Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Hugo D. Urbina"'
Autor:
Weijia Ou, Hugo D. Urbina, Reynand Pacoma, Jennifer L. Harris, Alana Althage, Daniel E. Mason, Andrew M. Schumacher, Juliano Alves, Gus Welzel, Tove Tuntland, Eric C. Peters, James Watson, Laura H. Jacobson, Bo Liu, John R. Walker
Publikováno v:
The Journal of Neuroscience. 33:2457-2464
Accumulation of β-amyloid (Aβ) in the brain is believed to contribute to the pathology of Alzheimer's Disease (AD). Aβ levels are controlled by the production of Aβ from amyloid precursor protein, degradation by proteases, and peripheral clearanc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb911df5ff3244ba5dd8aed4883288c1
https://doi.org/10.1523/jneurosci.3407-12.2013
https://doi.org/10.1523/jneurosci.3407-12.2013
Autor:
François Debaene, Jennifer L. Harris, Nicolas Winssinger, Daniel E. Mason, Hugo D. Urbina, Bernard Jost, Christine Bole-Feysot, Petr Kuzmic
Publikováno v:
ChemBioChem, Vol. 7, No 11 (2006) pp. 1790-1797
Small-molecule microarrays are attractive for chemical biology as they permit the analysis of hundreds to thousands of interactions in a highly miniaturized format. Methods to prepare small-molecule microarrays from combinatorial libraries by a self-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::468f259fab7aecf8c65f502a29abd790
https://doi.org/10.1002/cbic.200600242
https://doi.org/10.1002/cbic.200600242
Publikováno v:
Journal of Biological Chemistry. 279:19551-19558
IscS catalyzes the fragmentation of l-cysteine to l-alanine and sulfane sulfur in the form of a cysteine persulfide in the active site of the enzyme. In Escherichia coli IscS, the active site cysteine Cys(328) resides in a flexible loop that potentia
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3409ff8f63e62ca77b4101a42e3748a1
https://doi.org/10.1074/jbc.m401261200
https://doi.org/10.1074/jbc.m401261200
Publikováno v:
Journal of Molecular Biology. 330:1049-1059
IscS is a widely distributed cysteine desulfurase that catalyzes the pyridoxal phosphate-dependent desulfuration of L-cysteine and plays a central role in the delivery of sulfur to a variety of metabolic pathways. We report the crystal structure of E
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92eac8fb18bda48d0bcddc94b08df52b
https://doi.org/10.1016/s0022-2836(03)00690-9
https://doi.org/10.1016/s0022-2836(03)00690-9
Publikováno v:
Journal of Biological Chemistry. 276:44521-44526
The cysteine desulfurase enzymes NifS and IscS provide sulfur for the biosynthesis of Fe/S proteins. NifU and IscU have been proposed to serve as template or scaffold proteins in the initial Fe/S cluster assembly events, but the mechanism of sulfur t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::06ef94da61c690619d5184bcd5f4527d
https://doi.org/10.1074/jbc.m106907200
https://doi.org/10.1074/jbc.m106907200
Autor:
Lawrence E. Whipple, Mark A Wall, Adrienne Huston Davenport, Andrey Mirakyan, Bin Zhang, Richard D. Hutchins, Hugo D Urbina, Kenneth Barrett
Publikováno v:
All Days.
Summary Enzyme breakers have been previously used for hydrolyzing guar gels at temperatures below 150°F. There is an industry-wide demand for enzyme breakers that can function under higher-temperature (200–250°F) and extreme pH (≥10.5) conditio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f3bcea15d36c81b53b846df7b304edb
https://doi.org/10.2118/160033-ms
https://doi.org/10.2118/160033-ms
Autor:
Catherine Daguia, Hugo D. Urbina, Truc Huynh, Jeremy S. Caldwell, Ingo H. Engels, Achim Brinker, Andrew M. Schumacher, Jörg Buddenkotte
Publikováno v:
Analytical biochemistry. 390(1)
Neural precursor cell expressed, developmentally down-regulated gene 8 (NEDD8) is a recently discovered ubiquitin-like posttranslational modifier. NEDD8 acts predominantly as a regulator of ubiquitin-protein ligases and as a decoy for proteins target
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e9093d40b14757b6f8e3e6b4d667fce0
https://pubmed.ncbi.nlm.nih.gov/19328766
https://pubmed.ncbi.nlm.nih.gov/19328766
Autor:
Hugo D. Urbina, Hong Liu, Jun Li, Christine Tumanut, Robert Epple, Jennifer L. Harris, Daniel E. Mason, Badry Bursulaya, Ross Russo
Publikováno v:
Bioorganicmedicinal chemistry letters. 17(5)
A 6-oxa-1-aza-bicyclo[3.2.1]octan-7-one system inhibits the proteolytic activity of several cysteine proteases belonging to the papain family. In vitro mechanistic studies and in silico calculations suggest that the minimal pi-overlap between the bri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51bc4a6480bf9e8d8b8c276248a44f77
https://pubmed.ncbi.nlm.nih.gov/17196818
https://pubmed.ncbi.nlm.nih.gov/17196818
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 58(Pt 7)
IscS is a widely distributed cysteine desulfurase that catalyzes the pyridoxal phosphate dependent beta-elimination of sulfur from L-cysteine and plays a central role in the delivery of sulfur to a variety of metabolic pathways. Crystals of Escherich
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7daf6b3306213048a08d96943f564f96
https://pubmed.ncbi.nlm.nih.gov/12077450
https://pubmed.ncbi.nlm.nih.gov/12077450
Autor:
Hugo D. Urbina, François Debaene, Bernard Jost, Christine Bole-Feysot, Daniel E. Mason, Petr Kuzmic, Jennifer L. Harris, Nicolas Winssinger
Publikováno v:
ChemBioChem; Nov2006, Vol. 7 Issue 11, p1790-1797, 8p