Band 3 HT, a human red-cell variant associated with acanthocytosis and increased anion transport, carries the mutation Pro-868-->Leu in the membrane domain of band 3.
about
A substrate access tunnel in the cytosolic domain is not an essential feature of the solute carrier 4 (SLC4) family of bicarbonate transportersDifferential sensitivity of stilbenedisulfonates in their reaction with band 3 HT (Pro-868-->Leu).Novel topology in C-terminal region of the human plasma membrane anion exchanger, AE1.Brain, blood, and iron: perspectives on the roles of erythrocytes and iron in neurodegeneration.Developments in neuroacanthocytosis: expanding the spectrum of choreatic syndromes.Requirements for ion and solute transport, and pH regulation during enamel maturation.Electrogenic sulfate/chloride exchange in Xenopus oocytes mediated by murine AE1 E699Q.Characterization of oxalate transport by the human erythrocyte band 3 protein.Topology models of anion exchanger 1 that incorporate the anti-parallel V-shaped motifs found in the EM structure.The role of band 3 protein in oxygen delivery by red blood cells.Complementation studies with co-expressed fragments of human red cell band 3 (AE1): the assembly of the anion-transport domain in xenopus oocytes and a cell-free translation system.The substrate anion selectivity filter in the human erythrocyte Cl-/HCO3- exchange protein, AE1.Substitution Glu480Lys in erythroid band 3 corresponds to the Fr(a) blood group antigen and supports existence of the second ectoplasmic loop of band 3.Asymmetry of inverted-topology repeats in the AE1 anion exchanger suggests an elevator-like mechanism.Effect of band 3 subunit equilibrium on the kinetics and affinity of ankyrin binding to erythrocyte membrane vesicles.Mouse Models of SLC4-linked Disorders of HCO3- Transporter Dysfunction.
P2860
Q24338331-DAA65BE5-47E3-4199-9207-E33C9AFB3255Q33728252-865132D8-0DD5-48ED-BC9F-8068CEA95223Q34160435-0ABB3CE9-197D-478C-976A-C337DB00EC56Q34198997-5ABB8313-FED4-4A95-AB01-74BA4069E242Q34564227-114B8780-6973-45C6-AFFB-9DED60051A6FQ36026725-317B4980-608F-4E5F-B5D5-B52EA55E9B1AQ36411915-0B6FBA27-659F-4BD4-93FF-395A2D114CD3Q36415700-46C9E654-AF1D-4780-95FA-FE8A9D4D9129Q37860155-A3448EA3-FBA4-41E8-990B-5B6635538685Q42746820-BD3C0EA6-BAC8-4E6E-A2AC-8DC7F867A0F7Q42990645-CBD16ABA-E7CC-4FB4-A324-14E26F0763C9Q44814652-B5661C6A-1A63-4F4E-8F71-3C0F9BD783EFQ44856261-D336E43C-17B2-4B7E-86B2-5F7915ABCC4CQ47120898-ED30E64C-33BA-4147-B899-8BB2E1441422Q48010798-30517F52-16EE-4D76-9587-15B31AA8120BQ49559317-FCBA0035-B581-47CB-8354-68258A16F47C
P2860
Band 3 HT, a human red-cell variant associated with acanthocytosis and increased anion transport, carries the mutation Pro-868-->Leu in the membrane domain of band 3.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
1993年學術文章
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1993年學術文章
@zh-hant
name
Band 3 HT, a human red-cell va ...... the membrane domain of band 3.
@en
Band 3 HT, a human red-cell va ...... the membrane domain of band 3.
@nl
type
label
Band 3 HT, a human red-cell va ...... the membrane domain of band 3.
@en
Band 3 HT, a human red-cell va ...... the membrane domain of band 3.
@nl
prefLabel
Band 3 HT, a human red-cell va ...... the membrane domain of band 3.
@en
Band 3 HT, a human red-cell va ...... the membrane domain of band 3.
@nl
P2093
P2860
P356
P1433
P1476
Band 3 HT, a human red-cell va ...... the membrane domain of band 3.
@en
P2093
P2860
P304
P356
10.1042/BJ2930317
P407
P478
293 ( Pt 2)
P577
1993-07-01T00:00:00Z