ArticlePloS one2014
Compact conformations of human protein disulfide isomerase.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 34 citations in OpenAlex.
- Article
- Mechanistic basis of activation and inhibition of protein disulfide isomerase by allosteric antithrombotic compounds.Journal of thrombosis and haemostasis : JTH · 2025Article
- Exploring the Influence of Zinc Ions on the Conformational Stability and Activity of Protein Disulfide Isomerase.International journal of molecular sciences · 2024Article
- Molecular Design of FRET Probes Based on Domain Rearrangement of Protein Disulfide Isomerase for Monitoring Intracellular Redox Status.International journal of molecular sciences · 2023Article
- Oxidative Cysteine Modification of Thiol Isomerases in Thrombotic Disease: A Hypothesis.Antioxidants & redox signaling · 2021Review
- PDI-Regulated Disulfide Bond Formation in Protein Folding and Biomolecular Assembly.Molecules (Basel, Switzerland) · 2020Review
- Phosphorylation switches protein disulfide isomerase activity to maintain proteostasis and attenuate ER stress.The EMBO journal · 2020Article
- Article
- Stability and Conformational Resilience of Protein Disulfide Isomerase.Biochemistry · 2019Article
- An amebic protein disulfide isomerase (PDI) complements the yeast PDI1 mutation but is unable to support cell viability under ER or thermal stress.FEBS open bio · 2018Article
- '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
- The flexibility and dynamics of protein disulfide isomerase.Proteins · 2016Article
- Multivalency in the inhibition of oxidative protein folding by arsenic(III) species.Biochemistry · 2015Article
- S-nitrosylation of the thioredoxin-like domains of protein disulfide isomerase and its role in neurodegenerative conditions.Frontiers in chemistry · 2015Review
- Deciphering a proteomic signature for the early detection of breast cancer from breast milk: the role of quantitative proteomics.Expert review of proteomicsReview
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein disulfide isomerase (PDI) composed of four thioredoxin-like domains a, b, b', and a', is a key enzyme catalyzing oxidative protein folding in the endoplasmic reticulum. Large scale molecular dynamics simulations starting from the crystal structures of human PDI (hPDI) in the oxidized and reduced states were performed. The results indicate that hPDI adopts more compact conformations in solution than in the crystal structures, which are stabilized primarily by inter-domain interactions, including the salt bridges between domains a and b' observed for the first time. A prominent feature of the compact conformations is that the two catalytic domains a and a' can locate close enough for intra-molecular electron transfer, which was confirmed by the characterization of an intermediate with a disulfide between the two domains. Mutations, which disrupt the inter-domain interactions, lead to decreased reductase activity of hPDI. Our molecular dynamics simulations and biochemical experiments reveal the intrinsic conformational dynamics of hPDI and its biological impact.
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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.