Proteomics

Dataset Information

0

Hs_spindle_phospho_silac


ABSTRACT: Hs_spindle_phospho_silac

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Others

SUBMITTER: Malik R, Lenobel R, Santamaria A, Ries A, Nigg EA, K�rner R 

PROVIDER: PAe003755 | PeptideAtlas | 2009-12-31

REPOSITORIES: PeptideAtlas

Dataset's files

Source:
Action DRS
PAe003755_7600_tandem.params Other
PAe003755_README Other
PAe003755_Search_Results_7600_201211210922.properties Other
PAe003755_Search_Results_7600_201211210922.tar.gz Other
PAe003755_mzML_201211210857.properties Other
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Publications

Quantitative analysis of the human spindle phosphoproteome at distinct mitotic stages.

Malik Rainer R   Lenobel René R   Santamaria Anna A   Ries Albert A   Nigg Erich A EA   Körner Roman R  

Journal of proteome research 20091001 10


During mitosis, phosphorylation of spindle associated proteins is a key regulatory mechanism for spindle formation, mitotic progression, and cytokinesis. In the recent past, mass spectrometry has been applied successfully to identify spindle proteomes and phosphoproteomes, but did not address their dynamics. Here, we present a quantitative comparison of spindle phosphoproteomes prepared from different mitotic stages. In total, we report the identification and SILAC based relative quantitation of  ...[more]

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