Results 51 to 60 of about 11,541 (227)

The prolyl isomerase pin1 regulates mRNA levels of genes with short half-lives by targeting specific RNA binding proteins.

open access: yesPLoS 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 and PIN4 inhibition via parvulin impeders Juglone, PiB, ATRA, 6,7,4′-THIF, KPT6566, and EGCG thwarted hepatitis B virus replication

open access: yesFrontiers in Microbiology, 2023
IntroductionHuman parvulin peptidyl prolyl cis/trans isomerases PIN1 and PIN4 play important roles in cell cycle progression, DNA binding, protein folding and chromatin remodeling, ribosome biogenesis, and tubulin polymerization.
Umar Saeed, Zahra Zahid Piracha
doaj   +1 more source

Prolyl Isomerase Pin1 Regulates the Stability of Hepatitis B Virus Core Protein

open access: yesFrontiers in Cell and Developmental Biology, 2020
The dynamic interplay between virus and host proteins is critical for establishing efficient viral replication and virus-induced pathogenesis. Phosphorylation-dependent prolyl isomerization by Pin1 provides a unique mechanism of molecular switching to ...
Mayuko Nishi   +10 more
doaj   +1 more source

Peptidyl Prolyl Isomerase PIN1 Directly Binds to and Stabilizes Hypoxia-Inducible Factor-1α. [PDF]

open access: yesPLoS ONE, 2016
Peptidyl prolyl isomerase (PIN1) regulates the functional activity of a subset of phosphoproteins through binding to phosphorylated Ser/Thr-Pro motifs and subsequently isomerization of the phosphorylated bonds.
Hyeong-Jun Han   +13 more
doaj   +1 more source

Peptidthioester und Peptidtriazolderivate durch Duale Modifikation von Peptidthiosulfonaten auf dem Harz

open access: yesAngewandte Chemie, EarlyView.
Es wird eine Strategie zur dualen Modifikation von Peptiden auf der Festphase vorgestellt, die die S‐Alkinylierung von Peptidthiosulfonaten und eine regioselektive, iridiumkatalysierte Azid‐Thioalkin‐Zykloaddition umfasst. Dieses Verfahren ermöglicht zuverlässig den Zugang zu Peptiden mit komplexen, nicht‐kanonischen Modifikationen und ist mit ...
Marius Werner   +5 more
wiley   +1 more source

Analysis of the interaction of TIP60β and PIN1 with the ets family transcription factor ETV6 [PDF]

open access: yes, 2005
The ETV6 gene is involved in many chromosomal translocations forming different fusion genes in both myeloid and lymphoid leukemias as well as in some solid tumors.
Zhang, Chang-Dong
core  

Gears-In-Motion: The Interplay of WW and PPIase Domains in Pin1

open access: yesFrontiers 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

Peptide Thioester and Triazole Derivatives Through On‐Resin Dual‐Modification of Peptide Thiosulfonates

open access: yesAngewandte Chemie International Edition, EarlyView.
An on‐resin dual‐modification strategy for peptides is presented, comprising S‐alkynylation of peptide thiosulfonates and regioselective iridium‐catalyzed azide–thioalkyne cycloaddition. This method reliably provides access to peptides with intricate non‐canonical modifications, being compatible with complex peptides, alkynes and azides.
Marius Werner   +5 more
wiley   +1 more source

Pin1 targets Grb7 for proteasome-mediated degradation. [PDF]

open access: yes, 2016
(A) shLuc- or shPin1-infected A431 cells were treated with cycloheximide (CHX, 25 μg/ml) for the indicated times to stop protein translation. Cell lysates were collected and subjected to Western blotting with anti-Pin1, anti-Grb7, or anti-AKT antibody ...
Hsinyu Lee (149656)   +9 more
core   +1 more source

The role of the master cancer regulator Pin1 in the development and treatment of cancer

open access: yesFrontiers in Cell and Developmental Biology
This 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

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