ArticleBiophysical journal2004
The unfolding action of GroEL on a protein substrate.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.
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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
20 citing papers in PubMed, 1 synthesis or guideline pooled it.
- How soluble misfolded proteins bypass chaperones at the molecular level.Nature communications · 2023Pooled it
- From Microstates to Macrostates in the Conformational Dynamics of GroEL: A Single-Molecule Förster Resonance Energy Transfer Study.The journal of physical chemistry letters · 2023Article
- Friends in need: How chaperonins recognize and remodel proteins that require folding assistance.Frontiers in molecular biosciences · 2022Review
- Chaperones convert the energy from ATP into the nonequilibrium stabilization of native proteins.Nature chemical biology · 2018Article
- Electric-Field-Induced Protein Translocation via a Conformational Transition in SecDF: An MD Study.Biophysical journal · 2017Article
- Substrate binding accelerates the conformational transitions and substrate dissociation in multidrug efflux transporter AcrB.Frontiers in microbiology · 2015Article
- Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis.Cell stress & chaperones · 2013Article
- Analysis and elimination of a bias in targeted molecular dynamics simulations of conformational transitions: application to calmodulin.The journal of physical chemistry. B · 2012Article
- Unfolding and translocation pathway of substrate protein controlled by structure in repetitive allosteric cycles of the ClpY ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Equilibrium sampling for biomolecules under mechanical tension.Biophysical journal · 2010Article
- The conformational transition pathway of ATP binding cassette transporter MsbA revealed by atomistic simulations.The Journal of biological chemistry · 2010Article
- CHARMM: the biomolecular simulation program.Journal of computational chemistry · 2009Review
- Allosteric transitions of supramolecular systems explored by network models: application to chaperonin GroEL.PLoS computational biology · 2009Article
- Polar or apolar--the role of polarity for urea-induced protein denaturation.PLoS computational biology · 2008Article
- Allostery and cooperativity revisited.Protein science : a publication of the Protein Society · 2008Review
- Allosteric transitions in the chaperonin GroEL are captured by a dominant normal mode that is most robust to sequence variations.Biophysical journal · 2007Article
- Coupling between allosteric transitions in GroEL and assisted folding of a substrate protein.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Glu257 in GroEL is a sensor involved in coupling polypeptide substrate binding to stimulation of ATP hydrolysis.Protein science : a publication of the Protein Society · 2006Article
- Translocation boost protein-folding efficiency of double-barreled chaperonins.Biophysical journal · 2006Article
- GroEL-mediated protein folding: making the impossible, possible.Critical reviews in biochemistry and molecular biologyReview
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A molecular dynamics simulation of the active unfolding of denatured rhodanese by the chaperone GroEL is presented. The compact denatured protein is bound initially to the cis cavity and forms stable contacts with several of the subunits. As the cis ring apical domains of GroEL undergo the transition from the closed to the more open (ATP-bound) state, they exert a force on rhodanese that leads to the increased unfolding of certain loops. The contacts between GroEL and rhodanese are analyzed and their variation during the GroEL transition is shown. The major contacts, which give rise to the stretching force, are found to be similar to those observed in crystal structures of peptides bound to the apical domains. The results of the simulation show that multidomain interactions play an essential role, in accord with experiments. Implications of the results for mutation experiments and for the action of GroEL are discussed.
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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.