Charge-based interaction conserved within histone H3 lysine 4 (H3K4) methyltransferase complexes is needed for protein stability, histone methylation, and gene expression.
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| Title: | Charge-based interaction conserved within histone H3 lysine 4 (H3K4) methyltransferase complexes is needed for protein stability, histone methylation, and gene expression. |
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| Authors: | Mersman DP; Department of Biochemistry and Purdue University Center for Cancer Research, Purdue University, West Lafayette, Indiana 47907, USA., Du HN, Fingerman IM, South PF, Briggs SD |
| Source: | The Journal of biological chemistry [J Biol Chem] 2012 Jan 20; Vol. 287 (4), pp. 2652-65. Date of Electronic Publication: 2011 Dec 06. |
| Publication Type: | Journal Article; Research Support, N.I.H., Extramural |
| Journal Info: | Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1083-351X (Electronic) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE |
| Database: | MEDLINE Ultimate |
| FullText | Text: Availability: 0 |
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| Header | DbId: mdl DbLabel: MEDLINE Ultimate An: 22147691 AccessLevel: 2 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Charge-based interaction conserved within histone H3 lysine 4 (H3K4) methyltransferase complexes is needed for protein stability, histone methylation, and gene expression. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AU" term="%22Mersman+DP%22">Mersman DP</searchLink>; Department of Biochemistry and Purdue University Center for Cancer Research, Purdue University, West Lafayette, Indiana 47907, USA.<br /><searchLink fieldCode="AU" term="%22Du+HN%22">Du HN</searchLink><br /><searchLink fieldCode="AU" term="%22Fingerman+IM%22">Fingerman IM</searchLink><br /><searchLink fieldCode="AU" term="%22South+PF%22">South PF</searchLink><br /><searchLink fieldCode="AU" term="%22Briggs+SD%22">Briggs SD</searchLink> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%222985121R%22">The Journal of biological chemistry</searchLink> [J Biol Chem] 2012 Jan 20; Vol. 287 (4), pp. 2652-65. <i>Date of Electronic Publication: </i>2011 Dec 06. – Name: TypePub Label: Publication Type Group: TypPub Data: Journal Article; Research Support, N.I.H., Extramural – Name: TitleSource Label: Journal Info Group: Src Data: <i>Publisher: </i><searchLink fieldCode="PB" term="%22Elsevier+Inc%2E+on+behalf+of+American+Society+for+Biochemistry+and+Molecular+Biology%22">Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology </searchLink><i>Country of Publication: </i>United States <i>NLM ID: </i>2985121R <i>Publication Model: </i>Print-Electronic <i>Cited Medium: </i>Internet <i>ISSN: </i>1083-351X (Electronic) <i>Linking ISSN: </i><searchLink fieldCode="IS" term="%2200219258%22">00219258 </searchLink><i>NLM ISO Abbreviation: </i>J Biol Chem <i>Subsets: </i>MEDLINE |
| PLink | https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=mdl&AN=22147691 |
| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1074/jbc.M111.280867 Languages: – Code: eng Text: English PhysicalDescription: Pagination: StartPage: 2652 Titles: – TitleFull: Charge-based interaction conserved within histone H3 lysine 4 (H3K4) methyltransferase complexes is needed for protein stability, histone methylation, and gene expression. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Mersman DP – PersonEntity: Name: NameFull: Du HN – PersonEntity: Name: NameFull: Fingerman IM – PersonEntity: Name: NameFull: South PF – PersonEntity: Name: NameFull: Briggs SD IsPartOfRelationships: – BibEntity: Dates: – D: 20 M: 01 Text: 2012 Jan 20 Type: published Y: 2012 Identifiers: – Type: issn-electronic Value: 1083-351X Numbering: – Type: volume Value: 287 – Type: issue Value: 4 Titles: – TitleFull: The Journal of biological chemistry Type: main |
| ResultId | 1 |
