ReviewBiochimica et biophysica acta. Proteins and proteomics2017
'Something in the way she moves': The functional significance of flexibility in the multiple roles of protein disulfide isomerase (PDI).
Review in Biochimica et biophysica acta. Proteins and proteomics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
27 citing papers in PubMed.
- Luminespib and AZ5104 are effective antithrombotic drugs via targeting the platelet Ero1α-PDI pathway.Science advances · 2026Article
- Protein disulfide isomerase dissolves and detoxifies oligomeric assemblies of amyloid beta peptide.FEBS letters · 2026Article
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- Article
- Preparation of PLA Nanoparticles and Study of Their Influencing Factors.Molecules (Basel, Switzerland) · 2024Article
- Analysis of Punicalin and Punicalagin Interaction with PDIA3 and PDIA1.International journal of molecular sciences · 2024Article
- Discovery of 5-Hydroxy-1,4-naphthoquinone (Juglone) Derivatives as Dual Effective Agents Targeting Platelet-Cancer Interplay through Protein Disulfide Isomerase Inhibition.Journal of medicinal chemistry · 2024Article
- Probing the conformational dynamics of thiol-isomerases using non-canonical amino acids and single-molecule FRET.Methods (San Diego, Calif.) · 2023Article
- Functions and mechanisms of protein disulfide isomerase family in cancer emergence.Cell & bioscience · 2022Review
- Holotoxin disassembly by protein disulfide isomerase is less efficient for Escherichia coli heat-labile enterotoxin than cholera toxin.Scientific reports · 2022Article
- A 200 nanoseconds all-atom simulation of the pH-dependent EF loop transition in bovine β-lactoglobulin. The role of the orientation of the E89 side chain.Journal of biomolecular structure & dynamics · 2022Article
- A Comparative Analysis of Punicalagin Interaction with PDIA1 and PDIA3 by Biochemical and Computational Approaches.Biomedicines · 2021Article
- Protein Aggregation in the Pathogenesis of Ischemic Stroke.Cellular and molecular neurobiology · 2021Review
- Flexibility and mobility of SARS-CoV-2-related protein structures.Scientific reports · 2021Article
- Label-free proteomic analysis of serum exosomes from paroxysmal atrial fibrillation patients.Clinical proteomics · 2021Article
- Bioorthogonal Chemistry Enables Single-Molecule FRET Measurements of Catalytically Active Protein Disulfide Isomerase.Chembiochem : a European journal of chemical biology · 2021Article
- In case of stress, hold tight: phosphorylation switches PDI from an oxidoreductase to a holdase, tuning ER proteostasis.The EMBO journal · 2020Article
- Disulfide isomerase ERp57 improves the stability and immunogenicity of H3N2 influenza virus hemagglutinin.Virology journal · 2020Article
- Proteome of the Triatomine Digestive Tract: From Catalytic to Immune Pathways; Focusing on Annexin Expression.Frontiers in molecular biosciences · 2020Article
- Weighted Gene Co-expression Network Analysis Identifies Critical Genes for the Production of Cellulase and Xylanase inFrontiers in microbiology · 2020Article
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
Protein disulfide isomerase (PDI) has diverse functions in the endoplasmic reticulum as catalyst of redox transfer, disulfide isomerization and oxidative protein folding, as molecular chaperone and in multi-subunit complexes. It interacts with an extraordinarily wide range of substrate and partner proteins, but there is only limited structural information on these interactions. Extensive evidence on the flexibility of PDI in solution is not matched by any detailed picture of the scope of its motion. A new rapid method for simulating the motion of large proteins provides detailed molecular trajectories for PDI demonstrating extensive changes in the relative orientation of its four domains, great variation in the distances between key sites and internal motion within the core ligand-binding domain. The review shows that these simulations are consistent with experimental evidence and provide insight into the functional capabilities conferred by the extensive flexible motion of PDI.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.