نتایج جستجو برای: protein disulfide isomerase

تعداد نتایج: 1249610  

Journal: :American Journal of Physiology-Lung Cellular and Molecular Physiology 2002

Journal: :The Journal of biological chemistry 2009
Silvia A Arredondo Tiffany F Chen Austen F Riggs Hiram F Gilbert George Georgiou

The bacterial protein-disulfide isomerase DsbC is a homodimeric V-shaped enzyme that consists of a dimerization domain, two alpha-helical linkers, and two opposing thioredoxin fold catalytic domains. The functional significance of the two catalytic domains of DsbC is not well understood yet. We have engineered heterodimer-like DsbC derivatives covalently linked via (Gly(3)-Ser) flexible linkers...

Journal: :Molecular cell 1999
A R Frand C A Kaiser

Native protein disulfide bond formation in the endoplasmic reticulum (ER) requires protein disulfide isomerase (PDI) and Ero1p. Here we show that oxidizing equivalents flow from Ero1p to substrate proteins via PDI. PDI is predominantly oxidized in wild-type cells but is reduced in an ero1-1 mutant. Direct dithiol-disulfide exchange between PDI and Ero1p is indicated by the capture of PDI-Ero1p ...

2009
Guoping Ren Daniel Stephan Zhaohui Xu Ying Zheng Danming Tang Rosemary S. Harrison Mareike Kurz Russell Jarrott Stephen R. Shouldice Annie Hiniker Jennifer L. Martin James C. A. Bardwell

The thioredoxin fold is the core scaffold of numerous proteins that control disulfide redox activity in the cell (1–3). These redox proteins share very little sequence homology, but all of them incorporate the four-stranded -sheet, three flanking -helices, and the redox-active CXXC motif of the TRX5 fold (Fig. 1A). The archetype of the family is thioredoxin (4), a disulfide reductase thatmainta...

Journal: :The Journal of biological chemistry 1995
M C Laboissiere S L Sturley R T Raines

Protein-disulfide isomerase (PDI) is an abundant protein of the endoplasmic reticulum that catalyzes dithiol oxidation and disulfide bond reduction and isomerization using the active site CGHC. Haploid pdi1 delta Saccharomyces cerevisiae are inviable, but can be complemented with either a wild-type rat PDI gene or a mutant gene coding for CGHS PDI (shufflease). In contrast, pdi1 delta yeast can...

2011
Yayoi Onda Yasushi Kawagoe

During seed development, endosperm cells of highly productive cereals, including rice, synthesize disulfide-rich proteins in large amounts and deposit them into storage organelles. Disulfide bond formation involves electron transfer and generates H(2)O(2) as a by-product. To ensure proper development and maturation of seeds, the endosperm cells must supply large amounts of oxidizing equivalents...

2016
Huijun Gao Bing Sun Hailu Fu Xinming Chi Faming Wang Xiaoyu Qi Jun Hu Shujuan Shao

Protein disulfide isomerase family 6 (PDIA6) belongs to the protein disulfide isomerase (PDI) family, which function as isomerases and molecular chaperones. PDIA6 has recently been shown to promote the proliferation and growth of various types of human cancer cells; however the underlying molecular mechanism remains elusive. Here, we report that PDIA6 enhances the proliferation of HeLa cells th...

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