Linked Life Data

3947342

Source:http://linkedlifedata.com/resource/pubmed/id/3947342

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1986-3-24
pubmed:abstractText
Phosphorylation of high mobility group (HMG) chromatin proteins was studied both in intact Chinese hamster ovary cells (strain CHO-P22) and in vitro conditions using isolated HMG proteins from the same cells and purified protein kinases. Prominent phosphorylation of serine in a low Mr HMG protein designated as HMG P was observed in unsynchronized cells. Of the three protein kinases tested, only nuclear type II protein kinase phosphorylated HMG P in vitro. The phosphorylated amino acid was phosphoserine. Cyclic nucleotide dependent protein kinases did not phosphorylate HMG P but phosphorylated HMG 14 with a preference for cGMP-dependent protein kinase. 32P-labeling of HMG 17 was not observed in intact cells or in vitro.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
134
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
617-23
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Phosphorylation of a low Mr high mobility group protein in Chinese hamster ovary cells.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't