Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1974-3-22
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Acetamides, http://linkedlifedata.com/resource/pubmed/chemical/Alcohol Oxidoreductases, http://linkedlifedata.com/resource/pubmed/chemical/Aspartic Acid, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Carbon Radioisotopes, http://linkedlifedata.com/resource/pubmed/chemical/Homoserine, http://linkedlifedata.com/resource/pubmed/chemical/Iodine, http://linkedlifedata.com/resource/pubmed/chemical/Mercuribenzoates, http://linkedlifedata.com/resource/pubmed/chemical/NADP, http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases, http://linkedlifedata.com/resource/pubmed/chemical/Salicylates, http://linkedlifedata.com/resource/pubmed/chemical/Sulfhydryl Reagents, http://linkedlifedata.com/resource/pubmed/chemical/Threonine
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
38
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
325-35
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1973
pubmed:articleTitle
The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K 12. Intra and intersubunit interactions between the catalytic regions of the bifunctional enzyme.
pubmed:publicationType
Journal Article