Prolyl Isomerases and Nuclear Function

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Prolyl Isomerases and Nuclear Function

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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...

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Prolyl 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...

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Protein 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.

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Immunophilins and parvulins. Superfamily of peptidyl prolyl isomerases in Arabidopsis.

Immunophilins are defined as receptors for immunosuppressive drugs including cyclosporin A, FK506, and rapamycin. The cyclosporin A receptors are referred to as cyclophilins (CYPs) and FK506- and rapamycin-binding proteins are abbreviated as FKBPs. These two groups of proteins (collectively called immunophilins) share little sequence homology, but both have peptidyl prolyl cis/trans isomerase (...

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ژورنال

عنوان ژورنال: Cell

سال: 1998

ISSN: 0092-8674

DOI: 10.1016/s0092-8674(00)80906-x