The Crystal Structure of Yeast Protein Disulfide Isomerase Suggests Cooperativity between Its Active Sites
TLDR
Biochemical studies demonstrate that all domains of PDI, including the C-terminal tail, are required for full catalytic activity and defines a framework for rationalizing the differences between the two active sites and their respective roles in catalyzing the formation and rearrangement of disulfide bonds.About:
This article is published in Cell.The article was published on 2006-01-13 and is currently open access. It has received 379 citations till now. The article focuses on the topics: Protein disulfide-isomerase & Protein Disulfide-Isomerase Family.read more
Citations
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In and Out of the ER: Protein Folding, Quality Control, Degradation, and Related Human Diseases
TL;DR: Cellular and organismal homeostasis relies on a balanced activity of the ER folding, quality control, and degradation machineries as shown by the dozens of human diseases related to defective maturation or disposal of individual polypeptides generated in the ER.
Journal ArticleDOI
Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation.
Feras Hatahet,Lloyd W. Ruddock +1 more
TL;DR: This review aims to provide background on the chemistry of disulfide bond formation and rearrangement, including the concept of reduction potential, before examining the structure of PDI and discuss other human and yeast PDI-family members.
Journal ArticleDOI
The endoplasmic reticulum: folding, calcium homeostasis, signaling, and redox control.
TL;DR: Redox homeostasis appears to be a prerequisite for proper functioning of the ER, and a close relationship exists between oxidative stress and ER stress, which both may activate signaling events leading to a rebalance of folding capacity and folding demand or to cell death.
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Prolyl 4-hydroxylase
Kelly L. Gorres,Ronald T. Raines +1 more
TL;DR: The enzymic catalysts of prolyl hydroxylation are reviewed, along with the chemical and biochemical consequences of this subtle but abundant posttranslational modification.
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The human PDI family: Versatility packed into a single fold
TL;DR: The diversity of cellular functions described for the human PDIs is explored, which emphasizes as much their differences as their similarities, and underlines the versatility of the thioredoxin fold.
References
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Processing of X-ray diffraction data collected in oscillation mode
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Analysis of membrane and surface protein sequences with the hydrophobic moment plot.
TL;DR: An algorithm has been developed which identifies alpha-helices involved in the interactions of membrane proteins with lipid bilayers and which distinguishes them from helices in soluble proteins, and suggests four transmembrane helices and a surface-seeking helix in fragment B, the moiety known to have trans Membrane function.
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TL;DR: A suite of programs, PROMOTIF, that analyzes a protein coordinate file and provides details about the structural motifs in the protein, and can also be used to compare motifS in a group of related structures, such as an ensemble of NMR structures.
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