Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2009-9-30
pubmed:abstractText
The ErbB2/Her2/Neu receptor tyrosine kinase is amplified in approximately 30% of human breast cancers. Phosphorylation of the translation initiation factor, eIF2alpha inhibits global protein synthesis and activates a stress signaling and growth suppressive program. We have shown that forced phosphorylation of eIF2alpha can suppress head and neck, colorectal carcinoma and multiple myeloma tumor growth and/or survival. Here we explore whether ErbB2 modulates eIF2alpha phosphorylation and whether forced phosphorylation of the latter can antagonize ErbB2 deregulation of mammary acinar morphogenesis.
pubmed:grant
pubmed:commentsCorrections
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pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1471-2121
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
64
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Inhibition of eIF2alpha dephosphorylation inhibits ErbB2-induced deregulation of mammary acinar morphogenesis.
pubmed:affiliation
Department of Medicine, Division of Hematology and Oncology, Tisch Cancer Institute at Mount Sinai, Mount Sinai School of Medicine, One Gustave L. Levy Place, New York, NY 10029, USA. ss7267@albany.edu
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural