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Mice with a liver overexpression of insulin-like growth factor 2 (IGF2) mRNA-binding protein p62/IMP2-2/IGF2BP2-2 show elevated Ccl2 levels, which models all stages of non-alcoholic fatty liver disease.
We propose that autophagy is inhibited in the alphaB-R120G mutant lenses because of a defect in protein degradation after autophagosome formation.
p62 is up-regulated in mouse proteinopathic hearts and promotes aggresome formation and autophagy activation and protects cardiomyocytes against proteotoxic stress
cdk1 phosphorylates p62 in vitro and in vivo at T269 and S272, which is necessary for the maintenance of appropriate cyclin B1 levels and the levels of cdk1 activity necessary to allow cells to properly enter and exit mitosis.
p62 is a crucial regulator of ERK1 in metabolism
p62 normally antagonizes basal ERK activity and adipocyte differentiation and that its loss leads to the hyperactivation of ERK that favors adipogenesis and obesity.
These data demonstrate that PKCzeta and its adaptor protein p62 play a key role in the modulation of K(V) channel function in pulmonary arteries.
The results unveil a tight connection between TFIIH and KAT2A that controls higher-order chromatin structure and gene expression and provide new insights into transcriptional dysregulation in a cancer-prone DNA repair-deficient disorder, Xeroderma Pigmentosum B-Cockayne Syndrome.
The sensitivity of SWI/SNF-deficient cells to DNA damage induced by UV irradiation and cisplatin treatment depends on GTF2H1 levels.
Data suggest that a common TFIIH subunit p62 recruitment mechanism is shared by UV-stimulated scaffold protein A (UVSSA) in transcription-coupled repair (TCR) and xeroderma pigmentosum, complementation group C protein (XPC) in global genome repair (GGR).
The N-terminal highly acidic region of TFIIEalpha interacts with the pleckstrin homology domain of TFIIH and adopts an extended stringlike structure on the positive groove of the pleckstrin homology domain with two hydrophobic amino acids, Phe387 and Val390, inserting into two shallow hydrophobic pockets of the pleckstrin homology domain.
Here, the authors show that an acidic region of DP1, whose function has remained elusive, binds to the plekstrin homology (PH) domain of the p62 subunit of TFIIH that contributes to transcriptional activation.
Virulence factor NSs of rift valley fever virus recruits the FBXO3 to degrade subunit p62 of general transcription factor TFIIH.
These data suggest that the RVFV NSs protein is able to interact with the TFIIH subunit p62 inside infected cells and promotes its degradation, which can occur directly in the nucleus.
transcription factor b3, previously identified as a component of the transcription factor IIH core complex, is shown instead to be transcription factor b4
p62 subunit of TFIIH interacts with TRbeta in a ligand-dependent manner.
The pleckstrin homology domain from the 62 kDa subunit Tfb1 (residues 1-108) of TFIIH is sufficient for binding to the activation domain of herpes simplex virus protein VP16.
GTF2H1 polymorphisms/haplotypes may contribute to genetic susceptibility to lung cancer.
Component of the core-TFIIH basal transcription factor involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II.
general transcription factor IIH subunit 1
, TFIIH basal transcription factor complex p62 subunit
, basic transcription factor 2 62 kDa subunit
, general transcription factor IIH, polypeptide 1 (62kD subunit)
, general transcription factor IIH, polypeptide 1, 62kDa
, BTF2 p62
, general transcription factor IIH polypeptide 1
, general transcription factor IIH subunit 1-like