ArticleProteins2016
The flexibility and dynamics of protein disulfide isomerase.
Article in Proteins, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers, 1 of them a synthesis that pooled it.
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Who cites it
13 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Unveiling the thioredoxin fold: a systematic review and bioinformatic analysis of protein disulfide isomerase and Dsb family proteins.Frontiers in bioinformatics · 2026Pooled it
- Structural characterization of OsPDIL2-3, a rice protein disulfide isomerase involved in prolamin accumulation.The Biochemical journal · 2026Article
- Thiol Isomerases: Enzymatic Mechanisms, Models of Oxidation, and Antagonism by Galloylated Polyphenols.Antioxidants (Basel, Switzerland) · 2025Review
- Probing the conformational dynamics of thiol-isomerases using non-canonical amino acids and single-molecule FRET.Methods (San Diego, Calif.) · 2023Article
- A Comparative Analysis of Punicalagin Interaction with PDIA1 and PDIA3 by Biochemical and Computational Approaches.Biomedicines · 2021Article
- Flexibility and mobility of SARS-CoV-2-related protein structures.Scientific reports · 2021Article
- Bioorthogonal Chemistry Enables Single-Molecule FRET Measurements of Catalytically Active Protein Disulfide Isomerase.Chembiochem : a European journal of chemical biology · 2021Article
- Mechanisms of Disulfide Bond Formation in Nascent Polypeptides Entering the Secretory Pathway.Cells · 2020Review
- Stability and Conformational Resilience of Protein Disulfide Isomerase.Biochemistry · 2019Article
- Article
- 'Something in the way she moves': The functional significance of flexibility in the multiple roles of protein disulfide isomerase (PDI).Biochimica et biophysica acta. Proteins and proteomics · 2017Review
- Advances in vascular thiol isomerase function.Current opinion in hematology · 2017Review
- Machine Learning and Network Analysis of Molecular Dynamics Trajectories Reveal Two Chains of Red/Ox-specific Residue Interactions in Human Protein Disulfide Isomerase.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
We have studied the mobility of the multidomain folding catalyst, protein disulfide isomerase (PDI), by a coarse-graining approach based on flexibility. We analyze our simulations of yeast PDI (yPDI) using measures of backbone movement, relative positions and orientations of domains, and distances between functional sites. We find that there is interdomain flexibility at every interdomain junction but these show very different characteristics. The extent of interdomain flexibility is such that yPDI's two active sites can approach much more closely than is found in crystal structures-and indeed hinge motion to bring these sites into proximity is the lowest energy normal mode of motion of the protein. The flexibility predicted for yPDI (based on one structure) includes the other known conformation of yPDI and is consistent with (i) the mobility observed experimentally for mammalian PDI and (ii) molecular dynamics. We also observe intradomain flexibility and clear differences between the domains in their propensity for internal motion. Our results suggest that PDI flexibility enables it to interact with many different partner molecules of widely different sizes and shapes, and highlights considerable similarities of yPDI and mammalian PDI. Proteins 2016; 84:1776-1785. © 2016 Wiley Periodicals, Inc.
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