Results 11 to 20 of about 11,541 (227)
Pin1 in Neuronal Apoptosis [PDF]
Cell Cycle, 2007 While the role of the prolyl isomerase Pin1 in dividing cells has long been recognized, Pin1's function in postmitotic neurons is poorly understood. We have identified a novel mechanism by which Pin1 mediates activation of the mitochondrial cell death machinery specifically in neurons.
Becker, E, Bonni, A
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PIN1-Independent Leaf Initiation in Arabidopsis [PDF]
Plant Physiology, 2012 AbstractPhyllotaxis, the regular arrangement of leaves and flowers around the stem, is a key feature of plant architecture. Current models propose that the spatiotemporal regulation of organ initiation is controlled by a positive feedback loop between the plant hormone auxin and its efflux carrier PIN-FORMED1 (PIN1).
Guenot, B +7 more
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Activity and Affinity of Pin1 Variants [PDF]
Molecules, 2019 Pin1 is a peptidyl-prolyl isomerase responsible for isomerizing phosphorylated S/T-P motifs. Pin1 has two domains that each have a distinct ligand binding site, but only its PPIase domain has catalytic activity. Vast evidence supports interdomain allostery of Pin1, with binding of a ligand to its regulatory WW domain impacting activity in the PPIase ...
Alexandra Born +2 more
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Direct Delivery of Recombinant Pin1 Protein Rescued Osteoblast Differentiation of Pin1‐Deficient Cells [PDF]
Journal of Cellular Physiology, 2017 Pin1 is a peptidyl prolyl cis‐trans isomerase that specifically binds to the phosphoserine‐proline or phosphothreonine‐proline motifs of several proteins. We reported that Pin1 plays a critical role in the fate determination of Smad1/5, Runx2, and β‐catenin that are indispensable nuclear proteins for osteoblast differentiation.
Woo-Jin, Kim +7 more
core +5 more sources
The linchpin? Pin1 meets p73 [PDF]
Cancer Cell, 2004 A recent paper shows that the peptidyl-prolyl isomerase Pin1 conformationally alters p73, promoting its acetylation by p300 in a c-Abl dependent manner. Given previous findings with p53, Pin1 may represent a common mediator linking proapoptotic cooperative activity of the p53 family members.
Urist, Marshall, Prives, Carol
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Dissecting Pin1 and phospho‐pRb regulation [PDF]
Journal of Cellular Physiology, 2012 AbstractThe activity of the Retinoblastoma protein, the master regulator of the cell cycle, is finely regulated by phosphorylation. CDKs and cyclins are major players in phosphorylation and it has been recently discovered that the prolyl isomerase Pin1 is an essential protein that orchestrates this process.
Rizzolio, Flavio +10 more
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Oncogenic Hijacking of the PIN1 Signaling Network [PDF]
Frontiers in Oncology, 2019 Cellular choices are determined by developmental and environmental stimuli through integrated signal transduction pathways. These critically depend on attainment of proper activation levels that in turn rely on post-translational modifications (PTMs) of single pathway members. Among these PTMs, post-phosphorylation prolyl-isomerization mediated by PIN1
Alessandro Zannini +7 more
core +9 more sources
Targeting PIN1 as a Therapeutic Approach for Hepatocellular Carcinoma [PDF]
Frontiers in Cell and Developmental Biology, 2020 PIN1 is a peptidyl-prolyl cis/trans isomerase that specifically binds and catalyzes the cis/trans isomerization of the phosphorylated serine or threonine residue preceding a proline (pSer/Thr-Pro) motif of its interacting proteins.
Chi-Wai Cheng, Eric Tse
doaj +3 more sources
PIN1 in Cell Cycle Control and Cancer [PDF]
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 post-phosphorylation modification and functional regulation of these CDK-phosphorylated proteins ...
Chi-Wai Cheng, Eric Tse
openaire +5 more sources
Stereospecific NANOG PEST Stabilization by Pin1 [PDF]
BiochemistryNANOG protein levels correlate with stem cell pluripotency. NANOG concentrations fluctuate constantly with low NANOG levels leading to spontaneous cell differentiation. Previous literature implicated Pin1, a phosphorylation-dependent prolyl isomerase, as a key player in NANOG stabilization.
Josephine C. Ferreon +8 more
core +5 more sources