We are analyzing https://link.springer.com/chapter/10.1007/s10254-003-0011-3.

Title:
Regulation of peptide bond cis/trans isomerization by enzyme catalysis and its implication in physiological processes | SpringerLink
Description:
In some cases, the slow rotational movement underlying peptide bond cis/trans isomerizations is found to control the biological activity of proteins. Peptide bond cis/trans isomerases as cyclophilins, Fk506-binding proteins, parvulins, and bacterial hsp70 generally...
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Keywords {🔍}

google, scholar, cas, pubmed, prolyl, cistrans, biol, fischer, protein, chem, peptidyl, cyclophilin, isomerase, cell, mol, sci, activity, proc, usa, folding, biochemistry, natl, acad, isomerization, proteins, schmid, factor, peptide, isomerases, chaperone, coli, fkbp, escherichia, gene, trigger, lett, function, bond, embo, febs, biochem, human, calcineurin, binding, schutkowski, role, biophys, structure, hiv, proline,

Topics {✒️}

peptidyl-prolyl cis-trans-isomerase peptidyl-prolyl cis/trans isomerases stopped-flow double-mixing technique g1-arresting rapamycin-eceptor complex prolyl cis/trans isomerases slow cis/trans isomerization cis/trans isomerase function proline cis/trans isomerization x-pro peptide bond immunophilin-immunosuppressant fkbp12-fk506 complex peptidyl prolyl isomerases sin3-rpd3 histone deacetylase peptidyl prolyl isomerization cis/trans isomerization cis/trans isomers highly exposed α-helix prolyl isomerase pin1 cis prolyl isomerization rapamycin-modulated transcription defines hiv-1 gag protein—insights trigger integrin-mediated adhesion calcineurin-cyclophilin-cyclosporin shows common phosphorylation-dependent proline isomerization prolyl peptide bond month download article/chapter ess1 prolyl isomerase cis/trans isomerism cis/trans signatures cis/trans conformers excitotoxin-induced caspas activation 12-kda fk506-binding protein cdna-based microarray analysis t-cell signaling pathways proline-directed phosphorylation signaling cis/trans specificity cyclophilin-facilitated bradykinin inactivation proline-driven conformational switch cis/trans interconversion salmonella typhimurium copenhagen chaperone-mediated protein folding regulates hiv-1 infectivity tgf-β receptor inhibition dimensional nmr spectroscopy protein-drug complexes important nonprolyl peptide bonds block protein export privacy choices/manage cookies fk506-binding protein family fk506-independent interaction max-planck society

Questions {❓}

Sigal NH, Dumont F, Durette P, Siekierka JJ, Peterson L, Rich DH, Dunlap BE, Staruch MJ, Melino MR, Koprak SL, Willimas D, Witzel B, Pisano JM (1991) Is cyclophilin involved in the immunosuppressive and nephrotoxic mechanism of action of cyclosporin A?

Schema {🗺️}

ScholarlyArticle:
      headline:Regulation of peptide bond cis/trans isomerization by enzyme catalysis and its implication in physiological processes
      pageEnd:150
      pageStart:105
      image:https://media.springernature.com/w153/springer-static/cover/book/978-3-540-44834-1.jpg
      genre:
         Biomedical and Life Sciences
         Biomedical and Life Sciences (R0)
      isPartOf:
         name:Reviews of Physiology, Biochemistry and Pharmacology
         isbn:
            978-3-540-44834-1
            978-3-540-40136-0
         type:Book
      publisher:
         name:Springer Berlin Heidelberg
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:G. Fischer
            affiliation:
                  name:Max Planck Research Unit for Enzymology of Protein Folding
                  address:
                     name:Max Planck Research Unit for Enzymology of Protein Folding, Halle, Germany
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
            name:T. Aumüller
            affiliation:
                  name:Max Planck Research Unit for Enzymology of Protein Folding
                  address:
                     name:Max Planck Research Unit for Enzymology of Protein Folding, Halle, Germany
                     type:PostalAddress
                  type:Organization
            type:Person
      keywords:Peptide Bond, Trigger Factor, FK506 Binding Protein, Peptidyl Prolyl Isomerase, PPIase Activity
      description:In some cases, the slow rotational movement underlying peptide bond cis/trans isomerizations is found to control the biological activity of proteins. Peptide bond cis/trans isomerases as cyclophilins, Fk506-binding proteins, parvulins, and bacterial hsp70 generally assist in the interconversion of the polypeptide substrate cis/trans isomers, and rate acceleration is the dominating mechanism of action in cells. We present evidence disputing the hypothesis that some of the molecular properties of these proteins play an auxiliary role in enzyme function.
      datePublished:2003
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      name:Reviews of Physiology, Biochemistry and Pharmacology
      isbn:
         978-3-540-44834-1
         978-3-540-40136-0
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      name:Springer Berlin Heidelberg
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         type:ImageObject
      name:Max Planck Research Unit for Enzymology of Protein Folding
      address:
         name:Max Planck Research Unit for Enzymology of Protein Folding, Halle, Germany
         type:PostalAddress
      name:Max Planck Research Unit for Enzymology of Protein Folding
      address:
         name:Max Planck Research Unit for Enzymology of Protein Folding, Halle, Germany
         type:PostalAddress
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      name:G. Fischer
      affiliation:
            name:Max Planck Research Unit for Enzymology of Protein Folding
            address:
               name:Max Planck Research Unit for Enzymology of Protein Folding, Halle, Germany
               type:PostalAddress
            type:Organization
      email:[email protected]
      name:T. Aumüller
      affiliation:
            name:Max Planck Research Unit for Enzymology of Protein Folding
            address:
               name:Max Planck Research Unit for Enzymology of Protein Folding, Halle, Germany
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Max Planck Research Unit for Enzymology of Protein Folding, Halle, Germany
      name:Max Planck Research Unit for Enzymology of Protein Folding, Halle, Germany
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