Ribonucleotide reductase M1 subunit in cellular proliferation, quiescence, and differentiation.

Ribonucleotide Reductase Ml Subunit in Cellular Proliferation, Quiescence, and Differentiation

Ribonucleotide reducÃ-asecatalyzes the first unique, rate-limiting step in DNA synthesis; both its large (Ml) and small (M2) subunits are necessary for activity. While direct studies of M2 expression have previously shown a tight correlation with S phase, the kinetic features of Mi-expressing cells have remained ill defined. Therefore we have, using immunofluorescence flow cytometry, analyzed c...

An analysis of human equilibrative nucleoside transporter-1, ribonucleotide reductase subunit M1, ribonucleotide reductase subunit M2, and excision repair cross-complementing gene-1 expression in patients with resected pancreas adenocarcinoma: Implications for adjuvant treatment

18F-fluorodeoxyglucose Uptake with Expression of Excision Repair Cross-complementary Group 1 and Ribonucleotide Reductase Subunit M1 in Non-small Cell Lung Cancer

Fluorodeoxyglucose positron emission tomography/computed tomography (FDG PET/CT) is widely applied in non‐small cell lung cancer (NSCLC). The standardized uptake value (SUV), a semi‐quantitative index, plays an essential role in NSCLC for diagnosis, staging, and efficacy evaluation. It has been proposed that the SUVmax of tumors may correlate with the presence or absence of chemotherapy resista...

Herpes simplex virus ribonucleotide reductase induced in infected BHK-21/C13 cells: biochemical evidence for the existence of two non-identical subunits, H1 and H2.

In nearly all systems studied, ribonucleotide reductase consists of two non-identical subunits. We present here the results of our study on herpes simplex virus (HSV) ribonucleotide reductase in favour of the existence of two subunits, H1 and H2, different from the mammalian subunits, M1 and M2. First, although the viral subunits could not be separated by Blue Sepharose chromatography (unlike m...

Direct photoaffinity labeling of an allosteric site on subunit protein M1 of mouse ribonucleotide reductase by dTTP.

The protein M1 subunit of ribonucleotide reductase contains at least two allosteric nucleotide binding sites that control the capacity of the enzyme to reduce ribonucleotides to the deoxyribonucleotides required for DNA synthesis. Direct photoaffinity labeling of partially purified protein M1 from mouse T-lymphoma (S49) cells was observed after UV irradiation in the presence of dTTP at 0 degree...