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  Mass spectrometry for serine ADP-ribosylation? Think o-glycosylation!

Bonfiglio, J. J., Colby, T., & Matić, I. (2017). Mass spectrometry for serine ADP-ribosylation? Think o-glycosylation! Nucleic Acids Res, 45(11), 6259-6264. doi:10.1093/nar/gkx446.

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https://www.ncbi.nlm.nih.gov/pubmed/28520971 (beliebiger Volltext)
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 Urheber:
Bonfiglio, J. J.1, Autor           
Colby, T.2, Autor           
Matić, I.1, Autor           
Affiliations:
1Matic – ADP-ribosylation in DNA Repair and Ageing, Research Groups, Max Planck Institute for Biology of Ageing, Max Planck Society, ou_1942299              
2Proteomics, Core Facilities, Max Planck Institute for Biology of Ageing, Max Planck Society, ou_1942305              

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 Zusammenfassung: Protein ADP-ribosylation (ADPr), a biologically and clinically important post-translational modification, exerts its functions by targeting a variety of different amino acids. Its repertoire recently expanded to include serine ADPr, which is emerging as an important and widespread signal in the DNA damage response. Chemically, serine ADPr (and more generally o-glycosidic ADPr) is a form of o-glycosylation, and its extreme lability renders it practically invisible to standard mass spectrometry approaches, often leading to erroneous localizations. The knowledge from the mature field of o-glycosation and our own initial difficulties with mass spectrometric analyzes of serine ADPr suggest how to avoid these misidentifications and fully explore the scope of o-glycosidic ADPr in DNA damage response and beyond.

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 Datum: 2017
 Publikationsstatus: Erschienen
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 Identifikatoren: Anderer: 28520971
DOI: 10.1093/nar/gkx446
ISSN: 1362-4962 (Electronic)0305-1048 (Linking)
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Titel: Nucleic Acids Res
Genre der Quelle: Zeitschrift
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Seiten: - Band / Heft: 45 (11) Artikelnummer: - Start- / Endseite: 6259 - 6264 Identifikator: -