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Article: Protein-protein interaction of FHL2, a LIM domain protein preferentially expressed in human heart, with hCDC47

TitleProtein-protein interaction of FHL2, a LIM domain protein preferentially expressed in human heart, with hCDC47
Authors
Issue Date2000
PublisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/35503
Citation
Journal Of Cellular Biochemistry, 2000, v. 76 n. 3, p. 499-508 How to Cite?
AbstractIn the yeast two-hybrid library screening, the heart-specific FHL2 protein was found to interact with hCDC47. In vitro interaction study between FHL2 protein and hCDC47 was demonstrated. From the results of domain studies by the yeast two-hybrid assay, the second and third LIM domains in conjunction with the first half LIM domain of FHL2 were identified to be important in binding with hCDC47. Besides, in Northern blot hybridization of human cancer cell lines, the highest FHL2 mRNA expression was detected in colorectal adenocarcinoma SW480 and HeLa cell S3. Our results imply that FHL2 protein may associate with cancer development and may act as a molecular adapter to form a multicomplex with hCDC47 in the nucleus, thus it plays an important role in the specification or maintenance of the terminal differentiated phenotype of heart muscle cells.
Persistent Identifierhttp://hdl.handle.net/10722/171677
ISSN
2015 Impact Factor: 3.446
2015 SCImago Journal Rankings: 1.520
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorChan, KKen_US
dc.contributor.authorTsui, SKWen_US
dc.contributor.authorNgai, SMen_US
dc.contributor.authorLee, SMYen_US
dc.contributor.authorKotaka, Men_US
dc.contributor.authorWaye, MMYen_US
dc.contributor.authorLee, CYen_US
dc.contributor.authorFung, KPen_US
dc.date.accessioned2012-10-30T06:16:18Z-
dc.date.available2012-10-30T06:16:18Z-
dc.date.issued2000en_US
dc.identifier.citationJournal Of Cellular Biochemistry, 2000, v. 76 n. 3, p. 499-508en_US
dc.identifier.issn0730-2312en_US
dc.identifier.urihttp://hdl.handle.net/10722/171677-
dc.description.abstractIn the yeast two-hybrid library screening, the heart-specific FHL2 protein was found to interact with hCDC47. In vitro interaction study between FHL2 protein and hCDC47 was demonstrated. From the results of domain studies by the yeast two-hybrid assay, the second and third LIM domains in conjunction with the first half LIM domain of FHL2 were identified to be important in binding with hCDC47. Besides, in Northern blot hybridization of human cancer cell lines, the highest FHL2 mRNA expression was detected in colorectal adenocarcinoma SW480 and HeLa cell S3. Our results imply that FHL2 protein may associate with cancer development and may act as a molecular adapter to form a multicomplex with hCDC47 in the nucleus, thus it plays an important role in the specification or maintenance of the terminal differentiated phenotype of heart muscle cells.en_US
dc.languageengen_US
dc.publisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/35503en_US
dc.relation.ispartofJournal of Cellular Biochemistryen_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshCell Cycle Proteins - Genetics - Metabolismen_US
dc.subject.meshCell Differentiationen_US
dc.subject.meshDna Primers - Geneticsen_US
dc.subject.meshDna-Binding Proteinsen_US
dc.subject.meshEscherichia Coli - Geneticsen_US
dc.subject.meshGene Expressionen_US
dc.subject.meshHela Cellsen_US
dc.subject.meshHomeodomain Proteins - Chemistry - Genetics - Metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshLim-Homeodomain Proteinsen_US
dc.subject.meshMuscle Proteinsen_US
dc.subject.meshMyocardium - Cytology - Metabolismen_US
dc.subject.meshNuclear Proteinsen_US
dc.subject.meshPhenotypeen_US
dc.subject.meshProtein Bindingen_US
dc.subject.meshProtein Structure, Tertiaryen_US
dc.subject.meshRna, Messenger - Genetics - Metabolismen_US
dc.subject.meshRna, Neoplasm - Genetics - Metabolismen_US
dc.subject.meshRecombinant Proteins - Chemistry - Genetics - Metabolismen_US
dc.subject.meshSaccharomyces Cerevisiae - Geneticsen_US
dc.subject.meshSaccharomyces Cerevisiae Proteinsen_US
dc.subject.meshTranscription Factorsen_US
dc.subject.meshTumor Cells, Cultureden_US
dc.subject.meshTwo-Hybrid System Techniquesen_US
dc.subject.meshZinc Fingersen_US
dc.titleProtein-protein interaction of FHL2, a LIM domain protein preferentially expressed in human heart, with hCDC47en_US
dc.typeArticleen_US
dc.identifier.emailKotaka, M:masayo@hku.hken_US
dc.identifier.authorityKotaka, M=rp00293en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1002/(SICI)1097-4644(20000301)76:3<499::AID-JCB16>3.0.CO;2-4en_US
dc.identifier.pmid10649446-
dc.identifier.scopuseid_2-s2.0-0033980685en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0033980685&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume76en_US
dc.identifier.issue3en_US
dc.identifier.spage499en_US
dc.identifier.epage508en_US
dc.identifier.isiWOS:000085184500016-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridChan, KK=7406034649en_US
dc.identifier.scopusauthoridTsui, SKW=7004961364en_US
dc.identifier.scopusauthoridNgai, SM=7006074219en_US
dc.identifier.scopusauthoridLee, SMY=35233892600en_US
dc.identifier.scopusauthoridKotaka, M=6604073578en_US
dc.identifier.scopusauthoridWaye, MMY=7006687733en_US
dc.identifier.scopusauthoridLee, CY=7410142857en_US
dc.identifier.scopusauthoridFung, KP=35271657800en_US

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