The exosome-binding factors Rrp6 and Rrp47 form a composite surface for recruiting the Mtr4 helicase.

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Title: The exosome-binding factors Rrp6 and Rrp47 form a composite surface for recruiting the Mtr4 helicase.
Authors: Schuch B; Structural Cell Biology Department, Max Planck Institute of Biochemistry, Martinsried, Germany., Feigenbutz M; Molecular Biology and Biotechnology Department, The University of Sheffield, Sheffield, UK., Makino DL; Structural Cell Biology Department, Max Planck Institute of Biochemistry, Martinsried, Germany., Falk S; Structural Cell Biology Department, Max Planck Institute of Biochemistry, Martinsried, Germany., Basquin C; Structural Cell Biology Department, Max Planck Institute of Biochemistry, Martinsried, Germany., Mitchell P; Molecular Biology and Biotechnology Department, The University of Sheffield, Sheffield, UK p.j.mitchell@sheffield.ac.uk conti@biochem.mpg.de., Conti E; Structural Cell Biology Department, Max Planck Institute of Biochemistry, Martinsried, Germany p.j.mitchell@sheffield.ac.uk conti@biochem.mpg.de.
Source: The EMBO journal [EMBO J] 2014 Dec 01; Vol. 33 (23), pp. 2829-46. Date of Electronic Publication: 2014 Oct 15.
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
Journal Info: Publisher: Nature Publishing Group Country of Publication: England NLM ID: 8208664 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1460-2075 (Electronic) Linking ISSN: 02614189 NLM ISO Abbreviation: EMBO J Subsets: MEDLINE
Database: MEDLINE Ultimate
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  Data: The exosome-binding factors Rrp6 and Rrp47 form a composite surface for recruiting the Mtr4 helicase.
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  Data: <searchLink fieldCode="AU" term="%22Schuch+B%22">Schuch B</searchLink>; Structural Cell Biology Department, Max Planck Institute of Biochemistry, Martinsried, Germany.<br /><searchLink fieldCode="AU" term="%22Feigenbutz+M%22">Feigenbutz M</searchLink>; Molecular Biology and Biotechnology Department, The University of Sheffield, Sheffield, UK.<br /><searchLink fieldCode="AU" term="%22Makino+DL%22">Makino DL</searchLink>; Structural Cell Biology Department, Max Planck Institute of Biochemistry, Martinsried, Germany.<br /><searchLink fieldCode="AU" term="%22Falk+S%22">Falk S</searchLink>; Structural Cell Biology Department, Max Planck Institute of Biochemistry, Martinsried, Germany.<br /><searchLink fieldCode="AU" term="%22Basquin+C%22">Basquin C</searchLink>; Structural Cell Biology Department, Max Planck Institute of Biochemistry, Martinsried, Germany.<br /><searchLink fieldCode="AU" term="%22Mitchell+P%22">Mitchell P</searchLink>; Molecular Biology and Biotechnology Department, The University of Sheffield, Sheffield, UK p.j.mitchell@sheffield.ac.uk conti@biochem.mpg.de.<br /><searchLink fieldCode="AU" term="%22Conti+E%22">Conti E</searchLink>; Structural Cell Biology Department, Max Planck Institute of Biochemistry, Martinsried, Germany p.j.mitchell@sheffield.ac.uk conti@biochem.mpg.de.
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  Data: <searchLink fieldCode="JN" term="%228208664%22">The EMBO journal</searchLink> [EMBO J] 2014 Dec 01; Vol. 33 (23), pp. 2829-46. <i>Date of Electronic Publication: </i>2014 Oct 15.
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        Value: 10.15252/embj.201488757
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      – TitleFull: The exosome-binding factors Rrp6 and Rrp47 form a composite surface for recruiting the Mtr4 helicase.
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