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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

MyoD family inhibitor domain containing

Hic, I-mfa domain-containing protein
This gene product is a member of a family of proteins characterized by a specific cysteine-rich C-terminal domain, which is involved in transcriptional regulation of viral genome expression. Alternative translation initiation from an upstream non-AUG (GUG), and an in-frame, downstream AUG codon, results in the production of two isoforms, p40 and p32, respectively, which have different subcellular localization; p32 is mainly found in the cytoplasm, whereas p40 is targeted to the nucleolus. Both isoforms have transcriptional regulatory activity that is attributable to the cysteine-rich C-terminal domain. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Oct 2009] (from NCBI)
Top mentioned proteins: Hic-5, paxillin, LIM, CAN, Actin
Papers using Hic antibodies
A role for the juxtamembrane cytoplasm in the molecular dynamics of focal adhesions.
Parsons Maddy, In PLoS ONE, 2008
... paxillin and Hic-5 by Western blotting and immunofluorescence the mouse anti-paxillin (clone 165) and mouse anti-Hic-5 (BD Biosciences, Franklin Lakes, NJ) were ...
Amoeboid shape change and contact guidance: T-lymphocyte crawling through fibrillar collagen is independent of matrix remodeling by MMPs and other proteases.
Parsons Maddy, In PLoS ONE, 2002
... controls instead of wild-type MEFs because commercial antibodies to paxillin also recognize the FA protein Hic-5.Recombinant human PDGF-BB was obtained from BioVision.
Papers on Hic
Hic-5 mediates endothelial sprout initiation by regulating a key surface metalloproteinase.
Bayless et al., College Station, United States. In J Cell Sci, Feb 2016
We tested here whether the focal adhesion scaffold protein Hic-5 regulated endothelial sprouting in three-dimensions.
Hic-5 is required for myofibroblast differentiation by regulating mechanically dependent MRTF-A nuclear accumulation.
Van De Water et al., Albany, United States. In J Cell Sci, Feb 2016
We report here that the focal adhesion protein, Hic-5, is required for the mechanically dependent generation of stress fibers in response to TGF-β.
Hic-5 deficiency attenuates the activation of hepatic stellate cells and liver fibrosis through upregulation of Smad7 in mice.
Miyazaki et al., Tokyo, Japan. In J Hepatol, Jan 2016
BACKGROUND & AIM: Hydrogen peroxide-inducible clone-5 (Hic-5), also named as transforming growth factor beta-1-induced transcript 1 protein (Tgfb1i1), was found to be induced by TGF-β.
Tagged Chromosomal Insertion Site System: A Method to Study Lamina-Associated Chromatin.
Reddy et al., Baltimore, United States. In Methods Enzymol, Dec 2015
This system can be used to study the minimal DNA sequences that target the nuclear periphery (or other nuclear compartments), allowing researchers to understand how genome-wide results obtained, for example, by DNA adenine methyltransferase identification, chromosome conformation capture (HiC), or related methods, connect to the actual organization of DNA and chromosomes at the single-cell level.
Extracellular matrix-induced Hic-5 expression in glomerular mesangial cells leads to a prosclerotic phenotype independent of TGF-β.
Mooney et al., Leeds, United Kingdom. In Faseb J, Dec 2015
Mesangial cell expression of the LIM protein hydrogen peroxide-induced clone-5 (Hic-5) is important in its pathogenesis.
Hydrogen peroxide inducible clone-5 mediates reactive oxygen species signaling for hepatocellular carcinoma progression.
Wu et al., Taiwan. In Oncotarget, Nov 2015
Hydrogen peroxide inducible clone-5 (Hic-5), one of the paralogs of paxillin, exhibits many biological functions distinct from paxillin, but may cooperate with paxillin to trigger tumor progression.
Non-receptor tyrosine kinases and the actin cytoskeleton in contractile vascular smooth muscle.
Ohanian et al., Manchester, United Kingdom. In J Physiol, Oct 2015
Recent work has shown that non-receptor tyrosine kinases and tyrosine phosphorylation of focal adhesion proteins such as paxillin and Hic-5 are important for actin cytoskeleton and focal adhesion remodelling and contraction.
Hic-5 Regulates Actin Cytoskeletal Reorganization and Expression of Fibrogenic Markers and Myocilin in Trabecular Meshwork Cells.
Rao et al., Durham, United States. In Invest Ophthalmol Vis Sci, Aug 2015
PURPOSE: To explore the role of inducible focal adhesion (FA) protein Hic-5 in actin cytoskeletal reorganization, FA formation, fibrogenic activity, and expression of myocilin in trabecular meshwork (TM) cells.
Involvement of Mechanical Stress in Androgenetic Alopecia.
Tellez-Segura, Almería, Spain. In Int J Trichology, Jul 2015
Recent research shows that hair follicle androgen sensitivity is regulated by Hic-5, an androgen receptor co-activator which may be activated by the mechanical stimulation.
Can chromatin conformation technologies bring light into human molecular pathology?
Lewandowska et al., Bydgoszcz, Poland. In Acta Biochim Pol, 2014
Here we review and compare the original 3C and 3C-based methods including chromosome conformation capture-on-chip (4C), chromosome conformation capture carbon copy (5C), hi-resolution chromosome confomation capture (HiC).
Spatial reorganization of telomeres in long-lived quiescent cells.
Taddei et al., Paris, France. In Genome Biol, 2014
RESULTS: Here, combining live microscopy, DNA FISH and chromosome conformation capture (HiC) techniques, we report that chromosomes adopt distinct organizations according to the metabolic status of the cell.
The statistical-mechanics of chromosome conformation capture.
Langowski et al., Auckland, New Zealand. In Nucleus, 2013
Proximity ligation assays commonly known as chromosome conformation capture (3C) and 3C based methodologies (e.g., GCC, HiC and ChIA-Pet) are increasingly being incorporated into empirical studies to investigate the role that three-dimensional genome structure plays in the regulation of phenotype.
Chromatin looping and organization at developmentally regulated gene loci.
Duboule et al., Lausanne, Switzerland. In Wiley Interdiscip Rev Dev Biol, 2013
In recent years, the development of 3C and derived techniques (4C, 5C, HiC, ChIA-PET, etc.) has confirmed that chromatin looping is an important mechanism for the transfer of regulatory information in mammalian cells.
Hydrogen peroxide-inducible clone 5 (Hic-5) as a potential therapeutic target for vascular and other disorders.
Miyazaki et al., Tokyo, Japan. In J Atheroscler Thromb, 2011
Hydrogen peroxide-inducible clone-5 (Hic-5) is a focal adhesion scaffold protein primarily expressed in vascular and visceral smooth muscle cells.
Intermolecular masking of the HIV-1 Rev NLS by the cellular protein HIC: novel insights into the regulation of Rev nuclear import.
Gautier et al., Dublin, Ireland. In Retrovirology, 2010
We demonstrate that HIC selectively interferes with Rev NLS interaction with importin beta and impedes its nuclear import and function, but does not affect Rev nuclear import mediated by transportin.
Human I-mfa domain proteins specifically interact with KSHV LANA and affect its regulation of Wnt signaling-dependent transcription.
Eizuru et al., Kagoshima, Japan. In Biochem Biophys Res Commun, 2010
These data reveal for the first time that I-mfa domain proteins interact with LANA and negatively regulate LANA-mediated activation of Wnt signaling-dependent transcription by inhibiting the formation of the LANA.GSK-3beta complex.
Slit2-Robo4 signalling promotes vascular stability by blocking Arf6 activity.
Li et al., Salt Lake City, United States. In Nat Cell Biol, 2009
Here, we demonstrate that Robo4 mediates Slit2-dependent suppression of cellular protrusive activity through direct interaction with the intracellular adaptor protein paxillin and its paralogue, Hic-5.
Expression profile and differential regulation of the Human I-mfa domain-Containing protein (HIC) gene in immune cells.
Gautier et al., Dublin, Ireland. In Immunol Lett, 2009
This study describes that the immune expression of HIC is cell-specific, dynamic, and identifies the HIC gene as an IL-2 responsive gene.
The complex regulation of HIC (Human I-mfa domain containing protein) expression.
Naveh-Many et al., Jerusalem, Israel. In Plos One, 2008
strict regulation of HIC expression at the levels of mRNA stability, translation efficiency and protein stability suggests that expression of the HIC protein and its involvement in the various pathways is required only under specific cellular conditions
Molecular cloning of a novel human I-mfa domain-containing protein that differently regulates human T-cell leukemia virus type I and HIV-1 expression.
Mesnard et al., Montpellier, France. In J Biol Chem, 2000
Two isoforms, resulting from the use of a non-AUG (GUG) and a downstream in-frame AUG translation initiation codon, have different subcellular localization.
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