Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Mark F, Vickers"'
Autor:
Frank Visser, Mark F. Vickers, Thack Lang, Morris J. Robins, Jing Zhang, Carol E. Cass, Ireneusz Nowak, James D. Young, Lars P. C. Nielsen, Stephen A. Baldwin
Publikováno v:
Molecular Pharmacology. 64:1512-1520
An extensive series of structural analogs of uridine that differed in substituents in the sugar and/or base moieties were subjected to inhibitor-sensitivity assays in a yeast expression system to define uridine structural determinants for inhibitors
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09814fca6c2e1513132b4acfddcc4e4d
https://doi.org/10.1124/mol.64.6.1512
https://doi.org/10.1124/mol.64.6.1512
Autor:
Sylvia Y.M. Yao, Mark F. Vickers, Manickavasagam Sundaram, Amy M. L. Ng, James D. Young, Carol E. Cass, Stephen A. Baldwin
Publikováno v:
Journal of Biological Chemistry. 277:24938-24948
The human (h) and rat (r) equilibrative (Na(+)-independent) nucleoside transporters (ENTs) hENT1, rENT1, hENT2, and rENT2 belong to a family of integral membrane proteins with 11 transmembrane domains (TMs) and are distinguished functionally by diffe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b6547ae8e0c3088d30cc06fec5efd372
https://doi.org/10.1074/jbc.m200966200
https://doi.org/10.1074/jbc.m200966200
Autor:
Lori L. Jennings, James D. Young, Stephen A. Baldwin, Carol E. Cass, Chunhai Hao, Miguel A Cabrita, Mark F. Vickers
Publikováno v:
Neuropharmacology. 40:722-731
Nucleoside transport processes play an important role in human cells in salvage of nucleosides used in the biosynthesis of nucleic acids and in regulating endogenous adenosine concentrations in the human central nervous system (CNS). By altering the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9d35556f02ce8eeaf44d0d52aa20892
https://doi.org/10.1016/s0028-3908(00)00207-0
https://doi.org/10.1016/s0028-3908(00)00207-0
Publikováno v:
Molecular Membrane Biology. 18:73-79
The transport of nucleosides and nucleobases in the yeast Saccharomyces cerevisiae is reviewed and the use of this organism to study recombinant mammalian concentrative nucleoside transport (CNT) proteins is described. A selection strategy based on t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d62a15bbb629ae262c293d9021e88a8
https://doi.org/10.1080/09687680010033306
https://doi.org/10.1080/09687680010033306
Publikováno v:
Journal of Biological Chemistry. 275:25931-25938
FUI1 and function unknown now 26 (FUN26) are proteins of uncertain function with sequence similarities to members of the uracil/allantoin permease and equilibrative nucleoside transporter families of transporter proteins, respectively. [3H]Uridine in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0524d382e6cc84e8cb7f39a5f66ac10f
https://doi.org/10.1074/jbc.m000239200
https://doi.org/10.1074/jbc.m000239200
Publikováno v:
Emerging Therapeutic Targets. 4:515-539
Nucleosides are central salvage metabolites and, as precursors of nucleotides, play an essential role in intermediary metabolism and biosynthesis, as well as signal transduction through interaction with purinergic receptors. Nucleoside analogues are
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9229e93a5a14600a52ccf27718e476d9
https://doi.org/10.1517/14728222.4.4.515
https://doi.org/10.1517/14728222.4.4.515
Autor:
James D. Young, Rajam S. Mani, Manickavasagam Sundaram, Carol E. Cass, Stephen A. Baldwin, Mark F. Vickers, Douglas L. Hogue
Publikováno v:
Biochemical Journal. 339:21-32
We have produced recombinant human equilibrative nucleoside transporter (hENT1) in the yeast Saccharomyces cerevisiae and have compared the binding of inhibitors of equilibrative nucleoside transport with the wild-type transporter and a N-glycosylati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fae01a0bd7f0e5d822bd59df294c49ae
https://doi.org/10.1042/bj3390021
https://doi.org/10.1042/bj3390021
Autor:
Sylvia Y.M. Yao, Thach Lang, Mark F. Vickers, Tracey Tackaberry, Karen M. King, James D. Young, Vijaya L. Damaraju, Delores Mowles, Amy M. L. Ng, Carol E. Cass
Publikováno v:
Molecular pharmacology. 69(1)
2-Chloro-9-(2'-deoxy-2'-fluoro-beta-d-arabinofuranosyl)adenine (Cl-F-ara-A, clofarabine), a purine nucleoside analog with structural similarity to 2-chloro-2'-deoxyadenosine (Cl-dAdo, cladribine) and 9-beta-d-arabinofuranosyl-2-fluoroadenine (F-ara-A
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9c2f28c76c636fb81bfa83c03d878c0
https://pubmed.ncbi.nlm.nih.gov/16234483
https://pubmed.ncbi.nlm.nih.gov/16234483
Autor:
Mark F. Vickers, James D. Young, Stephen A. Baldwin, Lars P. C. Nielsen, Frank Visser, Jing Zhang, Ireneusz Nowak, Carol E. Cass, Morris J. Robins, Tracey Tackaberry
Publikováno v:
Nucleosides, nucleotidesnucleic acids. 23(1-2)
The sugar moiety of nucleosides has been shown to play a major role in permeant-transporter interaction with human equilibrative nucleoside transporters 1 and 2 (hENT1 and hENT2). To better understand the structural requirements for interactions with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f91aa65550ecad0859a833088fcbc2b
https://pubmed.ncbi.nlm.nih.gov/15043160
https://pubmed.ncbi.nlm.nih.gov/15043160
Autor:
Jing Zhang, Mark F. Vickers, Rakesh Kumar, R. Taylor Raborn, Jahangir Charania, Carol E. Cass, Frank Visser, James D. Young, Stephen A. Baldwin
Publikováno v:
Biochemistry and cell biology = Biochimie et biologie cellulaire. 80(5)
The human equilibrative nucleoside transporters 1 and 2 (hENT1, hENT2) share 50% amino acid identity and exhibit broad selectivities, accepting purine and pyrimidine nucleosides as permeants. The permeant selectivity of hENT2 is less well understood
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8b9f0011bd002c5450745a10d0224de
https://pubmed.ncbi.nlm.nih.gov/12440703
https://pubmed.ncbi.nlm.nih.gov/12440703