ReviewEMBO reports2002
Protein disulfide isomerases exploit synergy between catalytic and specific binding domains.
Review in EMBO reports, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 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.
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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
53 citing papers in PubMed, 185 citations in OpenAlex.
- Design and Evaluation of Novel Peptides Targeting Protein Disulfide Isomerase as Antiplatelet Agents.Molecules (Basel, Switzerland) · 2026Article
- Structural characterization of OsPDIL2-3, a rice protein disulfide isomerase involved in prolamin accumulation.The Biochemical journal · 2026Article
- Defects inFrontiers in genetics · 2026Article
- Protein disulfide isomerase is essential for osteoblast differentiation in mice.Communications biology · 2025Article
- Decoding PDI diversity: Insights into structure, domains, and functionality in sorghum.Computational and structural biotechnology journal · 2025Article
- How Electricity Prevents Us from Bleeding to Death.Reviews of physiology, biochemistry and pharmacology · 2025Review
- Molecular Design of FRET Probes Based on Domain Rearrangement of Protein Disulfide Isomerase for Monitoring Intracellular Redox Status.International journal of molecular sciences · 2023Article
- Redox proteomics and structural analyses provide insightful implications for additional non-catalytic thiol-disulfide motifs in PDIs.Redox biology · 2023Article
- PDI-Regulated Disulfide Bond Formation in Protein Folding and Biomolecular Assembly.Molecules (Basel, Switzerland) · 2020Review
- Methylmercury-Mediated Oxidative Stress and Activation of the Cellular Protective System.Antioxidants (Basel, Switzerland) · 2020Review
- '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
- Kinetic-based trapping by intervening sequence variants of the active sites of protein-disulfide isomerase identifies platelet protein substrates.The Journal of biological chemistry · 2017Article
- The flexibility and dynamics of protein disulfide isomerase.Proteins · 2016Article
- A substrate-driven allosteric switch that enhances PDI catalytic activity.Nature communications · 2016Article
- Structural basis of redox-dependent substrate binding of protein disulfide isomerase.Scientific reports · 2015Article
- N-linked sugar-regulated protein folding and quality control in the ER.Seminars in cell & developmental biology · 2015Review
- Comparative proteome analysis of embryo and endosperm reveals central differential expression proteins involved in wheat seed germination.BMC plant biology · 2015Article
- Structural insight into substrate recognition by the endoplasmic reticulum folding-sensor enzyme: crystal structure of third thioredoxin-like domain of UDP-glucose:glycoprotein glucosyltransferase.Scientific reports · 2014Article
- Organocatalysts of oxidative protein folding inspired by protein disulfide isomerase.Organic & biomolecular chemistry · 2014Article
- 19F NMR spectroscopy monitors ligand binding to recombinantly fluorine-labelled b'x from human protein disulphide isomerase (hPDI).Organic & biomolecular chemistry · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein disulfide isomerases (PDIs) catalyse the formation of native disulfide bonds in protein folding pathways. The key steps involve disulfide formation and isomerization in compact folding intermediates. The high-resolution structures of the a and b domains of PDI are now known, and the overall domain architecture of PDI and its homologues can be inferred. The isolated a and a' domains of PDI are good catalysts of simple thiol-disulfide interchange reactions but require additional domains to be effective as catalysts of the rate-limiting disulfide isomerizations in protein folding pathways. The b' domain of PDI has a specific binding site for peptides and its binding properties differ in specificity between members of the PDI family. A model of PDI function can be deduced in which the domains function synergically: the b' domain binds unstructured regions of polypeptide, while the a and a' domains catalyse the chemical isomerization steps.
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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.