Linked Life Data

9083116

Source:http://linkedlifedata.com/resource/pubmed/id/9083116

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1997-6-11
pubmed:abstractText
Channel-forming colicins undergo a remarkable series of conformational gyrations during their voyage from the extracellular milieu to the periplasmic membrane. Crystal structures of the intact colicin la molecule and a channel-forming domain of colicin E1 illuminate relationships between the molecular structure and biological function of these voltage-dependent channel-forming toxins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0969-2126
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
313-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
The long and short of colicin action: the molecular basis for the biological activity of channel-forming colicins.
pubmed:affiliation
Department of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168th Street, New York, NY 10032, USA. jeg52@columbia.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Review, Research Support, Non-U.S. Gov't