Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Eric Wildfang"'
Autor:
Melanie M. Ivancic, Alexey Eroshkin, Eric Wildfang, Guy S. Salvesen, Mari Enoksson, W. Andy Tao, Jingwei Li, John C. Timmer
Publikováno v:
Journal of Proteome Research. 6:2850-2858
The identification of natural substrates and their cleavage sites is pivotal to defining proteolytic pathways. Here we report a novel strategy for the identification of the signature of proteolytic cleavage events based on quantitative proteomics. Ly
Publikováno v:
Toxicology. 168:213-221
Inorganic arsenic is an important environmental toxicant of both natural and anthropogenic sources. It is a human carcinogen for which appropriate animal models of most arsenic-induced cancers are missing. Although methylation of inorganic arsenic ha
Publikováno v:
Toxicology and Applied Pharmacology. 140:77-84
Methylation of inorganic arsenic to methylarsonic acid (MMA) and dimethylarsinic acid (DMA) has been considered to be the major pathway of inorganic arsenic biotransformation and detoxification. Comparative studies, in vivo, have demonstrated variati
Autor:
W. Andy Tao, John C. Timmer, Mari Enoksson, Eric Wildfang, Yie-Hwa Chang, Yoshinobu Igarashi, Guy S. Salvesen, Benjamin Dummitt, Alexey Eroshkin, Jeffrey W. Smith, Alan E. Mast, Wenhong Zhu, Yuliang Ma, Jean-Benard Denault
Publikováno v:
The Biochemical journal. 407(1)
Most known organisms encode proteases that are crucial for constitutive proteolytic events. In the present paper, we describe a method to define these events in proteomes from Escherichia coli to humans. The method takes advantage of specific N-termi
Autor:
Eric Wildfang, Guy S. Salvesen, Henning R. Stennicke, Scott J. Snipas, Kelly M. Boatright, Tamim Nazif, Matthew Bogyo, Leif Christensen
Publikováno v:
Biological Chemistry. 385
Human paracaspase has been predicted to be a member of the protein structural fold that encompasses protease clan CD. To determine whether paracaspase has catalytic activity we have expressed the region corresponding to the catalytic domain and used
Autor:
Philip G. Board, Mary M. Aposhian, Jay S. Petrick, Robert A. Zakharyan, Eric Wildfang, Dean E. Carter, Adriana Sampayo-Reyes, H. Vasken Aposhian, D.N. Guha Mazumder, Sheila M. Healy
Publisher Summary The biotransformation of inorganic arsenate to dimethylarsinic acid (DMA) involves a series of enzymatic steps. Recent studies based on amino acid homology and other properties demonstrate that the human liver arsenate reductase and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::188ca203d0c1f868d5239626c1137ea6
https://doi.org/10.1016/b978-044451441-7/50018-x
https://doi.org/10.1016/b978-044451441-7/50018-x
Autor:
Mary M. Aposhian, Jürgen Gailer, Timothy R. Radabaugh, LaTanya A. Powell, Sheila M. Healy, Gregory M. Bogdan, Robert A. Zakharyan, H. Vasken Aposhian, Eric Wildfang
Publisher Summary Arsenate is reduced to arsenite enzymatically by arsenate reductase and nonenzymatically by GSH. An early step in the detoxification appears to be the formation of the Gailer compound, seleno-bis(S-glutathionyl) arsinium ion, which
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9069112afb38f7ac4a934539ce7e153b
https://doi.org/10.1016/b978-008043648-7/50033-9
https://doi.org/10.1016/b978-008043648-7/50033-9
Autor:
Mari Enoksson, Jingwei Li, Melanie M. Ivancic, John C. Timmer, Eric Wildfang, Alexey Eroshkin, Guy S. Salvesen, W. Andy Tao
Publikováno v:
Journal of Proteome Research; Jul2007, Vol. 6 Issue 7, p2850-2858, 9p