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HAMLET binding to ?-actinin facilitates tumor cell detachment

By Trulsson M., Yu H., Gisselsson L., Chao Y., Urbano A., Aits S., Mossberg A.-K. and Svanborg C.

Abstract

10.1371/journal.pone.0017179PLoS ONE63e1717

Topics: alpha actinin, alpha actinin 1, alpha actinin 4, alpha lactalbumin, beta1 integrin, F actin, focal adhesion kinase 1, human alpha lactalbumin made lethal to tumor cell, ion channel, mitogen activated protein kinase 1, small interfering RNA, unclassified drug, actin, actinin, beta1 integrin, cell extract, focal adhesion kinase, HAMLET complex, human, lactalbumin, oleic acid, peptide, amino acid sequence, article, binding site, cell adhesion, cell proliferation, cell structure, cell survival, cell viability, controlled study, enzyme phosphorylation, human, human cell, immunoprecipitation, in vitro study, molecular mechanics, polyacrylamide gel electrophoresis, protein binding, protein cross linking, protein domain, protein expression, protein isolation, protein localization, protein protein interaction, signal transduction, tumor cell, biological model, cell adhesion, cell death, chemical structure, chemistry, drug effect, enzymology, metabolism, molecular genetics, neoplasm, pathology, protein analysis, protein binding, protein transport, tumor cell line, Actinin, Actins, Amino Acid Sequence, Antigens, CD29, Binding Sites, Cell Adhesion, Cell Death, Cell Extracts, Cell Line, Tumor, Cell Survival, Focal Adhesion Protein-Tyrosine Kinases, Humans, Lactalbumin, Models, Biological, Models, Molecular, Molecular Sequence Data, Neoplasms, Oleic Acids, Peptides, Protein Binding, Protein Interaction Mapping, Protein Transport, Signal Transduction
Publisher: 'Public Library of Science (PLoS)'
Year: 2011
DOI identifier: 10.1371/journal.pone.0017179
OAI identifier: oai:scholarbank.nus.edu.sg:10635/162055
Provided by: ScholarBank@NUS
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