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We are analyzing https://genomebiology.biomedcentral.com/articles/10.1186/gb-2005-6-7-226.

Title:
The cyclophilins | Genome Biology | Full Text
Description:
Summary Cyclophilins (Enzyme Commission (EC) number 5.1.2.8) belong to a group of proteins that have peptidyl-prolyl cis-trans isomerase activity; such proteins are collectively known as immunophilins and also include the FK-506-binding proteins and the parvulins. Cyclophilins are found in all cells of all organisms studied, in both prokaryotes and eukaryotes; humans have a total of 16 cyclophilin proteins, Arabidopsis up to 29 and Saccharomyces 8. The first member of the cyclophilins to be identified in mammals, cyclophilin A, is the major cellular target for, and thus mediates the actions of, the immunosuppressive drug cyclosporin A. Cyclophilin A forms a ternary complex with cyclosporin A and the calcium-calmodulin-activated serine/threonine-specific protein phosphatase calcineurin; formation of this complex prevents calcineurin from regulating cytokine gene transcription. Recent studies have implicated a diverse array of additional cellular functions for cyclophilins, including roles as chaperones and in cell signaling.
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Keywords {🔍}

pubmed, article, scholar, google, cas, cyclophilin, cyclophilins, calcineurin, yeast, protein, central, cpr, complex, cell, cypa, human, structure, report, proteins, function, domain, role, nature, peptidylprolyl, activity, found, cyclosporin, csa, cyp, gene, cerevisiae, figure, binding, usa, heitman, cells, sci, functions, crystal, paper, chem, proc, natl, acad, biol, review, peptide, form, cpa, signal,

Topics {✒️}

fungus tolypocladium inflatum peptidyl-prolyl cis-trans isomerase peptidyl-prolyl cis-trans isomerases n-terminal cyclophilin-homologous domain gene organization springer nature receptor protein-tyrosine kinase sin3-rpd3 histone-deacetylase complex amino-terminal rna-binding domain peptidylprolyl cis-trans-isomerase cis-trans transition state peptidyl-prolyl isomerase cyclophilin amino-terminal signal sequences n-terminal signal sequence carboxy-terminal residues protrude references fischer immunosuppressive drug cyclosporin peptidylprolyl cis/trans isomerases sin3-rpd3 histone deacetylase virus-induced irf-3 phosphorylation human immunodeficiency virus calcineurin-cyclophilin-cyclosporin shows common generating cypd-deficient mice maintains histone-deacetylase activities immunosuppressive drug csa immunophilin-ligand complexes correlates 'peptidyl-prolyl isomerase' heat-shock protein hsp90 authors scientific editing regulatory subunit calcineurin calcineurin regulatory subunit koser pl author information authors fk506-sensitive yeast strains partial double-bond character nuclear rna-binding cyclophilin authors’ original file burroughs-wellcome scholar excitotoxin-induced caspase activation protein-folding processes depend calcineurin phosphatase activity peptidyl-prolyl bonds privacy choices/manage cookies peptidyl-prolyl isomerases peptidyl prolyl isomerases characteristic structural features proline-directed conformational switch proline-driven conformational switch prolyl isomerase requirement unactivated estrogen receptor

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What is peptidyl-prolyl isomerization and why does it require a catalyst?

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