Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5335
pubmed:dateCreated
1997-10-23
pubmed:abstractText
Chromosome maintenance region 1 (CRM1), a protein that shares sequence similarities with the karyopherin beta family of proteins involved in nuclear import pathway, was shown to form a complex with the leucine-rich nuclear export signal (NES). This interaction was inhibited by leptomycin B, a drug that prevents the function of the CRM1 protein in yeast. To analyze the role of the CRM1-NES interaction in nuclear export, a transport assay based on semipermeabilized cells was developed. In this system, which reconstituted NES-, cytosol-, and energy-dependent nuclear export, leptomycin B specifically blocked export of NES-containing proteins. Thus, the CRM1 protein could act as a NES receptor involved in nuclear protein export.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids, Unsaturated, http://linkedlifedata.com/resource/pubmed/chemical/I-kappa B Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Karyopherins, http://linkedlifedata.com/resource/pubmed/chemical/NF-kappaB inhibitor alpha, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Localization Signals, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Protein Sorting Signals, http://linkedlifedata.com/resource/pubmed/chemical/Pyruvate Kinase, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoplasmic and Nuclear, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/exportin 1 protein, http://linkedlifedata.com/resource/pubmed/chemical/leptomycin B
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
278
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
141-4
pubmed:dateRevised
2007-3-19
pubmed:meshHeading
pubmed-meshheading:9311922-Adenosine Triphosphate, pubmed-meshheading:9311922-Amino Acid Sequence, pubmed-meshheading:9311922-Biological Transport, pubmed-meshheading:9311922-Carrier Proteins, pubmed-meshheading:9311922-Cell Nucleus, pubmed-meshheading:9311922-DNA-Binding Proteins, pubmed-meshheading:9311922-Fatty Acids, Unsaturated, pubmed-meshheading:9311922-Fluorescent Antibody Technique, Indirect, pubmed-meshheading:9311922-HeLa Cells, pubmed-meshheading:9311922-Humans, pubmed-meshheading:9311922-I-kappa B Proteins, pubmed-meshheading:9311922-Immunoblotting, pubmed-meshheading:9311922-Karyopherins, pubmed-meshheading:9311922-Nuclear Localization Signals, pubmed-meshheading:9311922-Nuclear Proteins, pubmed-meshheading:9311922-Protein Sorting Signals, pubmed-meshheading:9311922-Pyruvate Kinase, pubmed-meshheading:9311922-Receptors, Cytoplasmic and Nuclear, pubmed-meshheading:9311922-Recombinant Fusion Proteins, pubmed-meshheading:9311922-Transfection
pubmed:year
1997
pubmed:articleTitle
Evidence for a role of CRM1 in signal-mediated nuclear protein export.
pubmed:affiliation
Institut Curie-CNRS Unité Mixte de Recherche 144, 26 rue d'Ulm, 75248 Paris Cedex 05, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't