Zobrazeno 1 - 10
of 11
pro vyhledávání: '"N K, Bernstein"'
Autor:
Mark Glover, Angus I. Lamond, Laura Trinkle-Mulcahy, N. K. Bernstein, Greg B. G. Moorhead, Annegret Ulke-Lemée, Nick Morrice, Steven G. Chaulk
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1774:1339-1350
The targeting of protein kinases and phosphatases is fundamental to their roles as cellular regulators. The type one serine/threonine protein phosphatase (PP1) is enriched in the nucleus, yet few nuclear PP1 targeting subunits have been described and
Autor:
Diana Cui, J. N. Mark Glover, R. Scott Williams, M Lee, N. K. Bernstein, Michael Weinfeld, Melissa L. Rakovszky, R. Green
Publikováno v:
Biochemistry and Cell Biology. 83:721-727
The response of eukaryotic cells to DNA damage requires a multitude of protein–protein interactions that mediate the ordered repair of the damage and the arrest of the cell cycle until repair is complete. Two conserved protein modules, BRCT and for
Autor:
N. K. Bernstein, Mark Glover, Michael Weinfeld, Mesfin Fanta, Feridoun Karimi-Busheri, Hong Zhang
Publikováno v:
Hybridoma. 20:237-242
Polydeoxyribonucleotide kinase (PNK) is a mammalian DNA repair enzyme that has the capacity to phosphorylate 5' DNA termini and dephosphorylate 3' DNA termini. A series of murine monoclonal antibodies (MAbs) was raised against the full-length recombi
Autor:
Michael N.G. James, N. K. Bernstein
Publikováno v:
Current Opinion in Structural Biology. 9:690-695
The recently determined crystal structures of two aspartic proteinase zymogens, prophytepsin from barley and proplasmepsin II from the malarial parasite Plasmodium falciparum, have provided new insights into zymogen inactivation. Prophytepsin shows a
Publikováno v:
Nature Structural Biology. 6:32-37
Proplasmepsin II is the zymogen of plasmepsin II, an aspartic proteinase used by Plasmodiumfalciparum to digest hemoglobin during the blood stage of malaria. A large shift between the N-domain and the central and C-domains of proplasmepsin II opens t
Autor:
Porntip Chavalitshewinkoon-Petmitr, J. N. Mark Glover, Feridoun Karimi-Busheri, Michael Weinfeld, Danny Aceytuno, Saranya Siribal, N. K. Bernstein
Publikováno v:
Molecular and biochemical parasitology. 180(1)
Polynucleotide kinase/phosphatase (PNKP) is a bifunctional enzyme that can phosphorylate the 5'-OH termini and dephosphorylate the 3'-phosphate termini of DNA. It is a DNA repair enzyme involved in the processing of strand break termini, which permit
Autor:
Martin Pelikan, J.N.M. Glover, R. S. Mani, Michal Hammel, M. Weinfeld, N. K. Bernstein, John A. Tainer
Publikováno v:
Nucleic Acids Research
Mammalian polynucleotide kinase (mPNK) is a critical DNA repair enzyme whose 5′-kinase and 3′-phoshatase activities function with poorly understood but striking specificity to restore 5′-phosphate/3′-hydroxyl termini at sites of DNA damage. H
Autor:
Feridoun Karimi-Busheri, Aghdass Rasouli-Nia, J.N.M. Glover, Rajam S. Mani, Grigory L. Dianov, N. K. Bernstein, Michael Weinfeld
Publikováno v:
Anti-cancer agents in medicinal chemistry. 8(4)
The cytotoxicity of many antineoplastic agents is due to their capacity to damage DNA and there is evidence indicating that DNA repair contributes to the cellular resistance to such agents. DNA strand breaks constitute a significant proportion of the
Autor:
Michael Weinfeld, Daniel Durocher, N. K. Bernstein, Sarah Galicia, Carol E. Cass, Feridoun Karimi-Busheri, C. Anne Koch, Rajam S. Mani, R. Green, R. Scott Williams, Diana Cui, Melissa L. Rakovszky, J. N. Mark Glover
Publikováno v:
Molecular cell. 17(5)
Mammalian polynucleotide kinase (PNK) is a key component of both the base excision repair (BER) and nonhomologous end-joining (NHEJ) DNA repair pathways. PNK acts as a 5'-kinase/3'-phosphatase to create 5'-phosphate/3'-hydroxyl termini, which are a n
Publikováno v:
Journal of molecular biology. 329(3)
The malarial aspartic proteinases (plasmepsins) have been discovered in several species of Plasmodium, including all four of the human malarial pathogens. In P.falciparum, plasmepsins I, II, IV and HAP have been directly implicated in hemoglobin degr