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Article

Cyclosporin A slows collagen triple-helix formation in vivo: indirect evidence for a physiologic role of peptidyl-prolyl cis-trans-isomerase.

1 Jan 1991

Abstract excerpt

Peptidyl-prolyl cis-trans-isomerase accelerates otherwise slow, rate-limiting isomerization steps during folding of proteins in vitro, but is not yet securely identified with any specific physiologic role. Peptidyl-prolyl cis-trans-isomerase and the cyclosporin A (CsA)-binding protein cyclophilin are identical, and peptidyl-prolyl cis-trans-isomerase activity is inhibited by the immunosuppressive drug CsA in...

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Identifiers

PMID: 1985948
DOI: 10.1016/s0021-9258(17)35315-2

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Cyclosporin A slows collagen triple-helix formation in vivo: indirect evidence for a physiologic role of peptidyl-prolyl cis-trans-isomerase.PMID 1985948Read ↗

Thermal stability and folding of the collagen triple helix and the effects of mutations in osteogenesis imperfecta on the triple helix of type I collagen.Semantic proximity Read ↗

Cyclophilin active site mutants have native prolyl isomerase activity with a protein substrate.Semantic proximity Read ↗

Multiple roles of prolyl residues in structure and folding.Semantic proximity Read ↗

A nonessential role for Arg 55 in cyclophilin18 for catalysis of proline isomerization during protein folding.Semantic proximity Read ↗

Substitutions for glycine alpha 1-637 and glycine alpha 2-694 of type I procollagen in lethal osteogenesis imperfecta. The conformational strain on the triple helix introduced by a glycine substitution can be transmitted along the helix.Semantic proximity Read ↗

Mutations that substitute serine for glycine alpha 1-598 and glycine alpha 1-631 in type I procollagen. The effects on thermal unfolding of the triple helix are position-specific and demonstrate that the protein unfolds through a series of cooperative blocks.Semantic proximity Read ↗

Mutation in cyclophilin B that causes hyperelastosis cutis in American Quarter Horse does not affect peptidylprolyl cis-trans isomerase activity but shows altered cyclophilin B-protein interactions and affects collagen folding.Semantic proximity Read ↗

Structural and evolutionary relationships among the immunophilins: two ubiquitous families of peptidyl-prolyl cis-trans isomerases.Semantic proximity Read ↗

Functions of FKBP12 and mitochondrial cyclophilin active site residues in vitro and in vivo in Saccharomyces cerevisiae.Semantic proximity Read ↗

Two cysteine substitutions in procollagen I: a glycine replacement near the N-terminus of alpha 1(I) chain causes lethal osteogenesis imperfecta and a glycine replacement in the alpha 2(I) chain markedly destabilizes the triple helix.Semantic proximity Read ↗

Folding of peptide models of collagen and misfolding in disease.Semantic proximity Read ↗

Thermodynamic and kinetic consequences of substituting glycine at different positions in a Pro-Hyp-Gly repeat collagen model peptide.Semantic proximity Read ↗

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