Results 31 to 40 of about 11,541 (227)
Pin1-induced cis/trans isomerization of lamin A/C. [PDF]
, 2016 (A-B) NMR spectroscopy of lamin A/C peptides in the presence or absence of Pin1. Superimposed expanded HN-HN regions of the 2D 1H-1H NOESY spectra are depicted for phosphorylated and unphosphorylated versions of a lamin A/C peptide comprising amino acids
Torgils Fossen (1632481) +10 more
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Frontiers in Cellular and Infection Microbiology, 2023 Here, we demonstrate that the peptidyl-prolyl cis/trans isomerase Pin1 interacts noncovalently with the hepatitis B virus (HBV) core particle through phosphorylated serine/threonine-proline (pS/TP) motifs in the carboxyl-terminal domain (CTD) but not ...
Hyeonjoong Kwon +17 more
doaj +1 more source
Landscape of Pin1 in the cell cycle [PDF]
Experimental Biology and Medicine, 2015 Pin1 is a peptidyl-prolyl isomerase which plays a critical role in many diseases including cancer and Alzheimer's disease. The essential role of Pin1 is to affect stability, localization or function of phosphoproteins by catalyzing structural changes. Among the collection of Pin1 substrates, many have been shown to be involved in regulating cell cycle ...
Cheng-Han, Lin +6 more
openaire +2 more sources
Pathology & Oncology Research, 2013 Pin1 (peptidylprolyl cis/trans isomerase, NIMA-interacting 1) plays a key role in a number of diseases including cancer and Alzheimer disease. Previous studies have identified a wide range of phosphoproteins as Pin1 substrates. Related pathways were analyzed separately.
Guo-Liang, Huang +6 more
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Prolyl isomerase Pin1 in cancer [PDF]
Cell Research, 2014 Proline-directed phosphorylation is a posttranslational modification that is instrumental in regulating signaling from the plasma membrane to the nucleus, and its dysregulation contributes to cancer development. Protein interacting with never in mitosis A1 (Pin1), which is overexpressed in many types of cancer, isomerizes specific phosphorylated Ser ...
Zhimin, Lu, Tony, Hunter
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Pin1 Promotes NLRP3 Inflammasome Activation by Phosphorylation of p38 MAPK Pathway in Septic Shock
Frontiers in Immunology, 2021 Pin1 is the only known peptidyl-prolyl cis-trans isomerase (PPIase) that can specifically recognize and isomerize the phosphorylated Serine/Threonine-Proline (pSer/Thr-Pro) motif, change the conformation of proteins through protein phosphorylation, thus ...
Ruijie Dong +6 more
doaj +1 more source
PIN1-induced FAAP20 isomerization promotes PP2A signaling and antagonizes FBW7-dependent FAAP20 degradation. [PDF]
, 2019 (A) 293T cells were transfected with indicated plasmids, and the amount of HA-B56α pulled-down by Flag-FAAP20 was analyzed by anti-Flag IP and WB. (B, C, D) U2OS cells were transfected with indicated plasmids, and pS113 levels of Flag-FAAP20 WT or ...
Markus Seeliger (6388112) +8 more
core +1 more source
Involvement of prolyl isomerase PIN1 in the cell cycle progression and proliferation of hepatic oval cells [PDF]
, 2017 Liver regenerates remarkably after toxic injury or surgical resection. In the case of failure of resident hepatocytes to restore loss, repopulation is carried out by induction, proliferation, and differentiation of the progenitor cell.
Chand, Lokendra +4 more
core +1 more source
Brown Algae Polyphenol, a Prolyl Isomerase Pin1 Inhibitor, Prevents Obesity by Inhibiting the Differentiation of Stem Cells into Adipocytes. [PDF]
PLoS ONE, 2016 While screening for an inhibitor of the peptidyl prolyl cis/trans isomerase, Pin1, we came across a brown algae polyphenol that blocks the differentiation of fibroblasts into adipocytes.
Atsuko Suzuki +4 more
doaj +1 more source
A phosphorylated prodrug for the inhibition of Pin1 [PDF]
Bioorganic & Medicinal Chemistry Letters, 2007 Fmoc-pSer-Psi[(Z)CHC]-Pro-(2)-N-(3)-ethylaminoindole 1, showed moderate inhibition towards the mitotic regulator, Pin1 (IC(50)=28.3microM). To improve the cell permeability, the charged phosphate was masked as the bis-pivaloyloxymethyl (POM) phosphate in Fmoc-(bisPOM)-pSer-Psi[(Z)CHC]-Pro-(2)-N-(3)-ethylaminoindole 2. Antiproliferative activity towards
Song, Zhao, Felicia A, Etzkorn
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