Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1990-3-26
pubmed:abstractText
Tumor necrosis factor alpha was found to rapidly phosphorylate the unique mammalian small heat shock protein hsp28 without impairing its cytoplasmic localization and without inducing the synthesis of the heat shock proteins. In contrast to the C-kinase-dependent phosphorylation of hsp28 in response to the tumor promoter phorbol-12-myristate-13-acetate, the heat- and tumor necrosis factor-mediated phosphorylation of this heat shock protein appears to occur independently of C kinase. These observations suggest that a C-kinase-independent phosphorylation of hsp28 may be an early event in the cellular action of tumor necrosis factor alpha.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-1103152, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-2410257, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-2427013, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-2439511, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-2536751, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-2645298, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-2661562, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-2721674, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-2745558, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-2762307, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-2846348, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-2967329, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-2995366, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-2997166, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-2999289, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-2999773, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-3031163, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-3072471, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-3107882, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-3123274, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-3170655, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-3264252, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-3358773, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-3680201, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-3756916, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-3764421, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-3919015, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-3933111, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-3972098, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-6083778, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-6193982, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-6285380, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-6717429, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-6772504, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-6828852, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-729577, http://linkedlifedata.com/resource/pubmed/commentcorrection/2304467-7306990
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0270-7306
pubmed:author
pubmed:issnType
Print
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1276-80
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Tumor necrosis factor induces the rapid phosphorylation of the mammalian heat shock protein hsp28.
pubmed:affiliation
Department of Molecular Biology, Universite de Geneva, Switzerland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't