Results 71 to 80 of about 11,541 (227)

The prolyl-isomerase Pin1 maintains heterochromatin by preserving nuclear envelope structure in brain tissue. [PDF]

open access: yes, 2019
The organization of chromatin is tightly regulated, being crucial for the control of gene expression programs, both during organism development and in tissue homeostasis. In particular, perinuclear heterochromatin has an evolutionarily conserved function
Ferrari Bravo, Gloria
core  

Functional characterization of 42 CK2α de novo variants associated with Okur‐Chung neurodevelopmental syndrome

open access: yesThe FEBS Journal, EarlyView.
Okur‐Chung neurodevelopmental syndrome (OCNDS) is a neurodevelopmental disorder associated with mutations in the gene coding for Protein kinase CK2α. In this work, 42 variants of CK2α associated with OCNDS were characterized in vitro. This included determination of catalytic activity and CK2α/CK2β‐interaction as well as an assessment of evolutionary ...
Alexander Gast   +3 more
wiley   +1 more source

THE MODEL FOR AUXIN REGULATED AtPIN1 EXPRESSION IN THE ROOT APICAL MERISTEM [PDF]

open access: yesJournal of Stress Physiology & Biochemistry, 2012
Plant hormone auxin regulates many aspects of plant growth and development. PIN-FORMED (PIN) gene family encodes transmembrane proteins, which mediate auxin efflux.
Ermakov A.A.   +6 more
doaj  

Ubiquitin and ubiquitin‐like modifications in the endoplasmic reticulum stress response

open access: yesThe FEBS Journal, EarlyView.
Endoplasmic reticulum (ER) stress activates various proteostasis control processes, including the unfolded protein response, ribosome‐associated quality control, and ER‐associated degradation. Ubiquitin and ubiquitin‐like modifications dynamically regulate these processes to determine cell fate, promoting adaptation or inducing cell death.
Tony Avril   +2 more
wiley   +1 more source

Stereospecific gating of functional motions in Pin1 [PDF]

open access: yesProceedings of the National Academy of Sciences, 2011
Pin1 is a modular enzyme that accelerates the cis - trans isomerization of phosphorylated-Ser/Thr-Pro (pS/T-P) motifs found in numerous signaling proteins regulating cell growth and neuronal survival.
Andrew T, Namanja   +6 more
openaire   +2 more sources

Pin1-mediated prolyl isomerization of Runx1 affects PU.1 expression in pre-monocytes [PDF]

open access: yes, 2014
Regulation of the hematopoietic transcription factor PU.1, a member of the ETS family, plays a critical role in the development of blood cells and in leukemia. The dosage of PU.1 has been shown to cause a shift in myelomonocytic progenitor fate.
J-H Baek (13628332)   +4 more
core  

PIN1 gene variants in Alzheimer's disease [PDF]

open access: yes, 2009
Background Peptidyl-prolyl isomerase, NIMA-interacting 1 (PIN1) plays a significant role in the brain and is implicated in numerous cellular processes related to Alzheimer's disease (AD) and other neurodegenerative conditions.
Berdynski, Mariusz   +38 more
core   +1 more source

Protein Never in Mitosis Gene A Interacting-1 regulates calpain activity and the degradation of cyclooxygenase-2 in endothelial cells

open access: yesJournal of Inflammation, 2009
Background The peptidyl-proline isomerase, Protein Never in Mitosis Gene A Interacting-1 (PIN1), regulates turnover of inducible nitric oxide synthase (iNOS) in murine aortic endothelial cells (MAEC) stimulated with E. coli endotoxin (LPS) and interferon-
Likhotvorik Rostislav I   +6 more
doaj   +1 more source

Human APOBEC3G suppresses homologous recombination and LIG4‐independent end joining in DNA double‐strand break repair

open access: yesThe FEBS Journal, EarlyView.
Chromosomal DNA double‐strand breaks (DSBs) are repaired by homologous recombination and nonhomologous end joining (NHEJ). Recent work has additionally established theta‐mediated end‐joining (TMEJ) as a mechanism for DSB joining. Cells lacking NHEJ and TMEJ can repair DSBs in a homology‐dependent manner.
Shinta Saito   +6 more
wiley   +1 more source

Proline Isomerase Pin1 represses terminal differentiation and Myocyte Enhancer Factor 2C function in Skeletal Muscle Cells [PDF]

open access: yes, 2011
MEF2 (myocyte enhancer factor 2) transcription factors (MEF2A-D) are highly expressed in skeletal muscle cells, they bind to a conserved AT rich DNA sequence through their N-ter MADS and MEF2 domains and activate transcription via their C-ter ...
MAGLI, Alessandro   +7 more
core  

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