Search

Your search keyword '"Auburger G"' showing total 10 results
Start Over Author "Auburger G" Language undetermined
10 results on '"Auburger G"'

1. Erratum

Author

Klionsky, DJ, Abdelmohsen, K, Abe, A, Abedin, MJ, Abeliovich, H, Arozena, AA, Adachi, H, Adams, CM, Adams, PD, Adeli, K, Adhihetty, PJ, Adler, SG, Agam, G, Agarwal, R, Aghi, MK, Agnello, M, Agostinis, P, Aguilar, PV, Aguirre-Ghiso, J, Airoldi, EM, Ait-Si-Ali, S, Akematsu, T, Akporiaye, ET, Al-Rubeai, M, Albaiceta, GM, Albanese, C, Albani, D, Albert, ML, Aldudo, J, Algül, H, Alirezaei, M, Alloza, I, Almasan, A, Almonte-Beceril, M, Alnemri, ES, Alonso, C, Altan-Bonnet, N, Altieri, DC, Alvarez, S, Alvarez-Erviti, L, Alves, S, Amadoro, G, Amano, A, Amantini, C, Ambrosio, S, Amelio, I, Amer, AO, Amessou, M, Amon, A, An, Z, Anania, FA, Andersen, SU, Andley, UP, Andreadi, CK, Andrieu-Abadie, N, Anel, A, Ann, DK, Anoopkumar-Dukie, S, Antonioli, M, Aoki, H, Apostolova, N, Aquila, S, Aquilano, K, Araki, K, Arama, E, Aranda, A, Araya, J, Arcaro, A, Arias, E, Arimoto, H, Ariosa, AR, Armstrong, JL, Arnould, T, Arsov, I, Asanuma, K, Askanas, V, Asselin, E, Atarashi, R, Atherton, SS, Atkin, JD, Attardi, LD, Auberger, P, Auburger, G, Aurelian, L, Autelli, R, Avagliano, L, Avantaggiati, ML, Avrahami, L, Azad, N, Awale, S, Bachetti, T, Backer, JM, Bae, DH, Bae, JS, Bae, ON, Bae, SH, Baehrecke, EH, Baek, SH, Baghdiguian, S, and Bagniewska-Zadworna, A

Subjects
Biochemistry & Molecular Biology, Biochemistry and Cell Biology
Published
2016

2. Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)

Author

Klionsky, D.J., Abdelmohsen, K., Abe, A., Abedin, M.J., Abeliovich, H., Acevedo Arozena, A., Adachi, H., Adams, C.M., Adams, P.D., Adeli, K., Adhihetty, P.J., Adler, S.G., Agam, G., Agarwal, R., Aghi, M.K., Agnello, M., Agostinis, P., Aguilar, P.V., Aguirre-Ghiso, J., Airoldi, E.M., Ait-Si-Ali, S., Akematsu, T., Akporiaye, E.T., Al-Rubeai, M., Albaiceta, G.M., Albanese, C., Albani, D., Albert, M.L., Aldudo, J., Algul, H., Alirezaei, M., Alloza, I., Almasan, A., Almonte-Beceril, M., Alnemri, E.S., Alonso, C., Altan-Bonnet, N., Altieri, D.C., Alvarez, S., Alvarez-Erviti, L., Alves, S., Amadoro, G., Amano, A., Amantini, C., Ambrosio, S., Amelio, I., Amer, A.O., Amessou, M., Amon, A., An, Z., Anania, F.A., Andersen, S.U., Andley, UP, Andreadi, C.K., Andrieu-Abadie, N., Anel, A., Ann, D.K., Anoopkumar-Dukie, S., Antonioli, M., Aoki, H., Apostolova, N., Aquila, S., Aquilano, K., Araki, K., Arama, E., Aranda, A., Araya, J., Arcaro, A., Arias, E., Arimoto, H., Ariosa, A.R., Armstrong, J.L., Arnould, T., Arsov, I., Asanuma, K., Askanas, V., Asselin, E., Atarashi, R., Atherton, S.S., Atkin, J.D., Attardi, L.D., Auberger, P., Auburger, G., Aurelian, L., Autelli, R., Avagliano, L., Avantaggiati, M.L., Avrahami, L., Awale, S., Azad, N., Bachetti, T., Backer, J.M., Bae, D.H., Bae, J.S., Bae, O.N., Bae, S.H., Baehrecke, E.H., Baek, S.H., Baghdiguian, S., Bagniewska-Zadworna, A., Netea-Maier, R.T., Joosten, L.A.B., Span, P.N., Nagelkerke, A.P., and Netea, M.G.

Subjects
lnfectious Diseases and Global Health Radboud Institute for Molecular Life Sciences [Radboudumc 4], Rare cancers Radboud Institute for Molecular Life Sciences [Radboudumc 9], Women's cancers Radboud Institute for Health Sciences [Radboudumc 17]
Abstract

Contains fulltext : 172645.pdf (Publisher’s version ) (Closed access)

Published
2016

3. Erratum

Author

Klionsky, DJ, Abdelmohsen, K, Abe, A, Abedin, MJ, Abeliovich, H, Arozena, AA, Adachi, H, Adams, CM, Adams, PD, Adeli, K, Adhihetty, PJ, Adler, SG, Agam, G, Agarwal, R, Aghi, MK, Agnello, M, Agostinis, P, Aguilar, PV, Aguirre-Ghiso, J, Airoldi, EM, Ait-Si-Ali, S, Akematsu, T, Akporiaye, ET, Al-Rubeai, M, Albaiceta, GM, Albanese, C, Albani, D, Albert, ML, Aldudo, J, Algül, H, Alirezaei, M, Alloza, I, Almasan, A, Almonte-Beceril, M, Alnemri, ES, Alonso, C, Altan-Bonnet, N, Altieri, DC, Alvarez, S, Alvarez-Erviti, L, Alves, S, Amadoro, G, Amano, A, Amantini, C, Ambrosio, S, Amelio, I, Amer, AO, Amessou, M, Amon, A, An, Z, Anania, FA, Andersen, SU, Andley, UP, Andreadi, CK, Andrieu-Abadie, N, Anel, A, Ann, DK, Anoopkumar-Dukie, S, Antonioli, M, Aoki, H, Apostolova, N, Aquila, S, Aquilano, K, Araki, K, Arama, E, Aranda, A, Araya, J, Arcaro, A, Arias, E, Arimoto, H, Ariosa, AR, Armstrong, JL, Arnould, T, Arsov, I, Asanuma, K, Askanas, V, Asselin, E, Atarashi, R, Atherton, SS, Atkin, JD, Attardi, LD, Auberger, P, Auburger, G, Aurelian, L, Autelli, R, Avagliano, L, Avantaggiati, ML, Avrahami, L, Azad, N, Awale, S, Bachetti, T, Backer, JM, Bae, DH, Bae, JS, Bae, ON, Bae, SH, Baehrecke, EH, Baek, SH, Baghdiguian, S, and Bagniewska-Zadworna, A

Subjects
Biochemistry & Molecular Biology, Biochemistry and Cell Biology
Published
2016

4. His1069Gln and six novel Wilson disease mutations: analysis of relevance for early diagnosis and phenotype

Author

Wolfgang Stremmel, Castañeda-Guillot C, Auburger G, Diane W. Cox, Hernández Hernández A, Harald Hefter, and Duc Hh

Subjects
Male, Genotype, Gene mutation, Biology, Polymerase Chain Reaction, Exon, Hepatolenticular Degeneration, Genetics, Humans, Missense mutation, Histidine, Polymorphism, Single-Stranded Conformational, Genetics (clinical), DNA Primers, Base Sequence, Haplotype, Intron, Phenotype, Stop codon, Pedigree, Haplotypes, Mutation, RNA splicing, Female
Abstract

In the present study we examined 33 German and 10 Cuban unrelated Wilson disease (WND) index patients and their relatives. The common His1069Gln mutation accounted for 42% of all WND chromosomes in the German series and the haplotype C was found to be highly predictive for this mutation. Six WND gene mutations have not been described previously and involved a splice site at intron 18 (3903 + del1G), a termination codon in the copper-binding region of exon 2 (Cys271X), and missense mutations in transmembrane region 2 (Gly710Ala), in transmembrane region 3 (Tyr741Cys), in the DKTGT motif (Thr1031Ile) and in the ATP loop region (Gly1176Arg). In 15 German WND index patients and three sibs both WND mutations could be determined and a genotype-phenotype correlation was attempted. Patients homozygous for the His1069Gln mutation showed almost the complete range of clinical presentations, and thus in our study this mutation is not associated with a late, neurological presentation.

Published
1998

7. Mutation detection in Machado-Joseph disease using repeat expansion detection

Author

Lindblad, K., Lunkes, A., Patricia Maciel, Stevanin, G., Zander, C., Klockgether, T., Ratzlaff, T., Brice, A., Rouleau, G. A., Hudson, T., Auburger, G., and Schalling, M.

Subjects
congenital, hereditary, and neonatal diseases and abnormalities, Base Sequence, Genetic Linkage, Molecular Sequence Data, Machado-Joseph Disease, Polymerase Chain Reaction, Pedigree, Mutation, Humans, Electrophoresis, Polyacrylamide Gel, Alleles, DNA Primers, Repetitive Sequences, Nucleic Acid, Research Article
Abstract

BACKGROUND: Several neurological disorders have recently been explained through the discovery of expanded DNA repeat sequences. Among these is Machado-Joseph disease, one of the most common spinocerebellar ataxias (MJD/SCA3), caused by a CAG repeat expansion on chromosome 14. A useful way of detecting repeat sequence mutations is offered by the repeat expansion detection method (RED), in which a thermostable ligase is used to detect repeat expansions directly from genomic DNA. We have used RED to detect CAG expansions in families with either MJD/SCA3 or with previously uncharacterized spinocerebellar ataxia (SCA). MATERIALS AND METHODS: Five MJD/SCA3 families and one SCA family where linkage to SCA1-5 had been excluded were analyzed by RED and polymerase chain reaction (PCR). RESULTS: An expansion represented by RED products of 180-270 bp segregated with MJD/SCA3 (p < 0.00001) in five families (n = 60) and PCR products corresponding to 66-80 repeat copies were observed in all affected individuals. We also detected a 210-bp RED product segregating with disease (p < 0.01) in a non-SCA1-5 family (n = 16), suggesting involvement of a CAG expansion in the pathophysiology. PCR analysis subsequently revealed an elongated MJD/SCA3 allele in all affected family members. CONCLUSIONS: RED products detected in Machado-Joseph disease families correlated with elongated PCR products at the MJD/SCA3 locus. We demonstrate the added usefulness of RED in detecting repeat expansions in disorders where linkage is complicated by phenotyping problems in gradually developing adult-onset disorders, as in the non-SCA1-5 family examined. The RED method is informative without any knowledge of flanking sequences. This is particularly useful when studying diseases where the mutated gene is unknown. We conclude that RED is a reliable method for analyzing expanded repeat sequences in the genome.

10. Hereditary early-onset Parkinson's disease caused by mutations in PINK1

Author

William P. Gilks, Robert L. Nussbaum, Alberto Albanese, S Salvi, Nicholas W. Wood, Roberk J. Harvey, Daniel G. Healy, Suzana Gispert, Domenico Del Turco, David S. Latchman, Eriza Maria Valente, Rafael González-Maldonado, Zeeshan Ali, Pietro Cortelli, Patrick M. Abou-Sleiman, Georg Auburger, Kirsten Harvey, Anna Rita Bentivoglio, Thomas Deller, Bruno Dallapiccola, Viviana Caputo, Miratul M. K. Muqit, Valente EM., Abou-Sleiman PM., Caputo V., Mugit MM., Harvey K., Gispert S., Ali Z., del Turco D., Bentivoglio AR., Healy DG., Albanese A., Nussbaum R., Gonzalez-Maldonado R., Deller T., Salvi S., Cortelli P., Gilks WP., Latchman DS., Harvey RJ., Dallapiccola B., Auburger G., and Wood NW.

Subjects
Leupeptins, Nonsense mutation, Molecular Sequence Data, Mutation, Missense, PINK1, Substantia nigra, Apoptosis, Biology, Transfection, Parkin, Membrane Potentials, chemistry.chemical_compound, PINK 1, Cell Line, Tumor, medicine, Missense mutation, Animals, Humans, Amino Acid Sequence, Genetics, Alpha-synuclein, Neurons, Multidisciplinary, Neurodegeneration, PARK7, Parkinson Disease, Exons, medicine.disease, Mitochondria, Protein Structure, Tertiary, GENETICA, Oxidative Stress, chemistry, Codon, Nonsense, COS Cells, Mutation, PARKINSON, Protein Kinases
Abstract

Parkinson's disease (PD) is a neurodegenerative disorder characterized by degeneration of dopaminergic neurons in the substantia nigra. We previously mapped a locus for a rare familial form of PD to chromosome 1p36 (PARK6). Here we show that mutations in PINK1 (PTEN-induced kinase 1) are associated with PARK6. We have identified two homozygous mutations affecting the PINK1 kinase domain in three consanguineous PARK6 families: a truncating nonsense mutation and a missense mutation at a highly conserved amino acid. Cell culture studies suggest that PINK1 is mitochondrially located and may exert a protective effect on the cell that is abrogated by the mutations, resulting in increased susceptibility to cellular stress. These data provide a direct molecular link between mitochondria and the pathogenesis of PD.

Published
2004

Catalog

Books, media, physical & digital resources
See catalog results