ArticleProtein science : a publication of the Protein Society2009
Characterizing and controlling the inherent dynamics of cyclophilin-A.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 40 citations in OpenAlex.
- Identifying and controlling inactive and active conformations of a serine protease.Science advances · 2025Article
- Relaxation and single site multiple mutations to identify and control allosteric networks.Methods (San Diego, Calif.) · 2023Review
- Molecular insight into the specific interactions of the SARS-Coronavirus-2 nucleocapsid with RNA and host protein.Protein science : a publication of the Protein Society · 2023Article
- Identifying structural and dynamic changes during the Biliverdin Reductase B catalytic cycle.Frontiers in molecular biosciences · 2023Article
- The Inherent Dynamics and Interaction Sites of the SARS-CoV-2 Nucleocapsid N-Terminal Region.Journal of molecular biology · 2021Article
- Proline/arginine dipeptide repeat polymers derail protein folding in amyotrophic lateral sclerosis.Nature communications · 2021Article
- The PyInteraph Workflow for the Study of Interaction Networks From Protein Structural Ensembles.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Modulating Enzyme FunctionFrontiers in molecular biosciences · 2021Article
- Dynamic design: manipulation of millisecond timescale motions on the energy landscape of cyclophilin A.Chemical science · 2020Article
- Interleukin-37 monomer is the active form for reducing innate immunity.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Biliverdin Reductase B Dynamics Are Coupled to Coenzyme Binding.Journal of molecular biology · 2018Article
- The clinical implication of serum cyclophilin A in patients with chronic obstructive pulmonary disease.International journal of chronic obstructive pulmonary disease · 2018Article
- Networks of Dynamic Allostery Regulate Enzyme Function.Structure (London, England : 1993) · 2017Article
- Dynamical network of residue-residue contacts reveals coupled allosteric effects in recognition, catalysis, and mutation.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Mapping the conformational landscape of a dynamic enzyme by multitemperature and XFEL crystallography.eLife · 2015Article
- Cyclophilin40 isomerase activity is regulated by a temperature-dependent allosteric interaction with Hsp90.Bioscience reports · 2015Article
- Structure and Dynamics of GeoCyp: A Thermophilic Cyclophilin with a Novel Substrate Binding Mechanism That Functions Efficiently at Low Temperatures.Biochemistry · 2015Article
- Inherent dynamics within the Crimean-Congo Hemorrhagic fever virus protease are localized to the same region as substrate interactions.Protein science : a publication of the Protein Society · 2015Article
- 1H, 13C, and 15N backbone and side chain resonance assignments of thermophilic Geobacillus kaustophilus cyclophilin-A.Biomolecular NMR assignments · 2014Article
- The dynamics of interleukin-8 and its interaction with human CXC receptor I peptide.Protein science : a publication of the Protein Society · 2014Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
With the recent advances in NMR relaxation techniques, protein motions on functionally important timescales can be studied at atomic resolution. Here, we have used NMR-based relaxation experiments at several temperatures and both 600 and 900 MHz to characterize the inherent dynamics of the enzyme cyclophilin-A (CypA). We have discovered multiple chemical exchange processes within the enzyme that form a "dynamic continuum" that spans 20-30 A comprising active site residues and residues proximal to the active site. By combining mutagenesis with these NMR relaxation techniques, a simple method of counting the dynamically sampled conformations has been developed. Surprisingly, a combination of point mutations has allowed for the specific regulation of many of the exchange processes that occur within CypA, suggesting that the dynamics of an enzyme may be engineered.
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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.