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The protein encoded by CPSF6 is one subunit of a cleavage factor required for 3' RNA cleavage and polyadenylation processing. Zusätzlich bieten wir Ihnen CPSF6 Proteine (5) und viele weitere Produktgruppen zu diesem Protein an.
Showing 10 out of 55 products:
Human Polyclonal CPSF6 Primary Antibody für WB - ABIN1881225
Lee, Ambrose, Martin, Oztop, Mulky, Julias, Vandegraaff, Baumann, Wang, Yuen, Takemura, Shelton, Taniuchi, Li, Sodroski, Littman, Coffin, Hughes, Unutmaz, Engelman, KewalRamani: Flexible use of nuclear import pathways by HIV-1. in Cell host & microbe 2010
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Human Polyclonal CPSF6 Primary Antibody für ICC, IF - ABIN253249
Fricke, Valle-Casuso, White, Brandariz-Nuñez, Bosche, Reszka, Gorelick, Diaz-Griffero: The ability of TNPO3-depleted cells to inhibit HIV-1 infection requires CPSF6. in Retrovirology 2013
Show all 3 Pubmed References
Human Polyclonal CPSF6 Primary Antibody für ICC, IF - ABIN4300333
De Iaco, Santoni, Vannier, Guipponi, Antonarakis, Luban: TNPO3 protects HIV-1 replication from CPSF6-mediated capsid stabilization in the host cell cytoplasm. in Retrovirology 2013
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Human Monoclonal CPSF6 Primary Antibody für IF, ELISA - ABIN524445
Kim, Yamamoto, Chen, Aida, Wada, Handa, Yamaguchi: Evidence that cleavage factor Im is a heterotetrameric protein complex controlling alternative polyadenylation. in Genes to cells : devoted to molecular & cellular mechanisms 2010
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Here we report that the CFIm subunits NUDT21/CPSF5 (zeige NUDT21 Antikörper) and CPSF6 are highly enriched in mouse male germ cells relative to somatic cells.
Studies suggest that binding of cleavage factor Im (CFIm) may be one of the earliest steps in promoting formation of an active cleavage complex.
CPSF6 binding to its docking site in HIV-1 capsid leads to the recruitment of CFIm tetramer, suggesting that CFIm mediates CPSF6 function(s) in integration site targeting.
integration targeting proceeds via two distinct mechanisms: capsid-CPSF6 binding directs HIV-1 to actively transcribed euchromatin, where the integrase-LEDGF/p75 (zeige PSIP1 Antikörper) interaction drives integration into gene bodies.
NUP153 (zeige NUP153 Antikörper) and CPSF6 have overlapping binding sites, but each makes unique capsid monomers (CA) interactions. Multiple ligands share an overlapping interface in HIV-1 capsid that is lost upon viral disassembly.
Structural basis of HIV-1 capsid recognition by PF74 and CPSF6.
study uncovers two opposing CA-dependent functions of CPSF6 in HIV-1 replication in vivo; however, the benefit for binding CPSF6 appears to outweigh the cost, providing support for a vital function of CPSF6 during HIV-1 replication in vivo
CPSF6 binds specifically to a novel proteinprotein interface on the N-terminal domain of HIV-1 capsid protein (CA).
These results suggested that inhibition of HIV-1 by TNPO3 (zeige TNPO3 Antikörper)-depleted cells requires CPSF6.
Loss-of-function of CFIm68 and CFIm25 (zeige NUDT21 Antikörper) leads to a transcriptome-wide increase in the use of proximal polyadenylation sites in HEK293 cells.
TNPO3 (zeige TNPO3 Antikörper) promotes HIV-1 infectivity indirectly, by shifting the CA-binding protein CPSF6 to the nucleus, thus preventing the excessive HIV-1 CA stability that would otherwise result from cytoplasmic accumulation of CPSF6.
The protein encoded by this gene is one subunit of a cleavage factor required for 3' RNA cleavage and polyadenylation processing. The interaction of the protein with the RNA is one of the earliest steps in the assembly of the 3' end processing complex and facilitates the recruitment of other processing factors. The cleavage factor complex is composed of four polypeptides. This gene encodes the 68kD subunit. It has a domain organization reminiscent of spliceosomal proteins.
cleavage and polyadenylation specific factor 6, 68kDa
, cleavage and polyadenylation specificity factor subunit 6
, cleavage and polyadenylation specific factor 6, 68 kD subunit
, CPSF 68 kDa subunit
, cleavage and polyadenylation specificity factor 68 kDa subunit
, cleavage factor Im complex 68 kDa subunit
, pre-mRNA cleavage factor I, 68kD subunit
, pre-mRNA cleavage factor Im (68kD)
, pre-mRNA cleavage factor Im 68 kDa subunit
, protein HPBRII-4/7