Cysteine-accessibility analysis of transmembrane domains 11-13 of human concentrative nucleoside transporter 3.
about
Crystal structure of a concentrative nucleoside transporter from Vibrio cholerae at 2.4 ÅGenetic selection for a highly functional cysteine-less membrane protein using site saturation mutagenesisIncreased water flux induced by an aquaporin-1/carbonic anhydrase II interactionA conformationally mobile cysteine residue (Cys-561) modulates Na+ and H+ activation of human CNT3Carbonic anhydrase II binds to and increases the activity of the epithelial sodium-proton exchanger, NHE3Conserved glutamate residues Glu-343 and Glu-519 provide mechanistic insights into cation/nucleoside cotransport by human concentrative nucleoside transporter hCNT3Substituted cysteine accessibility method analysis of human concentrative nucleoside transporter hCNT3 reveals a novel discontinuous region of functional importance within the CNT family motif (G/A)XKX3NEFVA(Y/M/F).Red fluorescent protein pH biosensor to detect concentrative nucleoside transportDrug transporter pharmacogenetics in nucleoside-based therapies.Transporters that translocate nucleosides and structural similar drugs: structural requirements for substrate recognition.A proton-mediated conformational shift identifies a mobile pore-lining cysteine residue (Cys-561) in human concentrative nucleoside transporter 3.Substituted cysteine accessibility method (SCAM) analysis of the transport domain of human concentrative nucleoside transporter 3 (hCNT3) and other family members reveals features of structural and functional importanceFunctional analysis of the human concentrative nucleoside transporter-1 variant hCNT1S546P provides insight into the sodium-binding pocket.Conserved glutamate residues are critically involved in Na+/nucleoside cotransport by human concentrative nucleoside transporter 1 (hCNT1).
P2860
Q27677998-09291FDF-F815-4AD0-900A-2A1E15BB53C7Q33283772-BB64097E-26F4-4B0D-8D6E-5EB0145EB173Q35171010-F535334E-3CB4-4328-8545-F069B96301CFQ35676740-5E851AF1-214E-4275-9F05-06EB84884AD6Q37123857-68EE65FB-E6A2-4D05-B0A3-B74CF24A3A83Q37285168-6DCB1F5B-FA13-4A43-A61D-E5BDF1E8A2DCQ37285173-B8B3EFE6-FDDA-465F-8737-404F9AC1A421Q37343945-4F909C94-0E8B-4B83-9FB5-9F8D67FCDD1EQ37760954-A9B3A769-AA51-4ADE-96F9-195D19AB522FQ37834510-578DCBB6-4D69-4831-BAF0-DDE60531A0DAQ38923874-A7045018-850C-4D1B-8926-074E4862F8D9Q41999847-77CC698E-A838-466E-889B-E5C8811EE3DEQ46429658-74563430-018E-427F-8DF1-146A28924DD4Q48785548-D71BFE6D-FAE3-430E-BE77-4D6747E3D615
P2860
Cysteine-accessibility analysis of transmembrane domains 11-13 of human concentrative nucleoside transporter 3.
description
2006 nî lūn-bûn
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2006年の論文
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2006年学术文章
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@zh-hans
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name
Cysteine-accessibility analysi ...... tive nucleoside transporter 3.
@en
Cysteine-accessibility analysi ...... tive nucleoside transporter 3.
@nl
type
label
Cysteine-accessibility analysi ...... tive nucleoside transporter 3.
@en
Cysteine-accessibility analysi ...... tive nucleoside transporter 3.
@nl
prefLabel
Cysteine-accessibility analysi ...... tive nucleoside transporter 3.
@en
Cysteine-accessibility analysi ...... tive nucleoside transporter 3.
@nl
P2093
P2860
P356
P1433
P1476
Cysteine-accessibility analysi ...... tive nucleoside transporter 3.
@en
P2093
Carol E Cass
Gerry Barron
James D Young
Jing Zhang
Mabel W L Ritzel
Taylor Raborn
Tracey Tackaberry
P2860
P304
P356
10.1042/BJ20051476
P407
P577
2006-03-01T00:00:00Z