Linked Life Data

18790693

Source:http://linkedlifedata.com/resource/pubmed/id/18790693

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2008-10-17
pubmed:abstractText
Nopp140, a highly phosphorylated nucleolar protein, negatively regulates CK2, a kinase essential for cell proliferation. We quantitatively analyzed the interaction between two subunits of CK2 and Nopp140 and characterized the mechanism by which InsP(6) inhibits the interaction. Nopp140 specifically binds to the catalytic subunit of CK2 (CK2alpha) with a dissociation constant of (K(d)) of 4nM, which interferes with the catalytic activity of CK2. The C-terminal region of Nopp140 is determined as CK2alpha-binding region by a yeast two-hybrid method as well as a direct measurement of the interaction between CK2alpha and deletion mutants of Nopp140. InsP(6) specifically binds to CK2alpha and disrupts the interaction between CK2alpha and Nopp140 with an IC(50) value of 25 microM, thereby attenuating the Nopp140-mediated repression of CK2 activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1090-2104
pubmed:author
pubmed:issnType
Electronic
pubmed:day
14
pubmed:volume
376
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
439-44
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Characterization of the InsP6-dependent interaction between CK2 and Nopp140.
pubmed:affiliation
Division of Life Sciences, Korea Institute of Science and Technology, 39-1, Hawolgok-dong, Songbuk-gu, 136-791, Seoul, Republic of Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't