Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
2001-1-26
pubmed:abstractText
Sister chromatid cohesion depends on a complex called cohesin, which contains at least four subunits: Smc1, Smc3, Scc1 and Scc3. Cohesion is established during DNA replication, is partially dismantled in many, but not all, organisms during prophase, and is finally destroyed at the metaphase-to-anaphase transition. A quite separate protein called Spo76 is required for sister chromatid cohesion during meiosis in the ascomycete Sordaria. Spo76-like proteins are highly conserved amongst eukaryotes and a homologue in Aspergillus nidulans, called BimD, is required for the completion of mitosis. The isolation of the cohesin subunit Smc3 as a suppressor of BimD mutations suggests that Spo76/BimD might function in the same process as cohesin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone, http://linkedlifedata.com/resource/pubmed/chemical/DNA, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/MCD1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Protein Subunits, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-myc, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/cohesins
pubmed:status
MEDLINE
pubmed:issn
0960-9822
pubmed:author
pubmed:issnType
Print
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1557-64
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11137006-Animals, pubmed-meshheading:11137006-Blotting, Western, pubmed-meshheading:11137006-Cell Cycle, pubmed-meshheading:11137006-Cell Cycle Proteins, pubmed-meshheading:11137006-Cell Separation, pubmed-meshheading:11137006-Chromatids, pubmed-meshheading:11137006-Chromosomal Proteins, Non-Histone, pubmed-meshheading:11137006-DNA, pubmed-meshheading:11137006-Flow Cytometry, pubmed-meshheading:11137006-Fungal Proteins, pubmed-meshheading:11137006-Genes, Reporter, pubmed-meshheading:11137006-Humans, pubmed-meshheading:11137006-Macromolecular Substances, pubmed-meshheading:11137006-Nuclear Proteins, pubmed-meshheading:11137006-Phosphoproteins, pubmed-meshheading:11137006-Precipitin Tests, pubmed-meshheading:11137006-Protein Structure, Tertiary, pubmed-meshheading:11137006-Protein Subunits, pubmed-meshheading:11137006-Proto-Oncogene Proteins c-myc, pubmed-meshheading:11137006-Recombinant Fusion Proteins, pubmed-meshheading:11137006-Saccharomyces cerevisiae, pubmed-meshheading:11137006-Saccharomyces cerevisiae Proteins
pubmed:articleTitle
Pds5 cooperates with cohesin in maintaining sister chromatid cohesion.
pubmed:affiliation
Research Institute of Molecular Pathology, Dr Bohr-gasse 7, A-1030 Vienna, Austria.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't