Results 91 to 100 of about 18,044 (216)
Negative Regulation of Peptidyl-Prolyl Isomerase Activity by Interdomain Contact in Human Pin1
, 2015 SummaryPin1 is a modular peptidyl-prolyl isomerase specific for phosphorylated Ser/Thr-Pro (pS/T-P) motifs, typically within intrinsically disordered regions of signaling proteins. Pin1 consists of two flexibly linked domains: an N-terminal WW domain for
Mahoney, Brendan J. +4 more
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Chemistry – A European Journal, Volume 32, Issue 24, 23 June 2026.This review highlights biocatalytic prenylation as a versatile strategy for tailoring the functional properties of peptides and proteins. By comparing branched isoprenoids with linear lipids, we illustrate how specific prenyl architectures modulate the behaviors of lipidated proteins within membrane environments.
Daisuke Fujinami +2 more
wiley +1 more source
유방암에서 Peptidyl–prolyl cis-trans isomerase NIMA- interacting 1에 의한 HIF-2α의 안정화 [PDF]
, 2023 학위논문(박사) -- 서울대학교대학원 : 융합과학기술대학원 분자의학 및 바이오제약학과, 2023. 8. Young Kee Shin.Peptidyl-prolyl isomerase (Pin1) is overexpressed in the majority of cancers and binds to target proteins containing phosphorylated serine or threonine residues followed by proline (
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Mass spectrometry, fluorescence polarisation and chymotrypsin-coupled PPIase assay data to accompany manuscript entitled "Dissecting the functional behaviour of the differentially phosphorylated prolyl isomerase, Pin1" by Kay et al ...
Leney, Aneika C. +4 more
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, 2023 The peptidyl prolyl cis-trans isomerase Pin1 plays vital roles in diverse cellular processes and pathological conditions. NeuroD is a differentiation and survival factor for a subset of neurons and pancreatic endocrine cells.
Yun-Jin Jiang (43148) +5 more
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Prolyl isomerase Pin1 enhances osteoblast differentiation through Runx2 regulation
, 2013 Peptidyl-prolyl isomerase 1 (Pin1) is the only enzyme known to catalyze isomerization of the pSer/Thr-Pro peptide bond. Pin1 induces conformational change of substrates and subsequently regulates diverse cellular processes.
Choi, Hong Seok +5 more
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PIN1 in Cell Cycle Control and Cancer
Frontiers in Pharmacology, 2018 Cell cycle progression is tightly controlled by many cell cycle-regulatory proteins that are in turn regulated by a family of cyclin-dependent kinases (CDKs) through protein phosphorylation. The peptidyl-prolyl cis/trans isomerase PIN1 provides a further
Chi-Wai Cheng, Eric Tse
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Journal of the American Heart Association: Cardiovascular and Cerebrovascular Disease, 2017 BackgroundAberrant Ca2+ handling is a prominent feature of heart failure. Elucidation of the molecular mechanisms responsible for aberrant Ca2+ handling is essential for the development of strategies to blunt pathological changes in calcium dynamics. The
Veronica Sacchi +15 more
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The Multiple Roles of Peptidyl Prolyl Isomerases in Brain Cancer [PDF]
Biomolecules, 2018 Peptidyl prolyl isomerases (PPIases) are broadly expressed enzymes that accelerate the cis-trans isomerization of proline peptide bonds. The most extensively studied PPIase family member is protein interacting with never in mitosis A1 (PIN1), which isomerizes phosphorylated serine/threonine–proline bonds.
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Peptidyl-prolyl cis-trans isomerase activity as studied by dynamic proton NMR spectroscopy
, 1991 Recently the identity of the peptidyl-prolyl cis-trans isomerase (PPIase), which accelerates the cis/trans isomerization of prolyl peptide bonds and cyclophilin, the binding protein for the immunosuppressive drug Cyclosporin A (CsA), was discovered.
Dorothee Hübner +7 more
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