Linked Life Data

10066480

Source:http://linkedlifedata.com/resource/pubmed/id/10066480

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1999-8-6
pubmed:abstractText
The recent discovery of binding protein dependent secondary transporters and the ever-growing family of membrane potential generating secondary transporters emphasize the diversity of transport systems in both the mechanistical and physiological sense. The vast amount of data on the lactose permease is now beginning to crystallize in a model that relates functional events to structural changes of the protein. Evidence has been presented that multidrug transporters pick up their substrates from the membrane, and the binding of a number of substrates to the binding-protein components of ATP-driven transporters is now understood in detail.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1369-5274
pubmed:author
pubmed:issnType
Print
pubmed:volume
1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
248-53
pubmed:dateRevised
2005-11-16
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Bacterial solute uptake and efflux systems.
pubmed:affiliation
Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands. j.s.lolkema@biol.rug.nl
pubmed:publicationType
Journal Article, Review