نتایج جستجو برای: protein disulfide isomerase

تعداد نتایج: 1249610  

Journal: :Trends in biochemical sciences 2004
Annie Hiniker James C A Bardwell

The essential flavoenzyme Ero1p both creates de novo disulfide bonds and transfers these disulfides to the folding catalyst protein disulfide isomerase (PDI). The recently solved crystal structure of Ero1p, in combination with previous biochemical, genetic and structural data, provides insight into the mechanism by which Ero1p accomplishes these tasks. A comparison of Ero1p with the smaller fla...

Journal: :The Journal of biological chemistry 2006
Mohini S Kulp Eva-Maria Frickel Lars Ellgaard Jonathan S Weissman

Native disulfide bond formation in eukaryotes is dependent on protein-disulfide isomerase (PDI) and its homologs, which contain varying combinations of catalytically active and inactive thioredoxin domains. However, the specific contribution of PDI to the formation of new disulfides versus reduction/rearrangement of non-native disulfides is poorly understood. We analyzed the role of individual ...

Journal: :The Journal of biological chemistry 1996
M Ostermeier K De Sutter G Georgiou

Eukaryotic protein disulfide isomerase (PDI) is a 55-kDa enzyme with cysteine oxidoreductase, chaperone, and antichaperone activities that catalyzes disulfide formation and rearrangement in the eukaryotic endoplasmic reticulum. In Gram-negative bacteria, the formation of disulfide bonds in the periplasm is mediated by DsbA, a strong cysteine oxidase but an inefficient catalyst of disulfide bond...

پایان نامه :دانشگاه آزاد اسلامی - دانشگاه آزاد اسلامی واحد علوم دارویی - دانشکده زیست شناسی 1392

مقدمه: scfv یکی از معروفترین قطعات حاصل از آنتی بادیهای تک دودمانی است و مخمر pichia pastoris یکی از مهمترین میزبان های بیانی اینگونه قطعات محسوب می شود. روش های بسیاری برای افزایش میزان بیان پروتئین های هترولوگ در این میزبان وجود دارد .باتوجه به اینکه فرایند تغییرات پس از ترجمه ای در شبکه آندوپلاسمی مرحله تعیین کننده سرعت در تولید پروتئین هاست، هدف قرار دادن چاپرون هایی نظیر pdi (protein disul...

Journal: :The Journal of biological chemistry 2000
M W Bader T Xie C A Yu J C Bardwell

The chemistry of disulfide exchange in biological systems is well studied. However, very little information is available concerning the actual origin of disulfide bonds. Here we show that DsbB, a protein required for disulfide bond formation in vivo, uses the oxidizing power of quinones to generate disulfides de novo. This is a novel catalytic activity, which to our knowledge has not yet been d...

Journal: :FEBS letters 1997
J Monnat U Hacker H Geissler R Rauchenberger E M Neuhaus M Maniak T Soldati

The primary activity of protein disulfide isomerase (PDI), a multifunctional resident of the endoplasmic reticulum (ER), is the isomerization of disulfide bridges during protein folding. We isolated a cDNA encoding Dictyostelium discoideum PDI (Dd-PDI). Phylogenetic analyses and basic biochemical properties indicate that it belongs to a subfamily called P5, many members of which differ from the...

Journal: :Functional food science 2023

Background: Stomach ulcer is one of the diseases that many patients suffer from all over world, and it causes damage to intestinal wall. Some research has shown Bauhinia thonningii extract, which been traditionally used treat a variety ailments, including stomach ulcers, powerful antioxidant mucus-increasing properties. Objective:This aimed at studying mechanism(s) through methanolic (MBST) chl...

2017
Ri-He Peng Jin Qiu Yong-Sheng Tian Jian-jie Gao Hong-juan Han Xiao-Yan Fu Bo Zhu Jing Xu Bo Wang Zhen-jun Li Li-juan Wang Quan-Hong Yao

Trichlorophenol (TCP) is a widely used and persistent environmentally toxic compound that poses a carcinogenic risk to humans. Phytoremediation is a proficient cleanup technology for organic pollutants. In this study, we found that the disulfide isomerase-like protein AtPDIL1-2 in plants is a good candidate for enhancing 2,4,6-TCP phytoremediation. The expression of AtPDIL1-2 in Arabidopsis was...

2001
Martin Bader Winfried Boos James Bardwell Michael Ehrmann

8 3.1. Catalysis of oxidative protein folding 8 3.2 De novo formation of disulfide bonds in E. coli: the discovery of DsbA 9 3.3. DsbA is the most oxidizing disulfide catalyst 11 3.4. DsbB provides the periplasm with oxidizing power 15 3.5. Correcting wrong disulfide bonds in the periplasm: disulfide bond isomerization by DsbC 18 3.6. DsbD provides reducing equivalents in a highly oxidizing env...

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