Results 21 to 30 of about 34,973 (226)

Substrate Specificity of B12-Depedent Ribonucleotide Reductases: Biotechnology and Metabolic Implications. [PDF]

open access: yesChembiochem
Ribonucleotide reductases (RNRs) are valuable biocatalysts for the biosynthesis of non‐natural deoxyribonucleotide, relevant in fields like medical science and synthetic biology. In this study, we explore the substrate spectrum of two thermostable RNRs and discuss their implications for nucleotide metabolism and biocatalytical applications ...
Eltoukhy L, Loderer C.
europepmc   +2 more sources

Immunohistochemical demonstration of poly(adenosine diphosphate-ribose) synthetase in bovine tissues.

open access: yesJournal of Histochemistry and Cytochemistry, 1983
The inter- and intracellular localization of poly(adenosine diphosphate-ribose)(poly(ADP-ribose] synthetase was investigated using an indirect immunofluorescence technique and a specific antibody against the enzyme purified from calf thymus.
K. Ikai, K. Ueda
semanticscholar   +2 more sources

Kinetic and Static Analysis of Poly-(Adenosine Diphosphate-Ribose) Polymerase-1-Targeted 18F-Fluorthanatrace PET Images of Ovarian Cancer. [PDF]

open access: yesJ Nucl Med, 2022
Visual Abstract The poly-(adenosine diphosphate-ribose) polymerase (PARP) family of proteins participates in numerous functions, most notably the DNA damage response.
Young AJ   +14 more
europepmc   +2 more sources

Natural occurence of a biopolymer, poly (adenosine diphosphate ribose)

open access: yesNucleic Acids Research, 1977
Evidence for the natural occurrence of poly(adenosine diphosphate ribose) in vivo was obtained using a sensitive radioimmunoassay and poly(adenosine diphosphate ribose) glycohydrolase, which specifically hydrolyzes poly(adenosine diphosphate ribose).
Masanao Miwa, Shimada T, Sugimura T
exaly   +4 more sources

Bovine thymus poly(adenosine diphosphate ribose) polymerase.

open access: yesJournal of Biological Chemistry, 1978
About 1,300-fold purification of poly(adenosine diphosphate ribose) polymerase has been achieved from the extract of bovine thymus with a recovery of 10 to 20%. The final preparation has a purity of 99%, and the enzyme is composed of a single peptide with a molecular weight of 130,000. The purified enzyme required NAD+, Mg2+, a thiol compound, DNA, and
K, Yoshihara   +5 more
openaire   +3 more sources

Studies on the Polymer of Adenosine Diphosphate Ribose

open access: yesJournal of Biological Chemistry, 1967
A particulate fraction obtained from rat liver nuclei is capable of polymerizing the adenosine diphosphate ribose moiety of nicotinamide adenine dinucleotide with the simultaneous release of nicotinamide.
Yasutomi Nishizuka   +3 more
semanticscholar   +3 more sources

Poly(adenosine diphosphate-ribose) polymerase as therapeutic target: lessons learned from its inhibitors. [PDF]

open access: yesOncotarget, 2017
Poly(ADP-ribose) polymerases are a family of DNA-dependent nuclear enzymes catalyzing the transfer of ADP-ribose moieties from cellular nicotinamide-adenine-dinucleotide to a variety of target proteins.
Cseh AM   +3 more
europepmc   +2 more sources

O6-[(2″,3″-O-Isopropylidene-5″-O-tbutyldimethylsilyl)pentyl]-5′-O-tbutyldiphenylsilyl-2′,3′-O-isopropylideneinosine

open access: yesMolbank, 2022
Cyclic adenosine diphosphate ribose (cADPR) is a cyclic nucleotide involved in the Ca2+ homeostasis. In its structure, the northern ribose, bonded to adenosine through an N1 glycosidic bond, is connected to the southern ribose through a pyrophosphate ...
Maria Marzano   +5 more
doaj   +1 more source

TNB-738, a biparatopic antibody, boosts intracellular NAD+ by inhibiting CD38 ecto-enzyme activity

open access: yesmAbs, 2022
Cluster of differentiation 38 (CD38) is an ecto-enzyme expressed primarily on immune cells that metabolizes nicotinamide adenine dinucleotide (NAD+) to adenosine diphosphate ribose or cyclic ADP-ribose and nicotinamide.
Harshad S. Ugamraj   +19 more
doaj   +1 more source

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