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Barrikade Väterlich Werdegang dia mass spectrometry nature Handschrift Vermittler Gehalt
Robust, reproducible and quantitative analysis of thousands of proteomes by micro-flow LC–MS/MS | Nature Communications
The Human Immunopeptidome Project: A Roadmap to Predict and Treat Immune Diseases | Molecular & Cellular Proteomics
Quantitative Proteome Landscape of the NCI-60 Cancer Cell Lines - ScienceDirect
Data-Independent Acquisition: A Superior Technique in Mass Spectrometry? | Technology Networks
Data‐independent acquisition‐based SWATH‐MS for quantitative proteomics: a tutorial | Molecular Systems Biology
Chromatogram libraries improve peptide detection and quantification by data independent acquisition mass spectrometry | Nature Communications
Discovering cellular protein‐protein interactions: Technological strategies and opportunities - Titeca - 2019 - Mass Spectrometry Reviews - Wiley Online Library
Nature Methods on Twitter: "Avant-garde: a tool for refining DIA-mass spectrometry data. @JaffeLab https://t.co/zIWJ9PUYiz… "
Group-DIA: analyzing multiple data-independent acquisition mass spectrometry data files | Nature Methods
Hybrid Spectral Library Combining DIA-MS Data and a Targeted Virtual Library Substantially Deepens the Proteome Coverage - ScienceDirect
DIA mass spectrometry | Nature Methods
Prosit: proteome-wide prediction of peptide tandem mass spectra by deep learning | Nature Methods
SWATH analysis - Why an advantage in mass spectrometry?
Data-independent acquisition mass spectrometry (DIA-MS) for proteomic applications in oncology - Molecular Omics (RSC Publishing) DOI:10.1039/D0MO00072H
PulseDIA: in-depth data independent acquisition mass spectrometry using enhanced gas phase fractionation | bioRxiv
PulseDIA: in-depth data independent acquisition mass spectrometry using enhanced gas phase fractionation | bioRxiv
DDIA: data dependent-independent acquisition proteomics - DDA and DIA in a single LC-MS/MS run | bioRxiv
Mass-spectrometric exploration of proteome structure and function | Nature
Data-independent acquisition mass spectrometry (DIA-MS) for proteomic applications in oncology - Molecular Omics (RSC Publishing) DOI:10.1039/D0MO00072H
Optimization of Experimental Parameters in Data-Independent Mass Spectrometry Significantly Increases Depth and Reproducibility
Assessing the Relationship Between Mass Window Width and Retention Time Scheduling on Protein Coverage for Data-Independent Acquisition | SpringerLink
DIA mass spectrometry | Nature Methods
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