Source:http://linkedlifedata.com/resource/pubmed/id/12893054
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
2003-8-1
|
| pubmed:abstractText |
Pore-forming protein toxins possess the remarkable property that they can exist either in a stable water-soluble state or as an integral membrane pore. In order to convert from the water-soluble to the membrane state, the toxin must undergo large conformational changes. Recent work on a class of pore-forming toxins that are rich in beta-sheet content suggests a common mechanism of membrane insertion may exist despite these toxins possessing very different primary, tertiary and quaternary structures.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
0041-0101
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
42
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1-6
|
| pubmed:dateRevised |
2010-11-18
|
| pubmed:meshHeading |
pubmed-meshheading:12893054-Amino Acid Sequence,
pubmed-meshheading:12893054-Animals,
pubmed-meshheading:12893054-Bacterial Proteins,
pubmed-meshheading:12893054-Bacterial Toxins,
pubmed-meshheading:12893054-Cell Membrane,
pubmed-meshheading:12893054-Hydrophobic and Hydrophilic Interactions,
pubmed-meshheading:12893054-Molecular Sequence Data,
pubmed-meshheading:12893054-Protein Conformation,
pubmed-meshheading:12893054-Sequence Analysis, Protein
|
| pubmed:year |
2003
|
| pubmed:articleTitle |
Cryptic clues as to how water-soluble protein toxins form pores in membranes.
|
| pubmed:affiliation |
Biota Structural Biology Laboratory, St Vincent's Institute of Medical Research, 9 Princes Street, Fitzroy, Victoria 3065, Australia. mwp@rubens.its.unimelb.edu.au
|
| pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
|