Zobrazeno 1 - 10
of 40
pro vyhledávání: '"Amy M L, Ng"'
Publikováno v:
Biochemical Journal. 475:3293-3309
Human equilibrative nucleoside transporter 1 (hENT1), the first identified member of the ENT family of integral membrane proteins, is the primary mechanism for cellular uptake of physiologic nucleosides and many antineoplastic and antiviral nucleosid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::169d77ca49d5a9ba91989e58210e2aff
https://doi.org/10.1042/bcj20180543
https://doi.org/10.1042/bcj20180543
Publikováno v:
The Journal of Biological Chemistry
The human SLC28 family of concentrative nucleoside transporter (CNT) proteins has three members: hCNT1, hCNT2, and hCNT3. Na+-coupled hCNT1 and hCNT2 transport pyrimidine and purine nucleosides, respectively, whereas hCNT3 transports both pyrimidine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::06b91e795003189b26af306842f505b4
http://europepmc.org/articles/PMC5465479
http://europepmc.org/articles/PMC5465479
Publikováno v:
The Biochemical journal. 475(20)
Human equilibrative nucleoside transporter 1 (hENT1), the first identified member of the ENT family of integral membrane proteins, is the primary mechanism for cellular uptake of physiologic nucleosides and many antineoplastic and antiviral nucleosid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4fd9f7616fa3d610f50794436c819c14
https://pubmed.ncbi.nlm.nih.gov/30254099
https://pubmed.ncbi.nlm.nih.gov/30254099
Autor:
Carol E. Cass, Amy M. L. Ng, Sylvia Y.M. Yao, Vijaya L. Damaraju, Zeen Tong, James D. Young, Delores Mowles
Publikováno v:
Nucleosides, Nucleotides and Nucleic Acids. 31:236-255
The nucleoside analogs 5-azacytidine (azacitidine) and 5-aza-2'-deoxycytidine (decitabine) are active against acute myeloid leukemia and myelodysplastic syndromes. Cellular transport across membranes is crucial for uptake of these highly polar hydrop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f0d69c7cad42e89d0a2bff8f9953151
https://doi.org/10.1080/15257770.2011.652330
https://doi.org/10.1080/15257770.2011.652330
Autor:
Edward Karpinski, Sylvia Y.M. Yao, Kyla M. Smith, James D. Young, Melissa D. Slugoski, Carol E. Cass, Stephen A. Baldwin, Amy M. L. Ng
Publikováno v:
Journal of Biological Chemistry. 284:17266-17280
Human concentrative nucleoside transporter 3 (hCNT3) utilizes electrochemical gradients of both Na(+) and H(+) to accumulate pyrimidine and purine nucleosides within cells. We have employed radioisotope flux and electrophysiological techniques in com
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d2dd1cca357cc154605c3ad034d1c3d
https://doi.org/10.1074/jbc.m109.009613
https://doi.org/10.1074/jbc.m109.009613
Autor:
Amy M. L. Ng, Queenie O.T. Lee, Edward Karpinski, Stephen A. Baldwin, Ras Mulinta, Ellen Morrison, Jing Zhang, Sylvia Y.M. Yao, Kyla M. Smith, Melissa D. Slugoski, James D. Young, Carol E. Cass
Publikováno v:
Journal of Biological Chemistry. 283:24922-24934
In humans, the SLC28 concentrative nucleoside transporter (CNT) protein family is represented by three Na+-coupled members; human CNT1 (hCNT1) and hCNT2 are pyrimidine and purine nucleoside-selective, respectively, whereas hCNT3 transports both purin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e80cdb4ac22ccf96b78b10b4b422c174
https://doi.org/10.1074/jbc.m801793200
https://doi.org/10.1074/jbc.m801793200
Autor:
Stephen A. Baldwin, Amy M. L. Ng, James D. Young, Edward Karpinski, Melissa D. Slugoski, Sylvia Y.M. Yao, Carol E. Cass, Ras Mulinta, Kyla M. Smith
Publikováno v:
Journal of Biological Chemistry. 282:30607-30617
Human concentrative nucleoside transporter 1 (hCNT1), the first discovered of three human members of the SLC28 (CNT) protein family, is a Na+/nucleoside cotransporter with 650 amino acids. The potential functional roles of 10 conserved aspartate and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8da15e34d2ee55d8c7010d27454fc3a
https://doi.org/10.1074/jbc.m703285200
https://doi.org/10.1074/jbc.m703285200
Autor:
Edward Karpinski, James D. Young, Amy M. L. Ng, Sylvia Y.M. Yao, Stephen A. Baldwin, Carol E. Cass, Shaun K. Loewen, Kyla M. Smith, Melissa D. Slugoski
Publikováno v:
Biochemistry. 46:1684-1693
The Na + /nudeoside cotransporters hCNT1 (650 residues) and hCNT2 (658 residues) are 72% identical in amino acid sequence and contain 13 putative transmembrane helices (TMs). Both transport uridine and adenosine but are otherwise selective for pyrimi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a70457f8c615e52adcdf79e4eb5d89c
https://doi.org/10.1021/bi061692s
https://doi.org/10.1021/bi061692s
Autor:
Hiremagalur N. Jayaram, Carol E. Cass, Amy M. L. Ng, Delores Mowles, Frank Visser, James D. Young, Jing Zhang, Vijaya L. Damaraju
Publikováno v:
Molecular Pharmacology. 67:273-279
Benzamide riboside (BR) and tiazofurin (TR) are converted to analogs of NAD that inhibit IMP dehydrogenase (IMPDH), resulting in cellular depletion of GTP and dGTP and inhibition of proliferation. The current work was undertaken to identify the human
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f68fe47b8effbb3122f6a6aca2ebd61
https://doi.org/10.1124/mol.104.004408
https://doi.org/10.1124/mol.104.004408
Autor:
Edward Karpinski, Xing-Zhen Chen, Amy M. L. Ng, Kyla M. Smith, Kathy A. Labedz, Leonard I. Wiebe, Edward E. Knaus, Sylvia Y.M. Yao, Stephen A. Baldwin, Carol E. Cass, James D. Young
Publikováno v:
The Journal of Physiology. 558:807-823
Physiological nucleosides and nucleoside analogues have important biochemical, physiological and pharmacological activities in humans. Adenosine, for example, has cell-surface receptor-mediated functions in processes such as modulation of immune resp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8da5aed05d7b4ff0cc56d9a23f31c043
https://doi.org/10.1113/jphysiol.2004.068189
https://doi.org/10.1113/jphysiol.2004.068189