Role of the charge pair aspartic acid-237-lysine-358 in the lactose permease of Escherichia coli.
about
Evolutionary mix-and-match with MFS transportersFunctional interactions between arginine-133 and aspartate-88 in the human reduced folate carrier: evidence for a charge-pair associationAlanine insertion scanning mutagenesis of lactose permease transmembrane helices.Neutralization of a conserved amino acid residue in the human Na+/glucose transporter (hSGLT1) generates a glucose-gated H+ channel.Helix packing of lactose permease in Escherichia coli studied by site-directed chemical cleavage.Mutation of conserved negatively charged residues in the S2 and S3 transmembrane segments of a mammalian K+ channel selectively modulates channel gatingFunctional architecture of MFS D-glucose transporters.Structure and function of the reduced folate carrier a paradigm of a major facilitator superfamily mammalian nutrient transporter.The central cytoplasmic loop of the major facilitator superfamily of transport proteins governs efficient membrane insertion.A molecular mechanism for energy coupling in a membrane transport protein, the lactose permease of Escherichia coli.Proton-coupled dynamics in lactose permease.Properties and purification of an active biotinylated lactose permease from Escherichia coli.Lessons from lactose permeaseAnalysis of substrate-binding elements in OxlT, the oxalate:formate antiporter of Oxalobacter formigenes.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.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.Interactions between residues in staphylococcal alpha-hemolysin revealed by reversion mutagenesis.Lactose permease H+-lactose symporter: mechanical switch or Brownian ratchet?Cysteine scanning mutagenesis of putative transmembrane helices IX and X in the lactose permease of Escherichia coli.Use of molecular modelling to probe the mechanism of the nucleoside transporter NupGBinding of monoclonal antibody 4B1 to homologs of the lactose permease of Escherichia coli.Helix dynamics in LacY: helices II and IVProperties of a LacY efflux mutantResidues in the H+ translocation site define the pKa for sugar binding to LacY.Site-directed mutagenesis reveals the importance of conserved charged residues for the transport activity of the PheP permease of Escherichia coli.Interacting domains in the epithelial sodium channel that mediate proteolytic activation.Specificity and promiscuity in membrane helix interactions.Mutagenesis studies of the cardiac Na(+)-Ca2+ exchanger.Deceleration of the E1P-E2P transition and ion transport by mutation of potentially salt bridge-forming residues Lys-791 and Glu-820 in gastric H+/K+-ATPase.Cysteine scanning mutagenesis of the N-terminal 32 amino acid residues in the lactose permease of Escherichia coli.Site-directed alkylation studies with LacY provide evidence for the alternating access model of transport.Conserved movement of TMS11 between occluded conformations of LacY and XylE of the major facilitator superfamily suggests a similar hinge-like mechanism.Phospholipid-assisted protein folding: phosphatidylethanolamine is required at a late step of the conformational maturation of the polytopic membrane protein lactose permease.Conservation of residues involved in sugar/H(+) symport by the sucrose permease of Escherichia coli relative to lactose permease.In vitro synthesis of lactose permease to probe the mechanism of membrane insertion and folding.In vitro folding of a membrane protein: effect of denaturation and renaturation on substrate binding by the lactose permease of Escherichia coli.Structure-function relationships in OxlT, the oxalate/formate transporter of Oxalobacter formigenes. Topological features of transmembrane helix 11 as visualized by site-directed fluorescent labeling.Role of the charge interaction between Arg(70) and Asp(120) in the Tn10-encoded metal-tetracycline/H(+) antiporter of Escherichia coli.Function, Structure, and Evolution of the Major Facilitator Superfamily: The LacY Manifesto
P2860
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P2860
Role of the charge pair aspartic acid-237-lysine-358 in the lactose permease of Escherichia coli.
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
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
@zh-hant
name
Role of the charge pair aspart ...... permease of Escherichia coli.
@en
Role of the charge pair aspart ...... permease of Escherichia coli.
@nl
type
label
Role of the charge pair aspart ...... permease of Escherichia coli.
@en
Role of the charge pair aspart ...... permease of Escherichia coli.
@nl
prefLabel
Role of the charge pair aspart ...... permease of Escherichia coli.
@en
Role of the charge pair aspart ...... permease of Escherichia coli.
@nl
P356
P1433
P1476
Role of the charge pair aspart ...... permease of Escherichia coli.
@en
P2093
Sahin-Tóth M
P304
P356
10.1021/BI00063A028
P407
P577
1993-03-01T00:00:00Z