Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2010-3-9
pubmed:abstractText
Cholesterol is a major constituent of the plasma membrane in eukaryotic cells. It regulates the physical state of the phospholipid bilayer and is crucially involved in the formation of membrane microdomains. Cholesterol also affects the activity of several membrane proteins, and is the precursor for steroid hormones and bile acids. Here, methods are described that are used to explore the binding and/or interaction of proteins to cholesterol. For this purpose, a variety of cholesterol probes bearing radio-, spin-, photoaffinity- or fluorescent labels are currently available. Examples of proven cholesterol binding molecules are polyene compounds, cholesterol-dependent cytolysins, enzymes accepting cholesterol as substrate, and proteins with cholesterol binding motifs. Main topics of this report are the localization of candidate membrane proteins in cholesterol-rich microdomains, the issue of specificity of cholesterol- protein interactions, and applications of the various cholesterol probes for these studies.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/4-Chloro-7-nitrobenzofurazan, http://linkedlifedata.com/resource/pubmed/chemical/7-nitrobenz-2-oxa-1,3-diazol-4-ylcho..., http://linkedlifedata.com/resource/pubmed/chemical/Affinity Labels, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol, http://linkedlifedata.com/resource/pubmed/chemical/Cyclodextrins, http://linkedlifedata.com/resource/pubmed/chemical/Cytotoxins, http://linkedlifedata.com/resource/pubmed/chemical/Filipin, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Spin Labels, http://linkedlifedata.com/resource/pubmed/chemical/Steroid Hydroxylases, http://linkedlifedata.com/resource/pubmed/chemical/Sterol O-Acyltransferase, http://linkedlifedata.com/resource/pubmed/chemical/Sulfotransferases, http://linkedlifedata.com/resource/pubmed/chemical/cholesterol 24-hydroxylase, http://linkedlifedata.com/resource/pubmed/chemical/cholesterol sulfotransferase, http://linkedlifedata.com/resource/pubmed/chemical/cholesterol-binding protein
pubmed:status
MEDLINE
pubmed:issn
0306-0225
pubmed:author
pubmed:issnType
Print
pubmed:volume
51
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-45
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Cholesterol-protein interaction: methods and cholesterol reporter molecules.
pubmed:affiliation
Institut für Biochemie, Johannes Gutenberg-Universität, Johann-Joachim-Becherweg 30, Mainz, Germany. Gimpl@uni-mainz.de
pubmed:publicationType
Journal Article, Review