Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Abigail I Guce"'
Autor:
Michael J. Maroney, Olivia E. Johnson, Scott C. Garman, Thomas C. Brunold, Abigail I. Guce, Diane E. Cabelli, Kelly C. Ryan
Publikováno v:
Biochemistry. 54:1016-1027
Crystal structures of nickel-dependent superoxide dismutases (NiSODs) reveal the presence of a H-bonding network formed between the NH group of the apical imidazole ligand from His1 and the Glu17 carboxylate from a neighboring subunit in the hexameri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::144a91000d347f82be32023823b090fa
https://doi.org/10.1021/bi501258u
https://doi.org/10.1021/bi501258u
Autor:
Sascha Lange, Marissa Bylsma, Marek Wieczorek, Abigail I Guce, Christian Freund, Lawrence J. Stern, Elizabeth D. Mellins, Liusong Yin, Wei Jiang, Peter Trenh, Jana Sticht
Publikováno v:
Journal of Biological Chemistry. 289:23449-23464
HLA-DM mediates the exchange of peptides loaded onto MHCII molecules during antigen presentation by a mechanism that remains unclear and controversial. Here, we investigated the sequence and structural determinants of HLA-DM interaction. Peptides int
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::20063027393aee8253195f6895ec7791
https://doi.org/10.1074/jbc.m114.585539
https://doi.org/10.1074/jbc.m114.585539
Autor:
Corrie A. Painter, Wei Jiang, Taejin Yoon, Sarah Mortimer, Lawrence J. Stern, Abigail I Guce, Elizabeth D. Mellins
Publikováno v:
Nature structural & molecular biology
Mammalian class II major histocompatibility (MHCII) proteins bind peptide antigens in endosomal compartments of antigen-presenting cells. The nonclassical MHCII protein HLA-DM chaperones peptide-free MHCII, protecting it against inactivation, and cat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5faa05150548f63186f3cafa29af9d4d
https://doi.org/10.1038/nsmb.2460
https://doi.org/10.1038/nsmb.2460
Publikováno v:
Chemistry & Biology. 18:1521-1526
SummaryFabry disease patients show a deficiency in the activity of the lysosomal enzyme α-galactosidase (α-GAL or α-Gal A). One proposed treatment for Fabry disease is pharmacological chaperone therapy, where a small molecule stabilizes the α-GAL
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ffe1b09763882601e2ec74ab59802867
https://doi.org/10.1016/j.chembiol.2011.10.012
https://doi.org/10.1016/j.chembiol.2011.10.012
Autor:
Nathaniel E. Clark, Eric N. Salgado, Scott C. Garman, Dina R. Ivanen, Harry Brumer, Anna A. Kulminskaya, Abigail I. Guce
Publikováno v:
Journal of Biological Chemistry. 285:3625-3632
The enzyme alpha-galactosidase (alpha-GAL, also known as alpha-GAL A; E.C. 3.2.1.22) is responsible for the breakdown of alpha-galactosides in the lysosome. Defects in human alpha-GAL lead to the development of Fabry disease, a lysosomal storage diso
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e4ea5cc26521e545e74c92a7073d305
https://doi.org/10.1074/jbc.m109.060145
https://doi.org/10.1074/jbc.m109.060145
Publikováno v:
The FASEB Journal. 25
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f8a003cc7be92148a85381896061c066
https://doi.org/10.1096/fasebj.25.1_supplement.lb66
https://doi.org/10.1096/fasebj.25.1_supplement.lb66
Publikováno v:
The Journal of biological chemistry. 285(28)
The human lysosomal enzymes alpha-galactosidase (alpha-GAL, EC 3.2.1.22) and alpha-N-acetylgalactosaminidase (alpha-NAGAL, EC 3.2.1.49) share 46% amino acid sequence identity and have similar folds. The active sites of the two enzymes share 11 of 13
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97895534cf05581df84851cfcece5e89
https://pubmed.ncbi.nlm.nih.gov/20444686
https://pubmed.ncbi.nlm.nih.gov/20444686
Autor:
Abigail I. Guce, Scott C. Garman
Publikováno v:
Fabry Disease ISBN: 9789048190324
The three-dimensional structure of human α-galactosidase A has been determined by x-ray crystallography, revealing the molecular and mechanistic basis for the defects leading to Fabry disease. The structure showed that the active site of the enzyme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d04c7b12501dc58d20f22331ae801c47
https://doi.org/10.1007/978-90-481-9033-1_2
https://doi.org/10.1007/978-90-481-9033-1_2
Autor:
Michael J. Maroney, Abigail I. Guce, Kelly C. Ryan, Scott C. Garman, Khadine A. Higgins, Robert W. Herbst, Diane E. Cabelli, Peter A. Bryngelson
Superoxide dismutases rely on protein structural elements to adjust the redox potential of the metallocenter to an optimum value near 300 mV (vs NHE), to provide a source of protons for catalysis, and to control the access of anions to the active sit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4b0247d4ef7ad508a60c0ea49cbf2fe
https://europepmc.org/articles/PMC3690555/
https://europepmc.org/articles/PMC3690555/
Publikováno v:
Molecular Genetics and Metabolism. 108:S41-S42
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4bc6c2c01d1e06c9307892f49b47bf1f
https://doi.org/10.1016/j.ymgme.2012.11.091
https://doi.org/10.1016/j.ymgme.2012.11.091