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Jürgen Cox

Researcher at Max Planck Society

Publications -  125
Citations -  28676

Jürgen Cox is an academic researcher from Max Planck Society. The author has contributed to research in topics: Proteomics & Proteome. The author has an hindex of 50, co-authored 117 publications receiving 22505 citations. Previous affiliations of Jürgen Cox include RWTH Aachen University & University of Bergen.

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The Perseus computational platform for comprehensive analysis of (prote)omics data.

TL;DR: The Perseus software platform was developed to support biological and biomedical researchers in interpreting protein quantification, interaction and post-translational modification data and it is anticipated that Perseus's arsenal of algorithms and its intuitive usability will empower interdisciplinary analysis of complex large data sets.
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Andromeda: a peptide search engine integrated into the MaxQuant environment

TL;DR: A novel peptide search engine using a probabilistic scoring model that can handle data with arbitrarily high fragment mass accuracy, is able to assign and score complex patterns of post-translational modifications, and accommodates extremely large databases.
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Accurate Proteome-wide Label-free Quantification by Delayed Normalization and Maximal Peptide Ratio Extraction, Termed MaxLFQ

TL;DR: A new intensity determination and normalization procedure called MaxLFQ is developed that is fully compatible with any peptide or protein separation prior to LC-MS analysis, which accurately detects the mixing ratio over the entire protein expression range, with greater precision for abundant proteins.
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Quantitative Phosphoproteomics Reveals Widespread Full Phosphorylation Site Occupancy During Mitosis

TL;DR: High-resolution mass spectrometry–based proteomics was applied to investigate the proteome and phosphoproteome of the human cell cycle on a global scale and quantified 6027 proteins and 20,443 unique phosphorylation sites and their dynamics, finding that nuclear proteins and proteins involved in regulating metabolic processes have high phosphorylated site occupancy in mitosis, suggesting that these proteins may be inactivated by phosphorylate in mitotic cells.
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Comprehensive mass-spectrometry-based proteome quantification of haploid versus diploid yeast.

TL;DR: Comparison of protein levels of essentially all endogenous proteins in haploid yeast cells to their diploid counterparts spans more than four orders of magnitude in protein abundance with no discrimination against membrane or low level regulatory proteins.