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21 results on '"Ericsson, Ulrika"'

2. Development of Inhibitors of PIP4K2 As a Treatment for Patients with Hematologic Malignancies

Author

McElligott, David L, primary, Kesicki, Edward, additional, Karukarichi, Kannan, additional, Shim, Hyeseok, additional, Wang, Rui, additional, Yu, Albert S., additional, Zolfaghari, Parisa, additional, Linstrom, Johan, additional, Persson, Lars, additional, Hoglund, Andreas, additional, Ericsson, Ulrika, additional, Trésaugues, Lionel, additional, Livendahl, Madeleine, additional, Santangelo, Ellen, additional, Viklund, Jenny, additional, Pettersson, Mariell, additional, Wähling, Horst, additional, Forsblom, Rickard, additional, Karlsson, Fredrik, additional, Ginman, Tobias, additional, Braga, Tiago, additional, Henley, Aine Brigette, additional, Talagas, Antoine, additional, Rahm, Fredrik, additional, Johansson, Tommy, additional, Martinsson, Jessica, additional, Andersson, Martin, additional, and Cantley, Lewis, additional

Published
2018
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3. Creation of a Novel Class of Potent and Selective MutT Homologue 1 (MTH1) Inhibitors Using Fragment-Based Screening and Structure-Based Drug Design

Author

Rahm, Fredrik, primary, Viklund, Jenny, additional, Trésaugues, Lionel, additional, Ellermann, Manuel, additional, Giese, Anja, additional, Ericsson, Ulrika, additional, Forsblom, Rickard, additional, Ginman, Tobias, additional, Günther, Judith, additional, Hallberg, Kenth, additional, Lindström, Johan, additional, Persson, Lars Boukharta, additional, Silvander, Camilla, additional, Talagas, Antoine, additional, Díaz-Sáez, Laura, additional, Fedorov, Oleg, additional, Huber, Kilian V. M., additional, Panagakou, Ioanna, additional, Siejka, Paulina, additional, Gorjánácz, Mátyás, additional, Bauser, Marcus, additional, and Andersson, Martin, additional

Published
2018
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4. Novel Class of Potent and Cellularly Active Inhibitors Devalidates MTH1 as Broad-Spectrum Cancer Target

Author

Ellermann, Manuel, primary, Eheim, Ashley, additional, Rahm, Fredrik, additional, Viklund, Jenny, additional, Guenther, Judith, additional, Andersson, Martin, additional, Ericsson, Ulrika, additional, Forsblom, Rickard, additional, Ginman, Tobias, additional, Lindström, Johan, additional, Silvander, Camilla, additional, Trésaugues, Lionel, additional, Giese, Anja, additional, Bunse, Stefanie, additional, Neuhaus, Roland, additional, Weiske, Jörg, additional, Quanz, Maria, additional, Glasauer, Andrea, additional, Nowak-Reppel, Katrin, additional, Bader, Benjamin, additional, Irlbacher, Horst, additional, Meyer, Hanna, additional, Queisser, Nina, additional, Bauser, Marcus, additional, Haegebarth, Andrea, additional, and Gorjánácz, Mátyás, additional

Published
2017
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5. Novel Class of Potent and Cellularly Active Inhibitors Devalidates MTH1 as Broad-Spectrum Cancer Target

Author

Ellermann, Manuel, Eheim, Ashley, Rahm, Fredrik, Viklund, Jenny, Guenther, Judith, Andersson, Martin, Ericsson, Ulrika, Forsblom, Rickard, Ginman, Tobias, Lindström, Johan, Silvander, Camilla, Trésaugues, Lionel, Giese, Anja, Bunse, Stefanie, Neuhaus, Roland, Weiske, Jörg, Quanz, Maria, Glasauer, Andrea, Nowak-Reppel, Katrin, Bader, Benjamin, Irlbacher, Horst, Meyer, Hanna, Queisser, Nina, Bauser, Marcus, Haegebarth, Andrea, and Gorjánácz, Mátyás

Abstract

MTH1 is a hydrolase responsible for sanitization of oxidized purine nucleoside triphosphates to prevent their incorporation into replicating DNA. Early tool compounds published in the literature inhibited the enzymatic activity of MTH1 and subsequently induced cancer cell death; however recent studies have questioned the reported link between these two events. Therefore, it is important to validate MTH1 as a cancer dependency with high quality chemical probes. Here, we present BAY-707, a substrate-competitive, highly potent and selective inhibitor of MTH1, chemically distinct compared to those previously published. Despite superior cellular target engagement and pharmacokinetic properties, inhibition of MTH1 with BAY-707 resulted in a clear lack of in vitroor in vivoanticancer efficacy either in mono- or in combination therapies. Therefore, we conclude that MTH1 is dispensable for cancer cell survival.

Published
2024
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6. Bringing global issues to medical teaching

Author

Bateman, Catherine, Baker, Tim, Hoornenborg, Elske, and Ericsson, Ulrika

Subjects
Globalization -- Health aspects, Medical students -- Curricula, Physicians -- Education
Published
2001

8. Massage : A study about how teachers can introduce massage i school

Author

Ericsson, Ulrika and Samuelsson, Gina

Subjects
Massage, Pedagogik, positiv beröring, kompismassage, introduktion, Education
Abstract

Denna uppsats handlar om hur man som lärare kan arbeta med massage i klassrummet. Frågor som behandlas i arbetet: Hur kan man introducera massage i skolan?, Vad visar studier på för nackdelar och fördelar?, Hur påverkas kroppen av massage? Arbetet bygger på litteraturstudier, en empirisk undersökning i form av intervjuer samt egna erfarenheter efter att introducerat massage på slutpraktiken. I resultatdelen redovisas intervjuerna som gjorts med två lärare som håller på med massage i skolan och tio elever samt hur vi genomförde vår egen massageintroduktion. Genom detta arbete har vi kommit fram till massage och beröring är mycket viktig för barns välbefinnande och att man med enkla medel kan introducera kompismassagen i skolan.

Published
1999

9. Massage : En studie om hur lärare kan introducera massage i skolan

Author

Ericsson, Ulrika and Samuelsson, Gina

Subjects
Massage, Pedagogik, positiv beröring, kompismassage, introduktion, Education
Abstract

Denna uppsats handlar om hur man som lärare kan arbeta med massage i klassrummet. Frågor som behandlas i arbetet: Hur kan man introducera massage i skolan?, Vad visar studier på för nackdelar och fördelar?, Hur påverkas kroppen av massage? Arbetet bygger på litteraturstudier, en empirisk undersökning i form av intervjuer samt egna erfarenheter efter att introducerat massage på slutpraktiken. I resultatdelen redovisas intervjuerna som gjorts med två lärare som håller på med massage i skolan och tio elever samt hur vi genomförde vår egen massageintroduktion. Genom detta arbete har vi kommit fram till massage och beröring är mycket viktig för barns välbefinnande och att man med enkla medel kan introducera kompismassagen i skolan.

Published
1999

10. A structural genomics pilot project : methods and applications

Author

Ericsson, Ulrika and Ericsson, Ulrika

Abstract

With the availability of many completely sequenced genomes, scientific research has shifted from genes to the products of the genes, the proteins. Structural genomics groups have been established worldwide, with the objective of determining protein structures on a genome-wide scale. New methods for protein production and structural determination have become necessary. Two methods for high throughput analysis of proteins are presented in the first part of this thesis. The first method is the thermofluor method, which presents a fast way to identify stabilizing conditions for a particular protein. It was shown that the addition of a stabilizing additive, identified with the thermofluor method, significantly increased the likelihood of growing protein crystals. The second method presented in this thesis provides a fast and robust way to detect metal containing proteins. The second part of this thesis describes the crystal structures of two RNA modifying enzymes, the pseudouridine synthase TruD and the RNA m5C methyltransferase YebU. The catalytic domain of TruD was shown to bear remarkable structural similarity to the other pseudouridine families despite a lack of sequence similarity. In addition to the catalytic domain, the structure of TruD also contained an insertion domain with a novel fold. YebU was also found have two structurally distinct domains. The N-terminal catalytic domain has a high structural similarity to other RNA m5C methyltransferases. The C-terminal domain was revealed to be a so-called PUA domain, which had not been predicted by previous sequence alignments.

Published
2006

18. The Structure of the RNA m5C Methyltransferase YebU from Escherichia coli Reveals a C-terminal RNA-recruiting PUA Domain

Author

Hallberg, B. Martin, Ericsson, Ulrika B., Johnson, Kenneth A., Andersen, Niels Møller, Douthwaite, Stephen, Nordlund, Pär, Beuscher, Albert E., and Erlandsen, Heidi

Subjects
*ESCHERICHIA coli, *NUCLEIC acids, *HOMOCYSTEINE, *ESCHERICHIA
Abstract

Abstract: Nucleotide methylations are the most common type of rRNA modification in bacteria, and are introduced post-transcriptionally by a wide variety of site-specific enzymes. Three 5-methylcytidine (m5C) bases are found in the rRNAs of Escherichia coli and one of these, at nucleotide 1407 in 16 S rRNA, is the modification product of the methyltransferase (MTase) YebU (also called RsmF). YebU requires S-adenosyl-l-methionine (SAM) and methylates C1407 within assembled 30 S subunits, but not in naked 16 S rRNA or within tight-couple 70 S ribosomes. Here, we describe the three-dimensional structure of YebU determined by X-ray crystallography, and we present a molecular model for how YebU specifically recognizes, binds and methylates its ribosomal substrate. The YebU protein has an N-terminal SAM-binding catalytic domain with structural similarity to the equivalent domains in several other m5C RNA MTases including RsmB and PH1374. The C-terminal one-third of YebU contains a domain similar to that in pseudouridine synthases and archaeosine-specific transglycosylases (PUA-domain), which was not predicted by sequence alignments. Furthermore, YebU is predicted to contain extended regions of positive electrostatic potential that differ from other RNA-MTase structures, suggesting that YebU interacts with its RNA target in a different manner. Docking of YebU onto the 30 S subunit indicates that the PUA and MTase domains make several contacts with 16 S rRNA as well as with the ribosomal protein S12. The ribosomal protein interactions would explain why the assembled 30 S subunit, and not naked 16 S rRNA, is the preferred substrate for YebU. [Copyright &y& Elsevier]

Published
2006
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21. Expression, purification, crystallization and preliminary diffraction studies of the tRNA pseudouridine synthase TruD from Escherichia coli.

Author

Ericsson UB, Andersson ME, Engvall B, Nordlund P, and Hallberg BM

Subjects
Cloning, Molecular, Crystallography, X-Ray, Hydro-Lyases chemistry, Crystallization, Escherichia coli Proteins chemistry, Intramolecular Transferases chemistry
Abstract

Pseudouridine, the 5-ribosyl isomer of uridine, is the most common modification of structural RNA. The recently identified pseudouridine synthase TruD belongs to a widespread class of pseudouridine synthases without significant sequence homology to previously known families. TruD from Escherichia coli was overexpressed, purified and crystallized. The crystals diffract to a minimum Bragg spacing of 2.4 A and belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 63.4, b = 108.6, c = 111.7 A.

Published
2004
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