Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Manickavasagam Sundaram"'
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
Autor:
Stephen A. Baldwin, Manickavasagam Sundaram, Jean C. Ingram, Carol E. Cass, Zoe A. Berry, Fatima Abidi, James D. Young, Sylvia Y.M. Yao
Publikováno v:
Journal of Biological Chemistry. 276:45270-45275
The human equilibrative nucleoside transporter hENT1, the first identified member of the ENT family of integral membrane proteins, is the primary mechanism for the cellular uptake of physiologic nucleosides, including adenosine, and many anti-cancer
Autor:
Stephen A. Baldwin, Carol E. Cass, Sylvia Y.M. Yao, Manickavasagam Sundaram, Amy M. L. Ng, James D. Young
Publikováno v:
Biochemistry. 40:8146-8151
The rat equilibrative nucleoside transporters rENT1 and rENT2 belong to a family of integral membrane proteins with 11 potential transmembrane segments (TMs) and are distinguished functionally by differences in sensitivity to inhibition by nitrobenzy
Autor:
Sylvia Y. M. YAO, Manickavasagam SUNDARAM, Eugene G. CHOMEY, Carol E. CASS, Stephen A. BALDWIN, James D. YOUNG
Publikováno v:
Biochemical Journal. 353:387-393
The human and rat equilibrative nucleoside transporter proteins hENT1, rENT1, hENT2 and rENT2 belong to a family of integral membrane proteins with 11 potential transmembrane segments (TMs), and are distinguished functionally by differences in transp
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
Autor:
Nick Beaumont, Christine E. Boumah, Manickavasagam Sundaram, Carol E. Cass, Sylvia Y.M. Yao, Imogen Coe, Francis Y. P. Kwong, Anthony Davies, Mark Griffiths, Stephen A. Baldwin, James D. Young
Publikováno v:
Nature Medicine. 3:89-93
In most mammalian cells nucleoside uptake occurs primarily via broad-specificity, es (e, equilibrative; 5, sensitive to NBMPR inhibition) transporters that are potently inhibited by nitrobenzylthioinosine (NBMPR). These transporters are essential for
Autor:
Sylvia Y M, Yao, Amy M L, Ng, Mark F, Vickers, Manickavasagam, Sundaram, Carol E, Cass, Stephen A, Baldwin, James D, Young
Publikováno v:
The Journal of biological chemistry. 277(28)
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
Autor:
Manickavasagam Sundaram, Carol E. Cass, James D. Young, Sylvia Y.M. Yao, Amy M. L. Ng, Stephen A. Baldwin
Publikováno v:
Molecular membrane biology. 18(2)
In the present study, one has determined the relative role of plasma membrane equilibrative (Na+-independent) ENT nucleoside transport proteins (particularly ENT2) in the uptake of antiviral nucleoside analogues for comparison with the previously rep
Autor:
James D. Young, Mark Griffiths, Amy M. L. Ng, Sylvia Y.M. Yao, Stephen A. Baldwin, Carol E. Cass, Manickavasagam Sundaram
Publikováno v:
The Journal of biological chemistry. 273(34)
We have recently isolated cDNAs from human placenta and rat jejunum encoding the prototypic human and rat equilibrative nitrobenzylthioinosine (NBMPR)-sensitive nucleoside transporters hENT1 and rENT1. The two proteins (456 and 457 residues, Mr 50,00
Publikováno v:
The Journal of biological chemistry. 273(6)
The hypothesis that the cellular uptake of retinol involves the specific interaction of a plasma membrane receptor with serum retinol-binding protein (RBP) at the extracellular surface followed by ligand transfer to cytoplasmic cellular retinol-bindi