Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein folding
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Structure of TSA2 reveals novel features of the active-site loop of peroxiredoxinsCytoplasmic HSP90α expression is associated with perineural invasion in pancreatic cancer.High expression of peroxiredoxin 4 affects the survival time of colorectal cancer patients, but is not an independent unfavorable prognostic factor.Thiol-disulfide exchange between the PDI family of oxidoreductases negates the requirement for an oxidase or reductase for each enzymeA novel reaction of peroxiredoxin 4 towards substrates in oxidative protein folding.Prdx4 is a compartment-specific H2O2 sensor that regulates neurogenesis by controlling surface expression of GDE2.Overexpression of Peroxiredoxin 4 Affects Intestinal Function in a Dietary Mouse Model of Nonalcoholic Fatty Liver Disease.Redox reactions in mammalian spermatogenesis and the potential targets of reactive oxygen species under oxidative stressArabidopsis protein disulfide isomerase-8 is a type I endoplasmic reticulum transmembrane protein with thiol-disulfide oxidase activity.Adiporedoxin, an upstream regulator of ER oxidative folding and protein secretion in adipocytes.Cysteines 208 and 241 in Ero1α are required for maximal catalytic turnoverAdverse Outcomes Associated with Cigarette Smoke Radicals Related to Damage to Protein-disulfide IsomeraseCalredoxin represents a novel type of calcium-dependent sensor-responder connected to redox regulation in the chloroplastDestroy and exploit: catalyzed removal of hydroperoxides from the endoplasmic reticulumTwo phases of disulfide bond formation have differing requirements for oxygen.Going through the barrier: coupled disulfide exchange reactions promote efficient catalysis in quiescin sulfhydryl oxidaseLack of an efficient endoplasmic reticulum-localized recycling system protects peroxiredoxin IV from hyperoxidation.Biochemical evidence that regulation of Ero1β activity in human cells does not involve the isoform-specific cysteine 262.Oxidative protein folding: from thiol-disulfide exchange reactions to the redox poise of the endoplasmic reticulum.TXNDC5, a newly discovered disulfide isomerase with a key role in cell physiology and pathology.Thioredoxin superfamily and its effects on cardiac physiology and pathology.Extracellular Thiol Isomerases and Their Role in Thrombus FormationPDI is an essential redox-sensitive activator of PERK during the unfolded protein response (UPR)Identification and characterization of GmPDIL7, a soybean ER membrane-bound protein disulfide isomerase family protein.Comparison of inter- and intraspecies variation in humans and fruit flies.Peroxiredoxin 1 interacts with and blocks the redox factor APE1 from activating interleukin-8 expression.Differential activity of rice protein disulfide isomerase family members for disulfide bond formation and reduction.Structural basis of pH-dependent client binding by ERp44, a key regulator of protein secretion at the ER-Golgi interface.Peroxiredoxin 4 improves insulin biosynthesis and glucose-induced insulin secretion in insulin-secreting INS-1E cells.Inhibition of the functional interplay between endoplasmic reticulum (ER) oxidoreduclin-1α (Ero1α) and protein-disulfide isomerase (PDI) by the endocrine disruptor bisphenol A.Human ER Oxidoreductin-1α (Ero1α) Undergoes Dual Regulation through Complementary Redox Interactions with Protein-Disulfide Isomerase.Cooperative Protein Folding by Two Protein Thiol Disulfide Oxidoreductases and 1 in Soybean.Chemistry and Enzymology of Disulfide Cross-Linking in Proteins.Misfolded proinsulin in the endoplasmic reticulum during development of beta cell failure in diabetes.Peroxiredoxin 4 (PRDX4): Its critical in vivo roles in animal models of metabolic syndrome ranging from atherosclerosis to nonalcoholic fatty liver disease.Polyamine Metabolism and Oxidative Protein Folding in the ER as ROS-Producing Systems Neglected in Virology.Mutual interaction between oxidative stress and endoplasmic reticulum stress in the pathogenesis of diseases specifically focusing on non-alcoholic fatty liver disease
P2860
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P2860
Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein folding
description
2013 nî lūn-bûn
@nan
2013 թուականին հրատարակուած գիտական յօդուած
@hyw
2013 թվականին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Synergistic cooperation of PDI ...... iven oxidative protein folding
@ast
Synergistic cooperation of PDI ...... iven oxidative protein folding
@en
Synergistic cooperation of PDI ...... iven oxidative protein folding
@nl
type
label
Synergistic cooperation of PDI ...... iven oxidative protein folding
@ast
Synergistic cooperation of PDI ...... iven oxidative protein folding
@en
Synergistic cooperation of PDI ...... iven oxidative protein folding
@nl
prefLabel
Synergistic cooperation of PDI ...... iven oxidative protein folding
@ast
Synergistic cooperation of PDI ...... iven oxidative protein folding
@en
Synergistic cooperation of PDI ...... iven oxidative protein folding
@nl
P2093
P2860
P3181
P356
P1433
P1476
Synergistic cooperation of PDI ...... iven oxidative protein folding
@en
P2093
Ken-ichi Maegawa
Kenji Inaba
Mamoru Suzuki
Masaki Okumura
Masatoshi Hagiwara
Masatoshi Saiki
Rieko Kojima
Shoji Masui
Tomohisa Horibe
Yoshimi Sato
P2860
P2888
P3181
P356
10.1038/SREP02456
P407
P577
2013-01-01T00:00:00Z
P5875
P6179
1023128574