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  Discovery-versus hypothesis-driven detection of protein-protein interactions and complexes

Bludau, I. (2021). Discovery-versus hypothesis-driven detection of protein-protein interactions and complexes. International Journal of Molecular Sciences, 22(9): 4450. doi:10.3390/ijms22094450.

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Genre: Zeitschriftenartikel

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externe Referenz:
https://www.mdpi.com/1422-0067/22/9/4450 (Verlagsversion)
Beschreibung:
Open Access
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Keine Angabe

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 Urheber:
Bludau, Isabell1, Autor           
Affiliations:
1Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              

Inhalt

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Schlagwörter: DATA-INDEPENDENT ACQUISITION; MASS-SPECTROMETRY; CROSS-LINKING; NETWORK; EXPLORATION; DYNAMICS; STRATEGY; WIDE; MAPBiochemistry & Molecular Biology; Chemistry; protein complexes; protein-protein interactions; interactomics; mass-spectrometry; targeted proteomics; data analysis; databases; systems biology;
 Zusammenfassung: Protein complexes are the main functional modules in the cell that coordinate and perform the vast majority of molecular functions. The main approaches to identify and quantify the interactome to date are based on mass spectrometry (MS). Here I summarize the benefits and limitations of different MS-based interactome screens, with a focus on untargeted interactome acquisition, such as co-fractionation MS. Specific emphasis is given to the discussion of discovery- versus hypothesis-driven data analysis concepts and their applicability to large, proteome-wide interactome screens. Hypothesis-driven analysis approaches, i.e., complex- or network-centric, are highlighted as promising strategies for comparative studies. While these approaches require prior information from public databases, also reviewed herein, the available wealth of interactomic data continuously increases, thereby providing more exhaustive information for future studies. Finally, guidance on the selection of interactome acquisition and analysis methods is provided to aid the reader in the design of protein-protein interaction studies.

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Sprache(n): eng - English
 Datum: 2021-04-21
 Publikationsstatus: Erschienen
 Seiten: 14
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Identifikatoren: ISI: 000650355300001
DOI: 10.3390/ijms22094450
 Art des Abschluß: -

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Titel: International Journal of Molecular Sciences
  Kurztitel : Int. J. Mol. Sci.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Basel, Switzerland : MDPI AG
Seiten: - Band / Heft: 22 (9) Artikelnummer: 4450 Start- / Endseite: - Identifikator: ISSN: 1422-0067
CoNE: https://pure.mpg.de/cone/journals/resource/1422-0067