Results 1 to 10 of about 2,931 (173)

The kingdom of the prolyl-isomerase Pin1: The structural and functional convergence and divergence of Pin1

open access: yesFrontiers in Cell and Developmental Biology, 2022
More than 20 years since its discovery, our understanding of Pin1 function in various diseases continues to improve. Pin1 plays a crucial role in pathogenesis and has been implicated in metabolic disorders, cardiovascular diseases, inflammatory diseases,
Yew Mun Lee   +3 more
doaj   +3 more sources

Pin1 in Neuronal Apoptosis [PDF]

open access: yesCell 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
openaire   +3 more sources

PIN1-Independent Leaf Initiation in Arabidopsis     [PDF]

open access: yesPlant 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
openaire   +7 more sources

Pin1 cysteine-113 oxidation inhibits its catalytic activity and cellular function in Alzheimer's disease

open access: yesNeurobiology of Disease, 2015
The unique proline isomerase Pin1 is pivotal for protecting against age-dependent neurodegeneration in Alzheimer's disease (AD), with its inhibition providing a molecular link between tangle and plaque pathologies.
Chun-Hau Chen   +2 more
exaly   +3 more sources

Activity and Affinity of Pin1 Variants [PDF]

open access: yesMolecules, 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
openaire   +3 more sources

The linchpin? Pin1 meets p73 [PDF]

open access: yesCancer 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
openaire   +3 more sources

Oncogenic Hijacking of the PIN1 Signaling Network [PDF]

open access: yesFrontiers 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   +7 more sources

Direct Delivery of Recombinant Pin1 Protein Rescued Osteoblast Differentiation of Pin1‐Deficient Cells

open access: yesJournal 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   +4 more sources

Targeting PIN1 as a Therapeutic Approach for Hepatocellular Carcinoma [PDF]

open access: yesFrontiers 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   +2 more sources

Dissecting Pin1 and phospho‐pRb regulation

open access: yesJournal 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
openaire   +4 more sources

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