Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Sanath R. Wijerathna"'
Autor:
Prem Singh Kaushal, Qun Wan, Chris G. Dealwis, Jianying Kiser, Hai Xu, James W. Fairman, Andrew Zhang, Sanath R. Wijerathna, Md. Faiz Ahmad
Publikováno v:
Pharmaceuticals, Vol 4, Iss 10, Pp 1328-1354 (2011)
Ribonucleotide reductase (RR) is a crucial enzyme in de novo DNA synthesis, where it catalyses the rate determining step of dNTP synthesis. RRs consist of a large subunit called RR1 (α), that contains two allosteric sites and one catalytic site, and
Externí odkaz:
https://doaj.org/article/cc9736ee1fed4dd88e3d13b9070a7567
Autor:
Tessianna A. Misko, Anthony J. Berdis, Tomas Radivoyevitch, Michael E. Harris, Chris Dealwis, Sanath R. Wijerathna, Md. Faiz Ahmad
Publikováno v:
FEBS letters. 590(12)
Sml1 is an intrinsically disordered protein inhibitor of Saccharomyces cerevisiae ribonucleotide reductase (ScRR1), but its inhibition mechanism is poorly understood. RR reduces ribonucleoside diphosphates to their deoxy forms, and balances the nucle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05ad7d91542db5eb9996f3180e137237
https://pubmed.ncbi.nlm.nih.gov/27155231
https://pubmed.ncbi.nlm.nih.gov/27155231
Autor:
Shalini Jha, Thomas Walz, A.K. Roos, R Martin Welin, Faiz Ahmad, P. Nordlund, Hai Xu, Sanath R. Wijerathna, Zongli Li, Ryo Nakano, Chris Dealwis, Jay S. Prendergast, James W. Fairman, Susanne Flodin
Publikováno v:
Nature Structural & Molecular Biology. 18:316-322
Ribonucleotide reductase (RR) is an αnβn (RR1●RR2) complex that maintains balanced dNTP pools by reducing ribonucleoside diphosphates to deoxyribonucleoside diphosphates. RR1 is the catalytic subunit and RR2 houses the free radical required for c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0341ab9e8f8dd1a61091497344b0296a
https://doi.org/10.1038/nsmb.2007
https://doi.org/10.1038/nsmb.2007
Publikováno v:
ChemMedChem. 4:1649-1656
Analysis of the recently solved X-ray crystal structures of yeast ribonucleotide reductase I (RnrI) in complex with effectors and substrates led to the discovery of a conserved water molecule located at the active site that interacted with the 2′ h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::11696e9fefd423680d08f308533e11c1
https://doi.org/10.1002/cmdc.200900236
https://doi.org/10.1002/cmdc.200900236
Autor:
Qun Wan, Xiuxiang An, Md. Faiz Ahmad, Prem Singh Kaushal, Chris Dealwis, Sanath R. Wijerathna, Mingxia Huang
Publikováno v:
Journal of molecular biology. 419(5)
Ribonucleotide reductases (RRs) catalyze the rate-limiting step of de novo deoxynucleotide (dNTP) synthesis. Eukaryotic RRs consist of two proteins, RR1 (α) that contains the catalytic site and RR2 (β) that houses a diferric-tyrosyl radical essenti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::75b5d4996cfe335e1958592b77cd3420
https://pubmed.ncbi.nlm.nih.gov/22465672
https://pubmed.ncbi.nlm.nih.gov/22465672
Autor:
Hai Xu, Barry S. Cooperman, Nathan R. Kreischer, James W. Fairman, Sanath R. Wijerathna, Chris Dealwis, Elizabeth Helmbrecht, John C. LaMacchia
Publikováno v:
Journal of medicinal chemistry. 51(15)
Eukaryotic ribonucleotide reductase (RR) catalyzes nucleoside diphosphate conversion to deoxynucleoside diphosphate. Crucial for rapidly dividing cells, RR is a target for cancer therapy. RR activity requires formation of a complex between subunits R
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a418e601f535d56156f29797abfbbee1
https://pubmed.ncbi.nlm.nih.gov/18610997
https://pubmed.ncbi.nlm.nih.gov/18610997