Results 21 to 30 of about 2,931 (173)

Prolyl Isomerase Pin1 Suppresses Thermogenic Programs in Adipocytes by Promoting Degradation of Transcriptional Co-activator PRDM16

open access: yesCell Reports, 2019
Summary: Non-shivering thermogenesis in adipocytes provides defense against low temperatures and obesity development, but the underlying regulatory mechanism remains to be fully clarified.
Yusuke Nakatsu   +24 more
doaj   +1 more source

Hyperglycemia induces gastric carcinoma proliferation and migration via the Pin1/BRD4 pathway

open access: yesCell Death Discovery, 2022
Diabetes is a potential risk factor for gastric cancer (GC). Pin1, a peptidyl–prolyl cis/trans isomerase, promotes GC cell proliferation and migration.
Jianjian Yu   +8 more
doaj   +1 more source

Pin1: A molecular orchestrator in the heart [PDF]

open access: yesTrends in Cardiovascular Medicine, 2014
Pin1 is an evolutionarily conserved peptidyl-prolyl isomerase that binds and changes the three-dimensional conformation of specific phospho-proteins. By regulating protein structure and folding, Pin1 affects the stability, interaction, and activity of a broad spectrum of target proteins, thus impacting upon diverse cellular processes.
Nirmala, Hariharan, Mark A, Sussman
openaire   +2 more sources

Pin1 and JNK1 cooperatively modulate TAp63γ [PDF]

open access: yesFEBS Open Bio, 2021
Thep63gene encodes at least 10 isoforms, which can be classified into TA and ∆N isotypes (TAp63 and ∆Np63 proteins) according to their differences at the N termini. TAp63γ is an important transcription factor. We previously reported that peptidyl‐prolyl isomerase (PPI) Pin1 directly binds to TAp63γ protein and identified that serine 12 (S12) in the ...
Xueying Fan   +6 more
openaire   +3 more sources

Serum peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 in combination with C-reactive protein and white blood cell as novel predictors for infants with community-acquired pneumonia

open access: yesEuropean Journal of Inflammation, 2020
The aim of this study was to investigate the predictive value of peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) with C-reactive protein (CRP) and white blood cell (WBC) count for community-acquired pneumonia (CAP) in infants. A total of 84
Heng Xue   +8 more
doaj   +1 more source

Peptidyl-prolyl cis/trans isomerase Pin1 interacts with hepatitis B virus core particle, but not with HBc protein, to promote HBV replication

open access: yesFrontiers 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

Prolyl isomerase Pin1 in cancer [PDF]

open access: yesCell 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
openaire   +2 more sources

Immunohistochemical Expression of Cyclin D1 and PIN1 in Endometrial Carcinoma [PDF]

open access: yesInternational Journal of Medical Arts, 2021
Background: Cyclin D1, a positive regular of the cell cycle, may lead to uncontrolled cell proliferation. Overexpression of Cyclin D1 has been associated with the diagnosis and prognosis of numerous tumors.
Shimaa Abu_Seadah   +2 more
doaj   +1 more source

Targeting Pin1 for Modulation of Cell Motility and Cancer Therapy

open access: yesBiomedicines, 2021
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) specifically binds and isomerizes the phosphorylated serine/threonine-proline (pSer/Thr-Pro) motif, which leads to changes in protein conformation and function. Pin1 is widely overexpressed in
Hsiang-Hao Chuang   +6 more
doaj   +1 more source

Prolyl Isomerase Pin1 Regulated Signaling Pathway Revealed by Pin1 +/+ and Pin1 −/− Mouse Embryonic Fibroblast Cells

open access: yesPathology & 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
openaire   +2 more sources

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