Zobrazeno 1 - 10
of 215
pro vyhledávání: '"Peter, Reichard"'
Autor:
Vera Bianchi, Peter Reichard, Paola Ferraro, Chiara Rampazzo, Giovanna Pontarin, Cristina Miazzi
Publikováno v:
The Journal of Biological Chemistry
Background: Genetic loss of SAMHD1, a catabolic enzyme preventing dNTP accumulation outside S phase, leads to disease in humans but not in mice. Results: Allosteric regulation by dNTPs works similarly in pure recombinant human and mouse SAMHD1. Concl
Autor:
Lars Thelander, Peter Reichard, Vera Bianchi, Giovanna Pontarin, Paola Ferraro, Pelle Håkansson
Publikováno v:
Journal of Biological Chemistry. 282:16820-16828
Human fibroblasts in culture obtain deoxynucleotides by de novo ribonucleotide reduction or by salvage of deoxynucleosides. In cycling cells the de novo pathway dominates, but in quiescent cells the salvage pathway becomes important. Two forms of act
Autor:
Pär, Nordlund, Peter, Reichard
Publikováno v:
Annual Review of Biochemistry. 75:681-706
Ribonucleotide reductases (RNRs) transform RNA building blocks to DNA building blocks by catalyzing the substitution of the 2′OH-group of a ribonucleotide with a hydrogen by a mechanism involving protein radicals. Three classes of RNRs employ diffe
Publikováno v:
Journal of Biological Chemistry. 281:5604-5611
Ribonucleotide reductases provide the building blocks for DNA synthesis. Three classes of enzymes are known, differing widely in amino acid sequence but with similar structural motives and allosteric regulation. Class I occurs in eukaryotes and aerob
Autor:
Vera Bianchi, Chiara Rampazzo, Peter Reichard, Katia Crovatto, Giovanna Pontarin, Eva Milanesi, Paola Ferraro, Lisa Gallinaro
Publikováno v:
Journal of Biological Chemistry. 277:35080-35087
Deoxynucleoside triphosphates (dNTPs) used for mitochondrial DNA replication are mainly formed by phosphorylation of deoxynucleosides imported into mitochondria from the cytosol. We earlier obtained evidence for a mitochondrial 5′-nucleotidase (dNT
Autor:
Peter Reichard
Publikováno v:
Journal of Biological Chemistry. 277:13355-13362
Publikováno v:
Journal of Biological Chemistry. 276:33488-33494
Deoxyribonucleotide synthesis by anaerobic class III ribonucleotide reductases requires two proteins, NrdD and NrdG. NrdD contains catalytic and allosteric sites and, in its active form, a stable glycyl radical. This radical is generated by NrdG with
Publikováno v:
Journal of Biological Chemistry. 276:6185-6190
5'-Nucleotidases are the catabolic members of the substrate cycles postulated to be involved in the regulation of intracellular deoxyribonucleoside triphosphate pools. Here, we attempt to identify the nature of the nucleotidases. Earlier, we construc
Autor:
Vera Bianchi, Monica Moras, Peter Reichard, Cinzia Gazziola, Paola Ferraro, Roberta Verin, Lisa Gallinaro, Chiara Rampazzo
Publikováno v:
Experimental Cell Research. 253:474-482
Human 293 cells were stably transfected with a plasmid introducing a receptor for the ecdysone analog muristerone. The cells were further stably transfected with muristerone-inducible expression vectors carrying either the cDNA for the human high K(M
Publikováno v:
Journal of Biological Chemistry. 274:7182-7189
Three separate classes of ribonucleotide reductases are known, each with a distinct protein structure. One common feature of all enzymes is that a single protein generates each of the four deoxyribonucleotides. Class I and III enzymes contain an allo