Results 51 to 60 of about 19,713 (201)
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
openaire +2 more sources
Tumor suppressive activity of prolyl isomerase Pin1 in renal cell carcinoma
Molecular Oncology, 2011 Pin1 specifically recognizes and catalyzes the cis‐trans isomerization of phosphorylated‐Ser/Thr‐Pro bonds, which modulate the stability, localization, and function of numerous Pin1 targets involved in tumor progression.
Brian L. Teng +4 more
doaj +1 more source
Acta Cirúrgica Brasileira, 2022 Purpose: To investigate the role of peptidyl-prolyl cis/trans isomerase 1 (Pin1) on renal ischemia-reperfusion (I/R) injury and underlying mechanism. Methods: By establishing the in vitro and in vivo models of renal I/R, the role of Pin1 was explored by
Honglin Yu +3 more
doaj +1 more source
PLoS ONE, 2014 The peptidyl-prolyl isomerase Pin1 is over-expressed in several cancer tissues is a potential prognostic marker in prostate cancer, and Pin1 ablation can suppress tumorigenesis in breast and prostate cancers.
Nithya Krishnan +2 more
doaj +1 more source
Pin1 positively affects tumorigenesis of esophageal squamous cell carcinoma and correlates with poor survival of patients [PDF]
, 2014 BACKGROUND: Pin1 promotes oncogenesis by regulating multiple oncogenic signaling. In this study, we investigated the involvement of Pin1 in tumor progression and in the prognosis of human esophageal squamous cell carcinoma (ESCC).
Bor-Shyang Sheu +9 more
core +1 more source
Gears-In-Motion: The Interplay of WW and PPIase Domains in Pin1
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
doaj +1 more source
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
openaire +4 more sources
WUSCHEL Transcription Factor: From Stem Cell Maintenance to Crop Improvement
Advanced Science, EarlyView.This review synthesizes emerging insights into WUSCHEL (WUS) as a central regulator of plant stem cell fate beyond Arabidopsis, highlighting its roles in regeneration, somatic embryogenesis (SE), and stress adaptation across crops. It explores how WUS‐centered regulatory networks, genome editing, and AI‐guided strategies can be leveraged for precise ...
Zishan Ahmad +6 more
wiley +1 more source
The role of the master cancer regulator Pin1 in the development and treatment of cancer
Frontiers in Cell and Developmental BiologyThis review examines the complex role of Pin1 in the development and treatment of cancer. Pin1 is the only peptidyl–prolyl isomerase (PPIase) that can recognize and isomerize phosphorylated Ser/Thr-Pro peptide bonds. Pin1 catalyzes a structural change in
Robert Stewart +13 more
doaj +1 more source
Journal of Hematology & Oncology, 2018 Background The increasing genomic complexity of acute myeloid leukemia (AML), the most common form of acute leukemia, poses a major challenge to its therapy.
Xiaolan Lian +20 more
doaj +1 more source