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Host cell factor C2

HCF-2, C2 factor
This gene encodes one of two proteins which interact with VP16, a herpes simplex virus protein that initiates virus infection. Both the encoded protein and the original Herpes host cell factor interact with VP16 through a beta-propeller domain. The original Herpes host cell factor, however, is effective at initiating viral infection while the encoded protein is not. Transcripts of varying length due to alternative polyadenylation signals have been described. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Host Cell Factor C1, CAN, ACID, Oct-1, fibronectin
Papers on HCF-2
Role of early lectin pathway activation in the complement-mediated killing of Trypanosoma cruzi.
Ramirez et al., Rio de Janeiro, Brazil. In Mol Immunol, 2009
Furthermore, lectin pathway activation by T. cruzi required the MBL-associated serine protease 2 (MASP2) activity resulting in C2 factor cleavage.
Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression.
Cleary et al., Stanford, United States. In Mol Cell Biol, 2004
Two other members of the novel MLL complex identified here are host cell factor 1 (HCF-1), a transcriptional coregulator, and the related HCF-2, both of which specifically interact with a conserved binding motif in the MLL(N) (p300) subunit of MLL and provide a potential mechanism for regulating its antagonistic transcriptional properties.
A C-terminal targeting signal controls differential compartmentalisation of Caenorhabditis elegans host cell factor (HCF) to the nucleus or mitochondria.
O'Hare et al., Maglie, Italy. In Eur J Cell Biol, 2003
A related protein HCF-2 is also present in humans and while at least HCF-1 appears to be required for normal cell growth there is currently little information on the precise cellular role(s) of these proteins.
Primary structure and compartmentalization of Drosophila melanogaster host cell factor.
O'Hare et al., Maglie, Italy. In Gene, 2003
A unique HCF orthologue has been found in Caenorhabditis elegans which is structurally more related to HCF-2 than HCF-1.
Molecular cloning of Drosophila HCF reveals proteolytic processing and self-association of the encoded protein.
Wilson et al., New York City, United States. In J Cell Physiol, 2003
Additional HCF proteins have been identified in mammals (HCF-2) and Caenorhabditis elegans (CeHCF).
PDCD2 is a negative regulator of HCF-1 (C1).
Sharp et al., Cambridge, United States. In Oncogene, 2002
This inter-action is conserved between human HCF-1 and HCF-2 and the C. elegans HCF.
Stabilization but not the transcriptional activity of herpes simplex virus VP16-induced complexes is evolutionarily conserved among HCF family members.
Herr et al., New York City, United States. In J Virol, 2001
HCF-1 and the related protein HCF-2 form an HCF protein family in humans that is related to a Caenorhabditis elegans homolog called CeHCF.
Developmental and cell-cycle regulation of Caenorhabditis elegans HCF phosphorylation.
Herr et al., New York City, United States. In Biochemistry, 2001
HCF-1 and a related protein called HCF-2 possess a homologue in Caenorhabditis elegans that can associate with and activate VP16.
HCF-1 amino- and carboxy-terminal subunit association through two separate sets of interaction modules: involvement of fibronectin type 3 repeats.
Herr et al., New York City, United States. In Mol Cell Biol, 2000
Unexpectedly, the related protein HCF-2, which is not proteolyzed, also contains a functional SAS1 association element, suggesting that this element does not function solely to maintain HCF-1(N) and HCF-1(C) subunit association.
Herpes simplex virus transactivator VP16 discriminates between HCF-1 and a novel family member, HCF-2.
Wilson et al., New York City, United States. In J Virol, 1999
Here we describe the identification of a second HCF-like protein, designated HCF-2.
C-myc gene binding factors in peripheral blood mononuclear cells from patients with systemic lupus erythematosus (SLE).
Kishimoto et al., Ōsaka, Japan. In Clin Exp Immunol, 1989
The binding site of the C1 factor (C1F) and C2 factor (C2F) which forms C1 and C2 respectively with Fmyc appeared to be common and were found to reside at 51 kbp sequence (from XhoI to Sau3A) of exon I of c-myc gene.
DNA polymorphism of MHC III genes in inbred and wild mouse strains.
Colten et al., In Immunogenetics, 1986
Conservation of the C2 factor B gene duplex was evidenced by relatively limited polymorphism associated with speciation and nucleotide sequence homology between mouse and human C2 and factor B. The C4-Slp gene duplex, on the other hand, showed extensive polymorphism by DNA blot analysis.
[Reduction of dehydroascorbic acid by thiols in presence of biocatalytic substances: polarographic study].
Devynck et al., In Int J Vitam Nutr Res, 1981
This catalytic effect is specifically obtained with flavan-3 ol complex with antiscorbutic activities of C2 factor type.
[Main part of two factors of exogenous origin contained in the blood capillary wall (author's transl)].
Mousseron et al., In J Mal Vasc, 1980
Besides the l-ascorbic acid (C1 factor), we put in evidence the l-epi-3',4',5',5,7-pentahydroxyflavan-3-ol (C2 factor) in the blood capillary wall.
Experimental botulism in chickens: the cecum as the site of production and absorption of botulinum toxin.
Sakaguchi et al., In Jpn J Med Sci Biol, 1978
Peroral administration of spores of a type C strain cured of its prophages and producing the C2 factor only also killed normal chickens.
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