Results 241 to 250 of about 281,775 (299)

Molecular Dynamics Simulations Provide Further Insights into the Allosteric Regulation of the Kinesin-5 Motor Domain by Loop 5. [PDF]

open access: yesJ Chem Inf Model
Rodríguez-Santos G   +5 more
europepmc   +1 more source

ADP-ribosylarginine hydrolases and ADP-ribosyltransferases. Partners in ADP-ribosylation cycles.

Advances in experimental medicine and biology, 1997
Mono-ADP-ribosylation is a reversible modification of arginine residues in proteins, with NAD:arginine ADP-ribosyltransferases and ADP-ribosylarginine hydrolases constituting opposing arms of a putative ADP-ribosylation cycle. The enzymatic components of an ADP-ribosylation cycle have been identified in both prokaryotic and eukaryotic systems.
J, Moss, A, Zolkiewska, I, Okazaki
openaire   +2 more sources

Poly(ADP-ribose) and ADP-ribosylation of proteins

Trends in Biochemical Sciences, 1976
Abstract Covalent modification of proteins, by attachment of ADP-ribose, appears to regulate cell growth, protein metabolism, DNA and RNA metabolism.
H, Hilz, P, Stone
openaire   +3 more sources

Mammalian ADP-ribosyltransferases and ADP-ribosylhydrolases

Frontiers in Bioscience, 2008
ADP-ribosyltransferases (ARTs) and ADP-ribosylhydrolases (ARHs) catalyze opposing reactions, which are termed ADP-ribosylation and de-ADP-ribosylation. ARTs transfer the ADP-ribose unit from NAD (nicotinamide adenine dinucleotide) onto an acceptor, while ARHs release the ADP-ribose from the target.
Friedrich, Koch-Nolte   +4 more
openaire   +2 more sources

Poly (ADP-Ribose) and ADP-Ribosylation of Proteins

Annual Review of Biochemistry, 1977
Publisher Summary This chapter analyzes poly(ADP-ribose) and ADP-ribosylation of proteins. Poly(ADP-ribose) and the ADP-ribosylation of proteins constitute a novel type of covalent modification of proteins. They are ubiquitously distributed in nature and are implicated in the regulation of cell proliferation, protein synthesis, and DNA as well as RNA
O, Hayaishi, K, Ueda
openaire   +2 more sources

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