منابع مشابه
Prolyl isomerases in yeast.
Prolyl isomerases are enzymes that catalyze cis-trans isomerization of peptidyl-prolyl bonds and span three structurally unrelated protein families: the cyclophilins, FKBPs, and parvulins. The genome of the budding yeast Saccharomyces cerevisiae encodes eight different cyclophilins (Cpr1 to Cpr8), four FKBPs (Fpr1 to Fpr4), and a single parvulin (Ess1). Remarkably, two of these proteins, cyclop...
متن کاملProlyl Isomerases and Nuclear Function
(calcium-signal modulating cyclophilin ligand), and Cyp40 is part of the Hsp90/Hsc70 complex that binds steroid receptors. Likewise, FKBP12 is a subunit of two calcium Tony Hunter Molecular Biology and Virology Laboratory The Salk Institute channels (the ryanodine receptor and the IP 3 receptor), 10010 North Torrey Pines Road is needed for the function of the MDR drug efflux pump La Jolla, Cali...
متن کاملProlyl Isomerases as New Therapeutic Targets
Prolyl isomerases comprise three main protein families totalling over thirty mammalian genes, and several hundred orthologues across the biological domains, with a very broad spectrum of physiological functions and disease implications. Potent small molecule inhibitors exist for members of the three main mammalian families (cyclophilins, FKBPs and parvulins),. but, until recently, these protein...
متن کاملProtein folding: Prolyl isomerases join the fold
Cyclophilins have prolyl isomerase activity, but evidence for their suggested role in protein folding in cells has been scarce; now they have been found to accelerate the folding of mitochondrial precursor proteins.
متن کاملPeptidyl-prolyl isomerases: a new twist to transcription.
Peptidyl-prolyl isomerases (PPIs) catalyse the cis-trans isomerisation of peptide bonds N-terminal to proline residues in polypeptide chains. They have roles in the folding of newly synthesised proteins and in the function of the immune system. In addition, members of the parvulin-like family of PPIs have been implicated in cell cycle control. Their activity is directed by the prior phosphoryla...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 2000
ISSN: 0014-2956
DOI: 10.1046/j.1432-1327.2000.01355.x