Results 11 to 20 of about 3,214 (169)
Gears-In-Motion: The Interplay of WW and PPIase Domains in Pin1 [PDF]
Frontiers in Oncology, 2018 Pin1 belongs to the family of the peptidyl-prolyl cis-trans isomerase (PPIase), which is a class of enzymes that catalyze the cis/trans isomerization of the Proline residue. Pin1 is unique and only catalyzes the phosphorylated Serine/Threonine-Proline (S/
Yew Mun Lee, Yih-Cherng Liou
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Update on the Neisseria Macrophage Infectivity Potentiator-Like PPIase Protein
Frontiers in Cellular and Infection Microbiology, 2022 Neisseria pathogens express a Macrophage Infectivity Potentiator Protein (MIP), which belongs to the FK506 binding protein (FKBP) family of proteins that exhibit peptidyl-prolyl cis/trans isomerase (PPIase) activity.
Myron Christodoulides
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Introduction to Peptidyl-Prolyl cis/trans Isomerase (PPIase) Series [PDF]
Biomolecules, 2019 About 30 years after the discovery of peptidyl-prolyl cis/trans isomerases (PPIases), research on this group of proteins has become somewhat calmer than it used to be, but it still generates lots of interest [...]
Andrzej Galat
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HSP-90/kinase complexes are stabilized by the large PPIase FKB-6 [PDF]
Scientific Reports, 2021 Protein kinases are important regulators in cellular signal transduction. As one major type of Hsp90 client, protein kinases rely on the ATP-dependent molecular chaperone Hsp90, which maintains their structure and supports their activation.
Siyuan Sima +7 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
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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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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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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
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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
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