A Critical Role of Peptidylprolyl Isomerase A Pseudogene 22/microRNA-197-3p/Peptidylprolyl Isomerase A Axis in Hepatocellular Carcinoma [PDF]
Frontiers in Genetics, 2021 The burden of hepatocellular carcinoma (HCC) worldwide is increasing over time, while the underlying molecular mechanism of HCC development is still under exploration.
Kangkang Yu, Tang Jia
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Dual-Family Peptidylprolyl Isomerases (Immunophilins) of Select Monocellular Organisms [PDF]
Biomolecules, 2018 The dual-family peptidylprolyl cis-trans isomerases (immunophilins) represent a naturally occurring chimera of the classical FK506-binding protein (FKBP) and cyclophilin (CYN), connected by a flexible linker.
Sailen Barik, Barik Sailen
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Peptidylprolyl isomerase C (Ppic) regulates invariant Natural Killer T cell (iNKT) differentiation in mice [PDF]
European Journal of Immunology, 2021 Abstract Peptidyl‐prolyl cis‐trans isomerase C ( Ppic ) is expressed in several bone marrow (BM) hematopoietic progenitors and in T‐cell precursors. Since the expression profile of Ppic in the hematoimmune system ...
Luis Graça +2 more
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Peptidylprolyl isomerase A guides SENP5/GAU1 DNA-lncRNA triplex generation for driving tumorigenesis [PDF]
Nature CommunicationsThe three-stranded DNA-RNA triplex hybridization is involved in various biological processes, including gene expression regulation, DNA repair, and chromosomal stability.
Xiaoyu Zhang +10 more
doaj +4 more sources
FKBP38 Peptidylprolyl Isomerase Promotes the Folding of Cystic Fibrosis Transmembrane Conductance Regulator in the Endoplasmic Reticulum [PDF]
Journal of Biological Chemistry, 2011 FK506-binding protein 38 (FKBP38), a membrane-anchored, tetratricopeptide repeat (TPR)-containing immunophilin, associates with nascent plasma membrane ion channels in the endoplasmic reticulum (ER). It promotes the maturation of the human ether-à-go-go-related gene (HERG) potassium channel and maintains the steady state level of the cystic fibrosis ...
Yeshavanth Kumar Banasavadi-Siddegowda +2 more
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Crystallization and preliminary X-ray diffraction analysis of the peptidylprolyl isomerase Par27 ofBordetella pertussis [PDF]
Acta Crystallographica Section F: Structural Biology Communications, 2008 Proteins with both peptidylprolyl isomerase (PPIase) and chaperone activities play a crucial role in protein folding in the periplasm of Gram-negative bacteria. Few such proteins have been structurally characterized and to date only the crystal structure of SurA from Escherichia coli has been reported.
Françoise Jacob-Dubuisson +2 more
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Peptidylprolyl Isomerase A (PPIA) as a Preferred Internal Control Over GAPDH and β-Actin in Quantitative RNA Analyses [PDF]
BioTechniques, 2002 A good internal control is critical in all quantitative analyses of gene expression. Levels of β-actin, glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and peptidylprolyl isomerase A (PPIA) were analyzed in 78 samples (data obtained from our laboratory
Yong Q Chen
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The Hsp90-binding peptidylprolyl isomerase FKBP52 potentiates glucocorticoid signaling in vivo [PDF]
EMBO Journal, 2003 Hsp90 is required for the normal activity of steroid receptors, and in steroid receptor complexes it is typically bound to one of the immunophilin-related co-chaperones: the peptidylprolyl isomerases FKBP51, FKBP52 or CyP40, or the protein phosphatase PP5.
Didier Picard +2 more
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High expression level of peptidylprolyl isomerase A is correlated with poor prognosis of liver hepatocellular carcinoma. [PDF]
Oncol Lett, 2019 Peptidylprolyl isomerase A (PPIA) has been reported to be correlated with cancer. The present study investigated the prognostic values of PPIA expression levels in cancer by comparing different types of cancer using databases. High expression levels of PPIA were observed in 17 out of 17 cancer types compared with normal adjacent tissues.
Wang S, Li M, Xing L, Yu J.
europepmc +4 more sources
The crystal structure of human WD40 repeat‐containing peptidylprolyl isomerase (PPWD1) [PDF]
FEBS Journal, 2008 Cyclophilins comprise one of the three classes of peptidylprolyl isomerases found in all eukaryotic and prokaryotic organisms, as well as viruses. Many of the 17 annotated human cyclophilins contain the catalytic domain in tandem with other domains, and many of the specific functions of a particular cyclophilin or its associated domains remain unknown.
Tara Davis, John R Walker
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