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  False discovery rate estimation for cross-linked peptides identified by mass spectrometry

Walzthoeni, T., Claassen, M., Leitner, A., Herzog, F., Bohn, S., Förster, F., et al. (2012). False discovery rate estimation for cross-linked peptides identified by mass spectrometry. NATURE METHODS, 9(9), 901-903. doi:10.1038/nmeth.2103.

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 Creators:
Walzthoeni, Thomas1, Author
Claassen, Manfred1, Author
Leitner, Alexander1, Author
Herzog, Franz1, Author
Bohn, Stefan2, Author           
Förster, Friedrich3, Author           
Beck, Martin1, Author
Aebersold, Ruedi1, Author
Affiliations:
1external, ou_persistent22              
2Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              
3Förster, Friedrich / Modeling of Protein Complexes, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565148              

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Free keywords: PROTEIN STRUCTURES; 26S PROTEASOME; LINKING; BIOINFORMATICS; ARCHITECTURE; COMPLEXES; STRATEGY
 Abstract: The mass spectrometric identification of chemically cross-linked peptides (CXMS) specifies spatial restraints of protein complexes; these values complement data obtained from common structure-determination techniques. Generic methods for determining false discovery rates of cross-linked peptide assignments are currently lacking, thus making data sets from CXMS studies inherently incomparable. Here we describe an automated target-decoy strategy and the software tool xProphet, which solve this problem for large multicomponent protein complexes.

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Language(s): eng - English
 Dates: 2012-09
 Publication Status: Issued
 Pages: 3
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000308497800022
DOI: 10.1038/nmeth.2103
 Degree: -

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Title: NATURE METHODS
Source Genre: Journal
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Publ. Info: MACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLAND : NATURE PUBLISHING GROUP
Pages: - Volume / Issue: 9 (9) Sequence Number: - Start / End Page: 901 - 903 Identifier: ISSN: 1548-7091