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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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Review
2007
Review
2007
The polyADP‐ribosylation reaction results in a unique post‐translational modification involved in various cellular processes and… Expand
2006
2006
Vaults are highly conserved, ubiquitous ribonucleoprotein (RNP) particles with an unidentified function. For the three protein… Expand
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
Review
2003
Review
2003
Vaults are ribonucleoprotein particles found in the cytoplasm of eucaryotic cells. The 13 MDa particles are composed of multiple… 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
Highly Cited
2001
Highly Cited
2001
Human vaults are intracellular ribonucleoprotein particles believed to be involved in multidrug resistance. The complex consists… Expand
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
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