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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
16
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pubmed:dateCreated |
2001-7-23
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pubmed:abstractText |
The specificity of XapB permease was compared with that of the known nucleoside transporters NupG and NupC. XapB-mediated xanthosine uptake is abolished by 2,4-dinitrophenol and exhibits saturation kinetics with an apparent K(m) of 136 microM. A 12-transmembrane-segment model was confirmed by translational fusions to alkaline phosphatase and the alpha fragment of beta-galactosidase.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11466294-10065837,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11466294-1593632,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11466294-1840539,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11466294-1943817,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11466294-2170984,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11466294-2826388,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11466294-374403,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11466294-3860846,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11466294-4354132,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11466294-4591127,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11466294-7007808,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11466294-7007809,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11466294-7559336,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11466294-773649,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11466294-8027026,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11466294-9917392
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/NupC protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/NupC protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/NupG protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleosides,
http://linkedlifedata.com/resource/pubmed/chemical/XapB protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/xanthosine
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9193
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
183
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4900-4
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:11466294-Amino Acid Sequence,
pubmed-meshheading:11466294-Bacterial Proteins,
pubmed-meshheading:11466294-Carrier Proteins,
pubmed-meshheading:11466294-Escherichia coli,
pubmed-meshheading:11466294-Escherichia coli Proteins,
pubmed-meshheading:11466294-Kinetics,
pubmed-meshheading:11466294-Membrane Proteins,
pubmed-meshheading:11466294-Membrane Transport Proteins,
pubmed-meshheading:11466294-Models, Molecular,
pubmed-meshheading:11466294-Molecular Sequence Data,
pubmed-meshheading:11466294-Protein Conformation,
pubmed-meshheading:11466294-Protein Structure, Secondary,
pubmed-meshheading:11466294-Ribonucleosides,
pubmed-meshheading:11466294-Software,
pubmed-meshheading:11466294-Substrate Specificity
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pubmed:year |
2001
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pubmed:articleTitle |
Specificity and topology of the Escherichia coli xanthosine permease, a representative of the NHS subfamily of the major facilitator superfamily.
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pubmed:affiliation |
Department of Biological Chemistry, Institute of Molecular Biology, University of Copenhagen, 1307 Copenhagen K, Denmark.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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