Properties of permease dimer, a fusion protein containing two lactose permease molecules from Escherichia coli.
about
The yeast mitochondrial ADP/ATP carrier functions as a monomer in mitochondrial membranesInteractions between co-expressed Arabidopsis sucrose transporters in the split-ubiquitin systemThe kamikaze approach to membrane transportThe lactose transport protein is a cooperative dimer with two sugar translocation pathwaysOligomerization of serotonin transporter and its functional consequencesEngineering a terbium-binding site into an integral membrane protein for luminescence energy transfer.Alanine insertion scanning mutagenesis of lactose permease transmembrane helices.Investigation of the biophysical and cell biological properties of ferroportin, a multipass integral membrane protein iron exporter.Distance determination in proteins using designed metal ion binding sites and site-directed spin labeling: application to the lactose permease of Escherichia coli.Identification of the minimal functional unit of the homo-oligomeric human reduced folate carrier.Helix packing of lactose permease in Escherichia coli studied by site-directed chemical cleavage.Surface-exposed positions in the transmembrane helices of the lactose permease of Escherichia coli determined by intermolecular thiol cross-linking.Changing the lactose permease of Escherichia coli into a galactose-specific symporterStructure-function relationships of integral membrane proteins: membrane transporters vs channels.Cloning and molecular characterization of the ontogeny of a rat ileal sodium-dependent bile acid transporter.An early event in the transport mechanism of LacY protein: interaction between helices V and I.The central cytoplasmic loop of the major facilitator superfamily of transport proteins governs efficient membrane insertion.The lactose permease of Escherichia coli: overall structure, the sugar-binding site and the alternating access model for transport.Conformational flexibility at the substrate binding site in the lactose permease of Escherichia coli.Intermolecular thiol cross-linking via loops in the lactose permease of Escherichia coli.Role of the irreplaceable residues in the LacY alternating access mechanismA molecular mechanism for energy coupling in a membrane transport protein, the lactose permease of Escherichia coli.A molecular biology-based approach to resolve the subunit orientation of lipoprotein lipase.The substrate-binding site in the lactose permease of Escherichia coli.Structural analysis of cloned plasma membrane proteins by freeze-fracture electron microscopy.Biochemical and biophysical analyses of tight junction permeability made of claudin-16 and claudin-19 dimerization.The oligomeric state and stability of the mannitol transporter, EnzymeII(mtl), from Escherichia coli: a fluorescence correlation spectroscopy study.Lessons from lactose permeaseExploiting luminescence spectroscopy to elucidate the interaction between sugar and a tryptophan residue in the lactose permease of Escherichia coli.Oligomeric structure and minimal functional unit of the electrogenic sodium bicarbonate cotransporter NBCe1-A.A general method for determining helix packing in membrane proteins in situ: helices I and II are close to helix VII in the lactose permease of Escherichia coli.Functional role of oligomerization for bacterial and plant SWEET sugar transporter family.Pentameric assembly of a neuronal glutamate transporter.Site-directed spin labeling and chemical crosslinking demonstrate that helix V is close to helices VII and VIII in the lactose permease of Escherichia coli.Single molecule analysis reveals coexistence of stable serotonin transporter monomers and oligomers in the live cell plasma membrane.Fluorescence of native single-Trp mutants in the lactose permease from Escherichia coli: structural properties and evidence for a substrate-induced conformational change.Ligand-induced conformational changes in the lactose permease of Escherichia coli: evidence for two binding sitesResidues gating the periplasmic pathway of LacY.Elucidation of substrate binding interactions in a membrane transport protein by mass spectrometry.The citrate carrier CitS probed by single-molecule fluorescence spectroscopy.
P2860
Q24674604-DF32AD29-AC76-4BE8-A3C7-B64CA3078B03Q24792412-BB4ED304-690F-4880-98E4-DCC54C3894A6Q28210636-1C9759BA-4E06-4E43-A21A-F3AD7A833DF9Q28366794-10C6580F-44DD-4F54-ABB6-116689A47440Q28576047-307E4BA0-4A9B-401C-AAE9-9286F8B98D1CQ30329955-BCB1227F-E8F9-495F-A6F3-8A378E5252E0Q30428848-C7BEE460-E77A-4FB3-A1B0-18EF9BF9B80FQ30487384-BD432552-4302-4362-B411-E89274A78BF5Q33666655-8DD8EBD6-CFCD-435A-BEA1-401F5E080F8DQ33717581-214C418C-A8BC-473C-87CB-F0C47D585EE5Q33891527-67F496DE-430B-46E7-A1A2-02C8500457CBQ34018588-B8C9F585-D3BD-412B-BB5B-E81E2666A2F9Q34067143-680D4A16-BE35-4717-9AFF-8973E5A900F2Q34136300-CF22326B-EC91-4B8C-82B4-0B7F59EC9FC1Q34201711-5D645A78-45B2-49D0-86C6-FA8D3D3D6B82Q35182861-A8CE783F-658B-4E6F-B891-754433101421Q35191643-A33D7DC6-E963-4AA8-89B0-EF60AF07566CQ35589999-76669CD5-B8A3-4E66-9044-279BE7A65A5CQ35641812-C3B0F6E3-7944-4EAA-9EA3-8C587D8CDA34Q35917647-AF83F103-4D08-4D71-AA32-CC8DDA94F3A2Q36140695-EE4C8A09-CF31-4627-9939-47ED2A58E535Q36150104-2181898B-745B-438B-BB1C-DF93A8C06AD6Q36151990-E9DB5CC4-FDB3-452D-B1C3-8ADA35CB2060Q36276555-D0769DC2-88E4-4848-BCB2-3FCA2F0CC1F0Q36308819-8D9939B2-C3FD-40CA-961B-54723F78DCE3Q36337005-97C07CC0-4B28-4C25-89DF-709486181331Q36458531-A1328648-AC89-4AA1-9E1E-2447A713D731Q36475370-03B2517E-7E63-4DAA-B7F8-32B7353AB72DQ36689630-E3220900-C6B8-454E-892F-3904CE97B526Q36897662-05E097CC-9051-489C-ABB1-1D36F0C8AB7CQ37042961-BB169D2D-69AD-4AD0-AC73-DF94B779EC92Q37203988-8B00DF98-150E-4E97-A3F1-B2FCAC53C7F1Q37236922-4CD7F80B-37BF-4C11-A684-05F2AD5736CEQ37327186-90787DBD-882D-4176-9FB7-BBFDA479C579Q37583590-15BD80AF-6174-4A93-97DD-40ACCBD12315Q38289728-E9A43B84-22A7-4E23-8EAB-394A1F7D6059Q38302054-0302484E-1576-4216-BF99-AC93AEE36676Q38350170-6FAF99B4-8F50-4F0C-9CB0-299011607048Q39744826-02341001-98E8-49F1-B608-93CE28D42185Q40231077-5645D71D-1802-42E4-9FEA-D4C5C243DDEF
P2860
Properties of permease dimer, a fusion protein containing two lactose permease molecules from Escherichia coli.
description
1994 nî lūn-bûn
@nan
1994 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Properties of permease dimer, ...... lecules from Escherichia coli.
@ast
Properties of permease dimer, ...... lecules from Escherichia coli.
@en
type
label
Properties of permease dimer, ...... lecules from Escherichia coli.
@ast
Properties of permease dimer, ...... lecules from Escherichia coli.
@en
prefLabel
Properties of permease dimer, ...... lecules from Escherichia coli.
@ast
Properties of permease dimer, ...... lecules from Escherichia coli.
@en
P2860
P356
P1476
Properties of permease dimer, ...... lecules from Escherichia coli.
@en
P2093
Lawrence MC
Sahin-Tóth M
P2860
P304
P356
10.1073/PNAS.91.12.5421
P407
P577
1994-06-01T00:00:00Z