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Showing 1–7 of 7 results
Advanced filters: Author: Martin Frejno Clear advanced filters
  • CHIMERYS is a spectrum-centric and data acquisition method-agnostic algorithm for the analysis of MS2 spectra. It is capable of deconvoluting any MS2 spectrum, regardless of whether it was acquired by DDA, DIA or PRM, thus unifying the analysis of bottom-up proteomics data.

    • Martin Frejno
    • Michelle T. Berger
    • Mathias Wilhelm
    ResearchOpen Access
    Nature Methods
    Volume: 22, P: 1017-1027
  • Kinases regulate cellular processes, making their study essential for understanding cellular function and disease. Here, the authors evaluate methods to infer kinase activity from phosphoproteomics data and provide a toolkit to evaluate future methods.

    • Sophia Müller-Dott
    • Eric J. Jaehnig
    • Julio Saez-Rodriguez
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-21
  • Proteome activity has a major role in cancer progression and response to drugs. Here, the authors use comprehensive proteomic and phosphoproteomic data, in conjunction with drug-sensitivity screens, to generate a community resource consisting of landscapes of pathway and kinase activity across different cell lines

    • Martin Frejno
    • Chen Meng
    • Bernhard Kuster
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-12
  • A quantitative atlas of the transcriptomes, proteomes and phosphoproteomes of 30 tissues of the model plant Arabidopsis thaliana provides a valuable resource for plant research.

    • Julia Mergner
    • Martin Frejno
    • Bernhard Kuster
    Research
    Nature
    Volume: 579, P: 409-414
  • This work presents a quantitative draft of the mouse proteome and phosphoproteome constructed from 41 healthy tissues covering 15 major anatomical systems and 66 cell lines.

    • Piero Giansanti
    • Patroklos Samaras
    • Bernhard Kuster
    Research
    Nature Methods
    Volume: 19, P: 803-811
  • A mass-spectrometry-based draft of the human proteome and a public database for analysis of proteome data are presented; assembled information is used to estimate the size of the protein-coding genome, to identify organ-specific proteins, proteins predicting drug resistance or sensitivity, and many translated long intergenic non-coding RNAs, and to reveal conserved control of protein abundance.

    • Mathias Wilhelm
    • Judith Schlegl
    • Bernhard Kuster
    Research
    Nature
    Volume: 509, P: 582-587