Proteome-wide analysis in Saccharomyces cerevisiae identifies several PHD fingers as novel direct and selective binding modules of histone H3 methylated at either lysine 4 or lysine 36.

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Title: Proteome-wide analysis in Saccharomyces cerevisiae identifies several PHD fingers as novel direct and selective binding modules of histone H3 methylated at either lysine 4 or lysine 36.
Authors: Shi X; Department of Biological Sciences, Stanford University, Stanford, California 94305, USA., Kachirskaia I, Walter KL, Kuo JH, Lake A, Davrazou F, Chan SM, Martin DG, Fingerman IM, Briggs SD, Howe L, Utz PJ, Kutateladze TG, Lugovskoy AA, Bedford MT, Gozani O
Source: The Journal of biological chemistry [J Biol Chem] 2007 Jan 26; Vol. 282 (4), pp. 2450-5. Date of Electronic Publication: 2006 Dec 01.
Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
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: Print ISSN: 0021-9258 (Print) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE
Database: MEDLINE Ultimate
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DbLabel: MEDLINE Ultimate
An: 17142463
AccessLevel: 2
PubType: Academic Journal
PubTypeId: academicJournal
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  Data: Proteome-wide analysis in Saccharomyces cerevisiae identifies several PHD fingers as novel direct and selective binding modules of histone H3 methylated at either lysine 4 or lysine 36.
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  Data: <searchLink fieldCode="AU" term="%22Shi+X%22">Shi X</searchLink>; Department of Biological Sciences, Stanford University, Stanford, California 94305, USA.<br /><searchLink fieldCode="AU" term="%22Kachirskaia+I%22">Kachirskaia I</searchLink><br /><searchLink fieldCode="AU" term="%22Walter+KL%22">Walter KL</searchLink><br /><searchLink fieldCode="AU" term="%22Kuo+JH%22">Kuo JH</searchLink><br /><searchLink fieldCode="AU" term="%22Lake+A%22">Lake A</searchLink><br /><searchLink fieldCode="AU" term="%22Davrazou+F%22">Davrazou F</searchLink><br /><searchLink fieldCode="AU" term="%22Chan+SM%22">Chan SM</searchLink><br /><searchLink fieldCode="AU" term="%22Martin+DG%22">Martin DG</searchLink><br /><searchLink fieldCode="AU" term="%22Fingerman+IM%22">Fingerman IM</searchLink><br /><searchLink fieldCode="AU" term="%22Briggs+SD%22">Briggs SD</searchLink><br /><searchLink fieldCode="AU" term="%22Howe+L%22">Howe L</searchLink><br /><searchLink fieldCode="AU" term="%22Utz+PJ%22">Utz PJ</searchLink><br /><searchLink fieldCode="AU" term="%22Kutateladze+TG%22">Kutateladze TG</searchLink><br /><searchLink fieldCode="AU" term="%22Lugovskoy+AA%22">Lugovskoy AA</searchLink><br /><searchLink fieldCode="AU" term="%22Bedford+MT%22">Bedford MT</searchLink><br /><searchLink fieldCode="AU" term="%22Gozani+O%22">Gozani O</searchLink>
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  Data: <searchLink fieldCode="JN" term="%222985121R%22">The Journal of biological chemistry</searchLink> [J Biol Chem] 2007 Jan 26; Vol. 282 (4), pp. 2450-5. <i>Date of Electronic Publication: </i>2006 Dec 01.
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  Data: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
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  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>Print <i>ISSN: </i>0021-9258 (Print) <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=17142463
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      – Type: doi
        Value: 10.1074/jbc.C600286200
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      – Code: eng
        Text: English
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        StartPage: 2450
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      – TitleFull: Proteome-wide analysis in Saccharomyces cerevisiae identifies several PHD fingers as novel direct and selective binding modules of histone H3 methylated at either lysine 4 or lysine 36.
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            – D: 26
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              Text: 2007 Jan 26
              Type: published
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              Value: 282
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              Value: 4
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