Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts.
about
Abnormal type I collagen post-translational modification and crosslinking in a cyclophilin B KO mouse model of recessive osteogenesis imperfectaAntamanide, a derivative of Amanita phalloides, is a novel inhibitor of the mitochondrial permeability transition poreThe FKBP-associated protein FAP48 is an antiproliferative molecule and a player in T cell activation that increases IL2 synthesisProliferating cell nuclear antigen in the cytoplasm interacts with components of glycolysis and cancerStructural insights into the catalytic mechanism of cyclophilin AThe crystal structure of PPIL1 bound to cyclosporine A suggests a binding mode for a linear epitope of the SKIP proteinFK506 binding protein 12 differentially accelerates fibril formation of wild type alpha-synuclein and its clinical mutants A30P or A53TNo death without life: vital functions of apoptotic effectorsThe FK506-binding protein 25 functionally associates with histone deacetylases and with transcription factor YY1.Developmental regulation of FKBP65. An ER-localized extracellular matrix binding-proteinAIPL1, the protein that is defective in Leber congenital amaurosis, is essential for the biosynthesis of retinal rod cGMP phosphodiesteraseThe cyclophilinsEnzymes: An integrated view of structure, dynamics and functionMolecular phylogenetics and comparative modeling of HEN1, a methyltransferase involved in plant microRNA biogenesisEnvironmental Regulation of Yersinia PathophysiologyDisulfide bond formation in the bacterial periplasm: major achievements and challenges aheadProlyl isomerase Pin1 in cancerThe genome of tolypocladium inflatum: evolution, organization, and expression of the cyclosporin biosynthetic gene clusterCrystal structure of the human U4/U6 small nuclear ribonucleoprotein particle-specific SnuCyp-20, a nuclear cyclophilinThe three-dimensional structure of two redox states of cyclophilin A from Schistosoma mansoni. Evidence for redox regulation of peptidyl-prolyl cis-trans isomerase activityStructure of CFA/I fimbriae from enterotoxigenic Escherichia coliCrystallographic structure of the tetratricopeptide repeat domain ofPlasmodium falciparumFKBP35 and its molecular interaction with Hsp90 C-terminal pentapeptideStructural basis for regulation of the Crk signaling protein by a proline switch.Crystal structure of N-domain of FKBP22 from Shewanella sp. SIB1: Dimer dissociation by disruption of Val-Leu knotStructure of a bacterial cytoplasmic cyclophilin A in complex with a tetrapeptideStructure and Activity of the Peptidyl-Prolyl Isomerase Domain from the Histone Chaperone Fpr4 toward Histone H3 Proline IsomerizationSolution structure of a putative FKBP-type peptidyl-propyl cis–trans isomerase from Giardia lambliaSolution structure of FK506-binding protein 12 from Aedes aegyptiStructure and evolution of the spliceosomal peptidyl-prolyl cis-trans isomerase Cwc27Cyclophilin A is localized to the nucleus and controls meiosis in Saccharomyces cerevisiae.The Ess1 prolyl isomerase is linked to chromatin remodeling complexes and the general transcription machinery.Cpr6 and Cpr7, two closely related Hsp90-associated immunophilins from Saccharomyces cerevisiae, differ in their functional properties.Inhibitor-Based Therapeutics for Treatment of Viral HepatitisPhysiological and Pathogenic Roles of Prolyl Isomerase Pin1 in Metabolic Regulations via Multiple Signal Transduction Pathway ModulationsKSHV reactivation and novel implications of protein isomerization on lytic switch controlA reassessment of the inhibitory capacity of human FKBP38 on calcineurinStructural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerasesUpregulation of vasopressin V1A receptor mRNA and protein in vascular smooth muscle cells following cyclosporin A treatmentCyclosporin A treatment of Leishmania donovani reveals stage-specific functions of cyclophilins in parasite proliferation and viabilitySolution structural analysis of the single-domain parvulin TbPin1
P2860
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P2860
Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts.
description
1999 nî lūn-bûn
@nan
1999 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի մարտին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts.
@ast
Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts.
@en
type
label
Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts.
@ast
Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts.
@en
prefLabel
Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts.
@ast
Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts.
@en
P356
P1476
Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts.
@en
P2093
M A Marahiel
S F Göthel
P2888
P304
P356
10.1007/S000180050299
P577
1999-03-01T00:00:00Z