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Hs_Ovary_chymotrypsin

ABSTRACT: Hs_Ovary_chymotrypsin

REANALYSIS of: PXD000865

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Female Reproductive System

SUBMITTER: Wilhelm et al.

PROVIDER: PAe004961 | PeptideAtlas | 2014-12-31

REPOSITORIES: PeptideAtlas

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Publications

Mass-spectrometry-based draft of the human proteome.

Wilhelm Mathias M Schlegl Judith J Hahne Hannes H Gholami Amin Moghaddas AM Lieberenz Marcus M Savitski Mikhail M MM Ziegler Emanuel E Butzmann Lars L Gessulat Siegfried S Marx Harald H Mathieson Toby T Lemeer Simone S Schnatbaum Karsten K Reimer Ulf U Wenschuh Holger H Mollenhauer Martin M Slotta-Huspenina Julia J Boese Joos-Hendrik JH Bantscheff Marcus M Gerstmair Anja A Faerber Franz F Kuster Bernhard B

Nature 20140501 7502

Proteomes are characterized by large protein-abundance differences, cell-type- and time-dependent expression patterns and post-translational modifications, all of which carry biological information that is not accessible by genomics or transcriptomics. Here we present a mass-spectrometry-based draft of the human proteome and a public, high-performance, in-memory database for real-time analysis of terabytes of big data, called ProteomicsDB. The information assembled from human tissues, cell lines ...[more]

PMID: 24870543

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