-John B. Schnog, Victor E. A. Gerdes, Jean Francis, David S. Geller, Knut Brockmann, Dong Wang, Darryl C. Vivo, Stefan Kölker, Elardus Erasmus, Lodewyk J. Mienie, John Vissing, Arnold Reuser, Catherine E. Correia, David A. Weinstein, Joseph I. Wolfsdorf, Yoon S. Shin, Reinout P. Hesselink, Maarten R. Drost, Anton J. M. Wagenmakers, Ger J. Vusse, Stefan Kiechl, Jonas Denecke, Ute Schepers, Thomas Kolter, Konrad Sandhoff, Dianna C. Martin, Barbara L. Triggs-Raine, Seda Sancak, Ralf Paschke, Dorin-Bogdan Borza, Sonja Ständer, Heiko Traupe, Michael A. Becker, Hanneke M. Straaten, Leo F. Verdonck, Hugo Ten Cate, Martin Mempel, Dietrich Abeck, Ismat Ghanem, Samer El Hage, Johannes G. Bode, Thomas A. Fleisher, Steven M. Holland, Bennett Myers, David Herrmann, Zaki Kraiem, Yaron Tomer, Terry F. Davies, James G. White, Sylvia Stöckler-Ipsiroglu, Guido Stoll, Klaus V. Toyka, Valéria Lamounier-Zepter, and Klaus Ruether
Published: 2009

48. Glutaric Acidemia

Author: David J. Timson, Richard J. Reece, James B. Thoden, Hazel M. Holden, Andrea L. Utz, Beverly M. K. Biller, Eugen-Matthias Strehle, Markus Böhm, Thomas A. Luger, Alexander K. C. Leung, Andrew L. Wong, Markus G. Donner, Dieter Häussinger, Nirmal S. Mann, Marcus Schmitt, William Lane M. Robson, Manisha Balwani, Ainu Prakash-Cheng, Robert J. Desnick, Holger Lerche, Ingrid E. Scheffer, Samuel F. Berkovic, Brigitte M. Lobnig, Peter L. M. Jansen, Siegfried Waldegger, Florian Lang, Hugo ten Cate, Hagen Thieme, Michael Weller, Bärbel Schütte, Ronnie Fass, Hideki Kato, Masaomi Nangaku, Anthony Chang, Pradeep V. Kadambi, Jessy J. Alexander, Pierre Ronco, Hanna Debiec, Christian Hugo, John-John B. Schnog, Victor E. A. Gerdes, Jean Francis, David S. Geller, Knut Brockmann, Dong Wang, Darryl C. Vivo, Stefan Kölker, Elardus Erasmus, Lodewyk J. Mienie, John Vissing, Arnold Reuser, Catherine E. Correia, David A. Weinstein, Joseph I. Wolfsdorf, Yoon S. Shin, Reinout P. Hesselink, Maarten R. Drost, Anton J. M. Wagenmakers, Ger J. Vusse, Stefan Kiechl, Jonas Denecke, Ute Schepers, Thomas Kolter, Konrad Sandhoff, Dianna C. Martin, Barbara L. Triggs-Raine, Seda Sancak, Ralf Paschke, Dorin-Bogdan Borza, Sonja Ständer, Heiko Traupe, Michael A. Becker, Hanneke M. Straaten, Leo F. Verdonck, Hugo Ten Cate, Martin Mempel, Dietrich Abeck, Ismat Ghanem, Samer El Hage, Johannes G. Bode, Thomas A. Fleisher, Steven M. Holland, Bennett Myers, David Herrmann, Zaki Kraiem, Yaron Tomer, Terry F. Davies, James G. White, Sylvia Stöckler-Ipsiroglu, Guido Stoll, Klaus V. Toyka, Valéria Lamounier-Zepter, and Klaus Ruether
Published: 2009

49. Guttate Parapsoriasis

Author: David J. Timson, Richard J. Reece, James B. Thoden, Hazel M. Holden, Andrea L. Utz, Beverly M. K. Biller, Eugen-Matthias Strehle, Markus Böhm, Thomas A. Luger, Alexander K. C. Leung, Andrew L. Wong, Markus G. Donner, Dieter Häussinger, Nirmal S. Mann, Marcus Schmitt, William Lane M. Robson, Manisha Balwani, Ainu Prakash-Cheng, Robert J. Desnick, Holger Lerche, Ingrid E. Scheffer, Samuel F. Berkovic, Brigitte M. Lobnig, Peter L. M. Jansen, Siegfried Waldegger, Florian Lang, Hugo ten Cate, Hagen Thieme, Michael Weller, Bärbel Schütte, Ronnie Fass, Hideki Kato, Masaomi Nangaku, Anthony Chang, Pradeep V. Kadambi, Jessy J. Alexander, Pierre Ronco, Hanna Debiec, Christian Hugo, John-John B. Schnog, Victor E. A. Gerdes, Jean Francis, David S. Geller, Knut Brockmann, Dong Wang, Darryl C. Vivo, Stefan Kölker, Elardus Erasmus, Lodewyk J. Mienie, John Vissing, Arnold Reuser, Catherine E. Correia, David A. Weinstein, Joseph I. Wolfsdorf, Yoon S. Shin, Reinout P. Hesselink, Maarten R. Drost, Anton J. M. Wagenmakers, Ger J. Vusse, Stefan Kiechl, Jonas Denecke, Ute Schepers, Thomas Kolter, Konrad Sandhoff, Dianna C. Martin, Barbara L. Triggs-Raine, Seda Sancak, Ralf Paschke, Dorin-Bogdan Borza, Sonja Ständer, Heiko Traupe, Michael A. Becker, Hanneke M. Straaten, Leo F. Verdonck, Hugo Ten Cate, Martin Mempel, Dietrich Abeck, Ismat Ghanem, Samer El Hage, Johannes G. Bode, Thomas A. Fleisher, Steven M. Holland, Bennett Myers, David Herrmann, Zaki Kraiem, Yaron Tomer, Terry F. Davies, James G. White, Sylvia Stöckler-Ipsiroglu, Guido Stoll, Klaus V. Toyka, Valéria Lamounier-Zepter, and Klaus Ruether
Published: 2009

50. Glucagon Secreting Tumor

Author: David J. Timson, Richard J. Reece, James B. Thoden, Hazel M. Holden, Andrea L. Utz, Beverly M. K. Biller, Eugen-Matthias Strehle, Markus Böhm, Thomas A. Luger, Alexander K. C. Leung, Andrew L. Wong, Markus G. Donner, Dieter Häussinger, Nirmal S. Mann, Marcus Schmitt, William Lane M. Robson, Manisha Balwani, Ainu Prakash-Cheng, Robert J. Desnick, Holger Lerche, Ingrid E. Scheffer, Samuel F. Berkovic, Brigitte M. Lobnig, Peter L. M. Jansen, Siegfried Waldegger, Florian Lang, Hugo ten Cate, Hagen Thieme, Michael Weller, Bärbel Schütte, Ronnie Fass, Hideki Kato, Masaomi Nangaku, Anthony Chang, Pradeep V. Kadambi, Jessy J. Alexander, Pierre Ronco, Hanna Debiec, Christian Hugo, John-John B. Schnog, Victor E. A. Gerdes, Jean Francis, David S. Geller, Knut Brockmann, Dong Wang, Darryl C. Vivo, Stefan Kölker, Elardus Erasmus, Lodewyk J. Mienie, John Vissing, Arnold Reuser, Catherine E. Correia, David A. Weinstein, Joseph I. Wolfsdorf, Yoon S. Shin, Reinout P. Hesselink, Maarten R. Drost, Anton J. M. Wagenmakers, Ger J. Vusse, Stefan Kiechl, Jonas Denecke, Ute Schepers, Thomas Kolter, Konrad Sandhoff, Dianna C. Martin, Barbara L. Triggs-Raine, Seda Sancak, Ralf Paschke, Dorin-Bogdan Borza, Sonja Ständer, Heiko Traupe, Michael A. Becker, Hanneke M. Straaten, Leo F. Verdonck, Hugo Ten Cate, Martin Mempel, Dietrich Abeck, Ismat Ghanem, Samer El Hage, Johannes G. Bode, Thomas A. Fleisher, Steven M. Holland, Bennett Myers, David Herrmann, Zaki Kraiem, Yaron Tomer, Terry F. Davies, James G. White, Sylvia Stöckler-Ipsiroglu, Guido Stoll, Klaus V. Toyka, Valéria Lamounier-Zepter, and Klaus Ruether
Published: 2009

Catalog

Books, media, physical & digital resources

See catalog results

Searchworks

Select search scope, currently: Articles Catalog books, media & more in Jio Institute collections Articles journal articles & other e-resources

Search

Search Constraints

Refine your results

Search Limiters

Topic

Publication Year Range

Language

Publication Type

Journal

Database

Publisher

223 results on '"Richard J. Reece"'

Search Results

Catalog

Select search scope, currently: Articles

Catalog

books, media & more in Jio Institute collections

Articles

journal articles & other e-resources