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PARP4 gene

Known as: VAULT POLY(ADP-RIBOSE) POLYMERASE, VAULT3, POLY(ADP-RIBOSE) POLYMERASE 4 
 
National Institutes of Health

Papers overview

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2006
2006
Vaults are highly conserved, ubiquitous ribonucleoprotein (RNP) particles with an unidentified function. For the three protein… Expand
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Review
2005
Review
2005
The poly(ADP-ribose)polymerases (PARPs) catalyse the transfer of ADP-ribose units from the substrate NAD(+) to acceptor proteins… Expand
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Highly Cited
2004
Highly Cited
2004
Previous studies have demonstrated that expression of p193 and p53 mutants with dominant-interfering activities renders embryonic… Expand
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2003
2003
Poly(ADP-ribose) polymerases (PARPs) are a group of protein-modifying and nucleotide-polymerizing enzymes able to catalyze the… Expand
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2002
2002
Vaults consist of multiple copies of three proteins (MVP, VPARP, and TEP1) and several untranslated RNAs. The function of vaults… Expand
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Highly Cited
2001
Highly Cited
2001
Vaults are ribonucleoprotein complexes comprised of the 100 kDa major vault protein (MVP), the 2 high m.w. vault proteins p193… Expand
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Highly Cited
2001
Highly Cited
2001
Human vaults are intracellular ribonucleoprotein particles believed to be involved in multidrug resistance. The complex consists… Expand
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2001
2001
Abstract— Expression of adenoviral E1A in cardiomyocytes results in the activation of DNA synthesis followed by apoptosis. In… Expand
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Highly Cited
2000
Highly Cited
2000
The vault complex is a ubiquitous 13-MDa ribonucleoprotein assembly, composed of three proteins (TEP1, 240 kDa; VPARP, 193 kDa… Expand
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Highly Cited
2000
Highly Cited
2000
A 193-kDa SV40 large T antigen (T-Ag)-binding protein, designated p193, was identified and cloned. Inspection of the deduced… Expand
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