About: Evidence that transmembrane segment 2 of the lactose permease is part of a conformationally sensitive interface between the two halves of the protein

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About: Evidence that transmembrane segment 2 of the lactose permease is part of a conformationally sensitive interface between the two halves of the protein Goto Sponge NotDistinct Permalink

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scientific article published in Journal of Biological Chemistry

Attributes	Values
rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) наукова стаття, опублікована в січні 1996 (uk) article publié dans la revue scientifique Journal of Biological Chemistry (fr) im Januar 1996 veröffentlichter wissenschaftlicher Artikel (de) scientific article published in Journal of Biological Chemistry (en)
publication date	wds:Q56903540-6F58CCA3-7ED1-4C14-8182-3E16A3A35123
publication date	1996-01-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q56903540-C9CE59D8-6F9D-49D8-8CE2-B2637730B894
language of work or name	English
cites work	wds:Q56903540-4BB8BA3F-C5A8-488F-A4F7-3B10B131A4D5 wds:Q56903540-4D9DDB6F-E26A-467C-AC0B-BE43C8E5FDAD wds:Q56903540-4F9977F2-1E63-4783-8899-9214A0CFE570 wds:Q56903540-4FAD5F3D-6318-4189-A097-677EBBFFE44A wds:Q56903540-517639EF-955B-42A5-8C7B-998638D59874 wds:Q56903540-59FBB183-E72A-4053-A005-E99FDD5C281A wds:Q56903540-5B76E1EE-793C-4DEF-943D-287434B94C9B wds:Q56903540-685EB509-A4BB-4403-8F2E-11F2F149D054 wds:Q56903540-77FE9321-AA78-4C32-A1A8-251FD43A370F wds:Q56903540-78E09201-A9C3-49E6-9286-98145E4B4C4C wds:Q56903540-7BA8FCA9-DC69-4B9E-9C04-31C07226B825 wds:Q56903540-82F6D61C-5CDB-4C5B-A649-8952A7EFA4DC wds:Q56903540-87D0ECD5-9381-42DE-BC4B-508881BBE5C6 wds:Q56903540-94E42E99-17AD-48D4-B624-E547AB683926 wds:Q56903540-B636CE74-21A5-4CF5-A9A5-AAB51E59F0FA wds:Q56903540-CA2F6325-9800-46C3-A386-A885D1820308
cites work	The interaction between aspartic acid 237 and lysine 358 in the lactose carrier of Escherichia coli Structural features of the uniporter/symporter/antiporter superfamily Membrane transport proteins: implications of sequence comparisons Amplification of the lactose carrier protein in Escherichia coli using a plasmid vector lac permease of Escherichia coli: topology and sequence elements promoting membrane insertion Cation specificity for sugar substrates of the melibiose carrier in Escherichia coli Lactose Carrier Protein of Escherichia coli Structure and Expression of Plasmids Carrying the Y Gene of the lac Operon A major superfamily of transmembrane facilitators that catalyse uniport, symport and antiport Structural mechanisms for domain movements in proteins Isolation and nucleotide sequencing of lactose carrier mutants that transport maltose Mammalian and bacterial sugar transport proteins are homologous Sequence of the lactose permease gene. The conserved motif, GXXX(D/E)(R/K)XG[X](R/K)(R/K), in hydrophilic loop 2/3 of the lactose permease. Proton-linked sugar transport systems in bacteria The lac permease of Escherichia coli: site-directed mutagenesis studies on the mechanism of beta-galactoside/H+ symport The lactose permease of Escherichia coli
author name string	wds:Q56903540-B84DC253-CE87-445A-B4D2-5BF48077D037 wds:Q56903540-D62DFBFC-D564-46AF-928D-9C87E4AC21DA
author name string	A E Jessen-Marshall R J Brooker
rdfs:label	Evidence that transmembrane segment 2 of the lactose permease is part of a conformationally sensitive interface between the two halves of the protein (en) Evidence that transmembrane segment 2 of the lactose permease is part of a conformationally sensitive interface between the two halves of the protein (nl)
skos:prefLabel	Evidence that transmembrane segment 2 of the lactose permease is part of a conformationally sensitive interface between the two halves of the protein (en) Evidence that transmembrane segment 2 of the lactose permease is part of a conformationally sensitive interface between the two halves of the protein (nl)
name	Evidence that transmembrane segment 2 of the lactose permease is part of a conformationally sensitive interface between the two halves of the protein (en) Evidence that transmembrane segment 2 of the lactose permease is part of a conformationally sensitive interface between the two halves of the protein (nl)
title	wds:Q56903540-6085E5D6-D833-4FAF-930F-D16B31BB642B
title	Evidence that transmembrane segment 2 of the lactose permease is part of a conformationally sensitive interface between the two halves of the protein (en)
page(s)	wds:Q56903540-14222FA7-AAE6-41D7-8BAD-D4CFBAB24E2F
page(s)	1400-1404
instance of	wds:Q56903540-FC48CC7F-5F91-4308-8DF0-EF5C89393ECE
instance of	scholarly article
main subject	wds:Q56903540-0B90A1F2-A5DB-4B07-AD90-1D93A2F8715C
main subject	transmembrane protein
PubMed ID	wds:Q56903540-0FFDA291-6B93-409C-A903-E058D905B01C
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8576130
PubMed ID	8576130
published in	wds:Q56903540-E89E63C6-3FB3-4FDB-A68D-0BC5EDD00DA5
published in	Journal of Biological Chemistry
issue	wds:Q56903540-CDEAD74B-F1D1-433E-BA2A-82276ADBAAAD
volume	wds:Q56903540-660F880C-4946-4B01-86F6-911D48D6D277
issue	3
volume	271
DOI	wds:Q56903540-0136EBCD-E2FE-4245-98A6-1FF6F715A638
DOI	http://dx.doi.org/10.1074/JBC.271.3.1400
DOI	10.1074/JBC.271.3.1400
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q56903540
is cites work of	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 The kamikaze approach to membrane transport Analysis of tryptophan residues in the staphylococcal multidrug transporter QacA reveals long-distance functional associations of residues on opposite sides of the membrane Structural model for 12-helix transporters belonging to the major facilitator superfamily Suppressor analysis of mutations in the loop 2-3 motif of lactose permease: evidence that glycine-64 is an important residue for conformational changes An analysis of suppressor mutations suggests that the two halves of the lactose permease function in a symmetrical manner Evidence that highly conserved residues of transmembrane segment 6 of Escherichia coli MntH are important for transport activity Helix dynamics in LacY: helices II and IV Structure of the YajR transporter suggests a transport mechanism based on the conserved motif A Proton-dependent multidrug efflux systems A revised model for the structure and function of the lactose permease. Evidence that a face on transmembrane segment 2 is important for conformational changes Four conserved cytoplasmic sequence motifs are important for transport function of the Leishmania inositol/H(+) symporter. Facilitated Drug Influx by an Energy-uncoupled Secondary Multidrug Transporter Functional significance of the "signature cysteine" in helix 8 of the Escherichia coli 4-aminobutyrate transporter from the amine-polyamine-choline superfamily. Restoration of Cys-300 to the Cys-less Gabp. Second-site suppressor mutations of inactivating substitutions at gly247 of the tetracycline efflux protein, Tet(B). Transmembrane remote conformational suppression of the Gly-332 mutation of the Tn10-encoded metal-tetracycline/H+ antiporter. Role of the charge interaction between Arg(70) and Asp(120) in the Tn10-encoded metal-tetracycline/H(+) antiporter of Escherichia coli. A suppressor analysis of residues involved in cation transport in the lactose permease: identification of a coupling sensor Uptake dynamics in the Lactose permease (LacY) membrane protein transporter
is cites work of	wds:Q34688092-270C4073-D390-4E2F-A70E-0F38822CFB7E wds:Q28210636-8CB41A94-9373-49F5-B150-8DAC7D4A0D85 wds:Q35622214-E666F984-EABA-4EB5-84D4-475F85A32CF3 wds:Q37042961-B807FCAB-959C-4FA1-A426-1AA171A81966 wds:Q33994981-D21CDCE3-2096-431A-BEA6-EDCE317BD5F9 wds:Q44619468-334F0735-4E1D-4A26-B786-CF7A8773B5F1 wds:Q58698722-40182DFE-A407-4F21-9CD8-F0004CC1D352

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