The human erythrocyte anion-transport protein. Partial amino acid sequence, conformation and a possible molecular mechanism for anion exchange.
about
Cloning and structural characterization of a human non-erythroid band 3-like protein.Familial distal renal tubular acidosis is associated with mutations in the red cell anion exchanger (Band 3, AE1) geneMutations in the chloride-bicarbonate exchanger gene AE1 cause autosomal dominant but not autosomal recessive distal renal tubular acidosisChromosomal localization of a human band 3-like gene to region 7q35----7q36Cloning and characterization of band 3, the human erythrocyte anion-exchange protein (AE1)Anatomy of the herpes simplex virus 1 strain F glycoprotein B gene: primary sequence and predicted protein structure of the wild type and of monoclonal antibody-resistant mutantsTopographical localization of the C-terminal region of the voltage-dependent sodium channel from Electrophorus electricus using antibodies raised against a synthetic peptide.Hypothesis about the function of membrane-buried proline residues in transport proteinsErythroid anion transporter assembly is mediated by a developmentally regulated recruitment onto a preassembled membrane cytoskeleton.Functional carboxyl groups in the red cell anion exchange protein. Modification with an impermeant carbodiimide.Structure of the murine anion exchange protein.Multiple glycoproteins synthesized by the smallest RNA segment (S10) of bluetongue virus.Polylactosaminoglycan modification of a small integral membrane glycoprotein, influenza B virus NBAlternative primary structures in the transmembrane domain of the chicken erythroid anion transporter.Two chicken erythrocyte band 3 mRNAs are generated by alternative transcriptional initiation and differential RNA splicing.Two different mRNAs are transcribed from a single genomic locus encoding the chicken erythrocyte anion transport proteins (band 3).Topology models of anion exchanger 1 that incorporate the anti-parallel V-shaped motifs found in the EM structure.The "tunneling" mode of biological carrier-mediated transport.Transmembrane folding of the human erythrocyte anion exchanger (AE1, Band 3) determined by scanning and insertional N-glycosylation mutagenesis.Role of substrate binding forces in exchange-only transport systems: II. Implications for the mechanism of the anion exchanger of red cells.Oligomeric structure and the anion transport function of human erythrocyte band 3 protein.Functional factors in the red cell membrane: interactions between the membrane and its underlying skeleton.Heterogeneity in the human erythrocyte band 3 anion-transporter revealed by Triton X-114 phase partitioning.The complete amino acid sequence of the human erythrocyte membrane anion-transport protein deduced from the cDNA sequenceA partial structure for the gamma-aminobutyric acid (GABAA) receptor is derived from the model for the nicotinic acetylcholine receptor. The anion-exchange protein of cell membranes is related to the GABAA receptor.The human erythrocyte anion-transport protein. Further amino acid sequence from the integral membrane domain homologous with the murine protein.Lysine-691 of the anion exchanger from human erythrocytes is located on its cytoplasmic surface.Isolation and characterization of the rainbow trout erythrocyte band-3 protein.Primary structure and transmembrane orientation of the murine anion exchange protein.Degradation of the human erythrocyte membrane band 3 studied with monoclonal antibody directed against an epitope on the cytoplasmic fragment of band 3.Molecular mechanism for the red blood cell senescence clock.Role of N-glycosylation in the expression of human band 3-mediated anion transport.Proton inhibition of chloride exchange: asynchrony of band 3 proton and anion transport sites?Structural determinants of substrate specificity of the erythrocyte anion transporter.Evidence for similar function of transmembrane segments in receptor and membrane-anchored proteins
P2860
Q24295022-8A64F462-F876-429C-9A02-8DD3728FB603Q24561520-302C484E-11C4-46D1-B148-2BEE73D35FD4Q24647772-F5949F0C-965E-4401-AD04-ACD6E2BCAC6FQ24676341-C8BBD3DD-B08C-4AF1-80E8-E3CE0AD0956FQ28609272-4E8E34D5-4480-43FD-806C-83EB6B2229D6Q30403318-95A336F1-43EC-4A68-BB73-0767CFCFF009Q34587067-8443C7F1-8203-422C-8918-BF0B3005F35AQ35590093-E7C9A7D9-6A53-4620-8D24-0013E596424DQ36217645-9695F39D-8DD5-4E9D-A3F3-DAC7D51AEB71Q36410272-92FFF7BD-005B-43D3-835D-EBE8E102571BQ36485656-26E7453A-3ADA-41DF-BE3B-5C015175EC26Q36686946-AE3CC136-5C49-437A-8C42-27E92949BDD3Q36785093-7CB098F9-382A-4FC9-99FD-2B293B91BA54Q36785586-1F27498A-862A-4CB1-B40C-17885AC84893Q36796363-45AA139D-EE6A-40E6-B7E9-32F593495671Q36847410-7F9838B9-308F-4EDD-AC3E-6591B4BE1F95Q37860155-99CD9F3B-D1F2-4D94-96D7-5A47C3A83CC4Q38189342-B4D062B2-397C-4DCE-B58A-1A7EA60E6C2FQ38326334-6E45FD14-A180-4761-9022-297FB1A1E3BAQ38682163-7B404BBD-77A0-4153-A427-27759A2D8FCCQ40077925-D1CB20A6-86C4-444D-AFBE-8D24A83D6F3BQ40505233-2716109D-792A-4971-911B-058A6A1B9849Q41774418-1DC325A8-1371-4CB8-99FC-CAE49205C468Q42068548-AA77F506-A266-45E2-9887-4A915B46BD2FQ42200378-932E231C-B556-4A6E-AAD7-1D2374598A90Q42853495-8C6E460F-3056-45AC-938B-E4B8ADB79FAAQ42992245-3AB20235-4175-4692-98C3-6EFB3967C46EQ43459461-3CE25E7C-C8B2-46CE-8250-DFE742E660F3Q43489711-4745F6C8-AF5A-4DAC-B416-1D8134A888A1Q45256802-593D6CCB-842D-4AE6-8D60-AA36D3FE6B8DQ47294448-D22BDB79-CBB9-45DA-85C6-F2E40BE5D01AQ49121585-5DDF5E81-403D-4C5A-B6CF-45C9E0280932Q50155092-D64DB808-D5B8-4562-950A-BF3A17499C08Q52390087-32B12CB3-4C0A-49E9-98F7-3267754E87BAQ57685705-39AD3196-6763-4C2A-8122-6CA715D11F68
P2860
The human erythrocyte anion-transport protein. Partial amino acid sequence, conformation and a possible molecular mechanism for anion exchange.
description
1983 nî lūn-bûn
@nan
1983年の論文
@ja
1983年論文
@yue
1983年論文
@zh-hant
1983年論文
@zh-hk
1983年論文
@zh-mo
1983年論文
@zh-tw
1983年论文
@wuu
1983年论文
@zh
1983年论文
@zh-cn
name
The human erythrocyte anion-tr ...... mechanism for anion exchange.
@ast
The human erythrocyte anion-tr ...... mechanism for anion exchange.
@en
type
label
The human erythrocyte anion-tr ...... mechanism for anion exchange.
@ast
The human erythrocyte anion-tr ...... mechanism for anion exchange.
@en
prefLabel
The human erythrocyte anion-tr ...... mechanism for anion exchange.
@ast
The human erythrocyte anion-tr ...... mechanism for anion exchange.
@en
P2093
P2860
P356
P1433
P1476
The human erythrocyte anion-tr ...... mechanism for anion exchange.
@en
P2093
P2860
P304
P356
10.1042/BJ2130577
P407
P577
1983-09-01T00:00:00Z