Mechanism of enzymatic and nonenzymatic prolyl cis-trans isomerization. (Q40818804)

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29 October 2019

review article

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title

Mechanism of enzymatic and nonenzymatic prolyl cis-trans isomerization (English)

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8317295%20AND%20SRC:MED&resulttype=core&format=json

29 October 2019

author name string

Stein RL

series ordinal

1

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29 October 2019

publication date

1 January 1993

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8317295%20AND%20SRC:MED&resulttype=core&format=json

Advances in Protein Chemistry

29 October 2019

published in

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8317295%20AND%20SRC:MED&resulttype=core&format=json

29 October 2019

volume

44

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29 October 2019

page(s)

1-24

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Unfolding and refolding occur much faster for a proline-free proteins than for most proline-containing proteins

29 October 2019

cites work

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Cis-trans equilibrium and kinetic studies of acetyl-L-proline and glycyl-L-proline

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Kinetic beta-deuterium isotope effects suggest a covalent mechanism for the protein folding enzyme peptidylprolyl cis/trans-isomerase

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Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins

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The effect of adjacent charges on the kinetics of rotation of the peptide bond

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A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase

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Mechanistic studies of peptidyl prolyl cis-trans isomerase: evidence for catalysis by distortion

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Substrate specificities of the peptidyl prolyl cis-trans isomerase activities of cyclophilin and FK-506 binding protein: evidence for the existence of a family of distinct enzymes

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Rusting of the Lock and Key Model for Protein-Ligand Binding

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Determination of kinetic constants for peptidyl prolyl cis-trans isomerases by an improved spectrophotometric assay

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Determination of cis-trans proline isomerization by trypsin proteolysis. Application to a model pentapeptide and to oxidized ribonuclease A

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Cloning, expression, and purification of human cyclophilin in Escherichia coli and assessment of the catalytic role of cysteines by site-directed mutagenesis

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Solution Structure of FKBP, a Rotamase Enzyme and Receptor for FK506 and Rapamycin

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Solution structure of the major binding protein for the immunosuppressant FK506

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Hydrophobic interactions

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Influences of solvent water on protein folding: free energies of solvation of cis and trans peptides are nearly identical

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Inhibition of FKBP rotamase activity by immunosuppressant FK506: twisted amide surrogate.

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Isergonic relations and their significance for catalysis

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A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin

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Exploring the catalytic activity of immunophilins

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Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin

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7 January 2021

Atomic structure of FKBP-FK506, an immunophilin-immunosuppressant complex

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Receptor-induced conformation change of the immunosuppressant cyclosporin A.

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Identifiers

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