Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2001-3-15
pubmed:abstractText
A variety of sodium-substrate cotransport systems are known in bacteria. Sodium enters the cell down an electrochemical concentration gradient. There is obligatory coupling between the entry of the ion and the entry of substrate with a stoichiometry (in the cases studied) of 1:1. Thus, the downhill movement of sodium ion into the cell leads to the accumulation of substrate within the cell. The melibiose carrier of Escherichia coli is perhaps the most carefully studied of the sodium cotransport systems in bacteria. This carrier is of special interest because it can also use protons or lithium ions for cotransport. Other sodium cotransport carriers that have been studied recently are for proline, glutamate, serine-threonine, citrate and branched chain amino acids.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acid Transport System X-AG, http://linkedlifedata.com/resource/pubmed/chemical/Amino Acid Transport Systems..., http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids, Branched-Chain, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Citric Acid, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Glutamate Plasma Membrane..., http://linkedlifedata.com/resource/pubmed/chemical/Glutamates, http://linkedlifedata.com/resource/pubmed/chemical/Melibiose, http://linkedlifedata.com/resource/pubmed/chemical/PutP protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/Serine, http://linkedlifedata.com/resource/pubmed/chemical/Sodium, http://linkedlifedata.com/resource/pubmed/chemical/Symporters, http://linkedlifedata.com/resource/pubmed/chemical/Threonine
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
1505
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
121-30
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed-meshheading:11248194-Amino Acid Sequence, pubmed-meshheading:11248194-Amino Acid Transport System X-AG, pubmed-meshheading:11248194-Amino Acid Transport Systems, Neutral, pubmed-meshheading:11248194-Amino Acids, Branched-Chain, pubmed-meshheading:11248194-Bacterial Proteins, pubmed-meshheading:11248194-Binding Sites, pubmed-meshheading:11248194-Carrier Proteins, pubmed-meshheading:11248194-Citric Acid, pubmed-meshheading:11248194-Cytoplasm, pubmed-meshheading:11248194-Escherichia coli Proteins, pubmed-meshheading:11248194-Glutamate Plasma Membrane Transport Proteins, pubmed-meshheading:11248194-Glutamates, pubmed-meshheading:11248194-Ion Transport, pubmed-meshheading:11248194-Melibiose, pubmed-meshheading:11248194-Molecular Sequence Data, pubmed-meshheading:11248194-Periplasm, pubmed-meshheading:11248194-Serine, pubmed-meshheading:11248194-Sodium, pubmed-meshheading:11248194-Substrate Specificity, pubmed-meshheading:11248194-Symporters, pubmed-meshheading:11248194-Threonine
pubmed:year
2001
pubmed:articleTitle
Sodium-substrate cotransport in bacteria.
pubmed:affiliation
Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA. thomas_wilson@hms.harvard.edu
pubmed:publicationType
Journal Article, Review