Results 181 to 190 of about 40,696 (222)

The Intersection of Mitophagy and Autism Spectrum Disorder: A Systematic Review. [PDF]

open access: yesInt J Mol Sci
Kovacheva E   +4 more
europepmc   +1 more source

RNA oxidation: Role of polynucleotide phosphorylase in the quality control of oxidized RNA

JoLS, Journal of Life Sciences, 2021
Reactive oxygen species is one of the most common cellular RNA damaging agents in living organisms. A growing number of studies show a strong correlation between oxidatively damaged RNA and human diseases, predominantly age-related neurodegenerative ...
Sulochan Malla, Alexander Kwakye
semanticscholar   +1 more source

Mechanism of polynucleotide phosphorylase

Biochemistry, 1989
The de novo polymerization of RNA initiated by polynucleotide phosphorylase from nucleoside diphosphates was examined. End group analysis performed under conditions designed to specifically end label the polymer revealed no evidence for a 5'-pyrophosphate-terminated polymer.
Silvio P. Marchese-Ragona   +3 more
openaire   +3 more sources

THE MECHANISM OF ACTION OF POLYNUCLEOTIDE PHOSPHORYLASE

Annals of the New York Academy of Sciences, 1959
The purpose of this paper is to review certain aspects of the mechanism of action of polynucleotide phosphorylase and to present, rather briefly, some recent findings. The discussion will be concerned with studies carried out by S. Ochoa and his associates a t New York University, New York, N.
Maxine F. Singer   +2 more
openaire   +2 more sources

Model for the elongation of polynucleotide chains by polynucleotide phosphorylase

Journal of Molecular Biology, 1970
Abstract The experiments described in this paper were designed to elucidate the mechanism of elongation of a polynucleotide chain catalysed by polynucleotide phosphorylase. The problem has been approached in three different ways, essentially: (1) examination of the size distribution of the end products isolated during the course of the reaction; (2 ...
M. Grunberg-Manago   +2 more
openaire   +3 more sources

Polynucleotide Phosphorylase and the T3SS

2007
Low temperatures as well as encounters with host phagocytes are two stresses that have been relatively well studied in many species of bacteria. The exoribonuclease polynucleotide phosphorylase (PNPase) has previously been shown to be required by several species of bacteria, including Yersinia, for low-temperature growth. We have shown that PNPase also
Kurt Schesser, Jason A. Rosenzweig
openaire   +3 more sources

Photometric Assay for Polynucleotide Phosphorylase

Analytical Biochemistry, 1999
Polynucleotide phosphorylase (PNPase) is a prokaryotic enzyme that catalyzes phosphorolysis of polynucleotides with release of NDPs. It is also believed to play a key role in turnover of prokaryotic transcripts, thus regulating gene expression. At the moment, only radioisotopic methods are available for assaying PNPase in crude extracts; these involve ...
Rebecca Favaro   +5 more
openaire   +3 more sources

The origin of polynucleotide phosphorylase domains

Molecular Phylogenetics and Evolution, 2004
In this report, we document the presence of polynucleotide phosphorylase (PNPase) in the animal eukaryotes. These proteins contain several domains, including 2 RNase PH domains (PNPase 1 and PNPase 2) which are closely related functionally and in sequence similarity to ribonuclease PH (RPH) protein.
Rob DeSalle   +3 more
openaire   +2 more sources

The relationship of mono- and polynucleotide conformation to catalysis by polynucleotide phosphorylase

Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1970
Abstract 8-Bromoguanosine 5′-diphosphate, 8-oxoguanosine 5′-diphosphate, 6-methylcytidine 5′-diphosphate and 2,6-quinazoline dione 1′-ribosyl 5′-diphosphate are inactive as substrates for homopolymer synthesis with polynucleotide phosphorylase. They inhibit polymerization and exchange but not phosphorolysis.
A.M. Michelson, C. Monny, A.M. Kapuler
openaire   +3 more sources

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