Results 21 to 30 of about 3,959 (198)
Identification of RNA targets for the nuclear multidomain cyclophilin atCyp59 and their effect on PPIase activity [PDF]
Nucleic Acids Research, 2012 AtCyp59 is a multidomain cyclophilin containing a peptidyl-prolyl cis/trans isomerase (PPIase) domain and an evolutionarily highly conserved RRM domain. Deregulation of this class of cyclophilins has been shown to affect transcription and to influence phosphorylation of the C-terminal repeat domain of the largest subunit of the RNA polymerase II.
Bannikova, Olga +5 more
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Cyclophilin J PPIase Inhibitors Derived from 2,3-Quinoxaline-6 Amine Exhibit Antitumor Activity
Frontiers in Pharmacology, 2018 Cyclophilin J (CyPJ), also called peptidylprolyl isomerase like 3, has been identified as a novel member of the cyclophilin family. Our previous research has resolved the three-dimensional structure of CyPJ and demonstrated the peptidylprolyl cis–trans ...
Xuemei Zhao +7 more
doaj +2 more sources
High‐resolution insights into binding of unfolded polypeptides by the PPIase chaperone SlpA
The FASEB Journal, 2012 SlpA is a 2‐domain protein consisting of an FK506‐binding protein (FKBP) domain that harbors the peptidyl‐prolyl cis / trans ‐isomerase (PPIase) active site and a small insert‐in‐flap (IF) domain that endows the protein with chaperone activity.
Quistgaard EM, Nordlund P, Löw C
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PPIase independent chaperone‐like function of recombinant human Cyclophilin A during arginine kinase refolding [PDF]
FEBS Letters, 2013 Whether Cyclophilin A (CyPA) functions as a foldase or a chaperone when assisting protein folding has long been argued. In this study, we engineered four variants of recombinant human Cyclophilin A (rhCyPA), all of which were inactive to tetrapeptide substrate Suc‐AAPF‐pNA.
Zhang, Xin-Chao +3 more
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Biophysical characterization of Cyclophilin B reveals membrane localization as its primary functional determinant as a prolyl isomerase. [PDF]
Protein SciAbstract The endoplasmic reticulum (ER) provides a specialized environment for the folding of secreted and membrane proteins, a process supported by many different chaperones. Among these chaperones, peptidyl‐prolyl cis/trans isomerases (PPIases) catalyze a rate‐limiting conformational step in protein folding, yet the principles governing isoform ...
DeVoe SC +7 more
europepmc +2 more sources
Human Cyclophilins-An Emerging Class of Drug Targets. [PDF]
Med Res RevABSTRACT Cyclophilins are a family of enzymes with peptidyl‐prolyl isomerase activity found in all cells of all organisms. To date, 17 cyclophilin isoforms have been identified in the human body, participating in diverse biological processes. Consequently, cyclophilins have emerged as promising targets for drug development to address a wide array of ...
Jurkova K +3 more
europepmc +2 more sources
Structural insights into Plasmodium PPIases
Frontiers in Cellular and Infection Microbiology, 2022 Malaria is one of the most prevalent infectious diseases posing a serious challenge over the years, mainly owing to the emergence of drug-resistant strains, sparking a need to explore and identify novel protein targets. It is a well-known practice to adopt a chemo-genomics approach towards identifying targets for known drugs, which can unravel a novel ...
Sreekanth Rajan +3 more
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The competitive interplay of 12-oxophytodienoic acid (OPDA), protein thiols, and glutathione. [PDF]
FEBS J12‐Oxophytodienoic acid (OPDA) is a phytohormone involved in plant growth and stress defense. Due to its cyclopentenone moiety, OPDA can form Michael adducts with thiol‐containing compounds such as glutathione and cysteine residues of proteins, resulting in alterations of the cellular redox regulatory network.
Knieper M +8 more
europepmc +2 more sources
A cavity with an appropriate size is the basis of the PPIase activity [PDF]
Protein Engineering Design and Selection, 2008 Peptidyl-prolyl isomerases (PPIases) are biologically very important enzymes but their catalytic mechanism is not fully understood. Recently, our comprehensive mutational study on a PPIase, human FK506-binding protein 12 (FKBP12), suggested that only presence of a cavity was required for the catalysis.
Teikichi, Ikura +2 more
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AtFKBP53: a chimeric histone chaperone with functional nucleoplasmin and PPIase domains [PDF]
Nucleic Acids Research, 2019 AbstractFKBP53 is one of the seven multi-domain FK506-binding proteins present in Arabidopsis thaliana, and it is known to get targeted to the nucleus. It has a conserved PPIase domain at the C-terminus and a highly charged N-terminal stretch, which has been reported to bind to histone H3 and perform the function of a histone chaperone.
Dileep Vasudevan +4 more
openaire +5 more sources