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Strategies to enable large-scale proteomics for reproducible research |  Nature Communications
Strategies to enable large-scale proteomics for reproducible research | Nature Communications

IceR improves proteome coverage and data completeness in global and  single-cell proteomics | Nature Communications
IceR improves proteome coverage and data completeness in global and single-cell proteomics | Nature Communications

DIAMetAlyzer allows automated false-discovery rate-controlled analysis for  data-independent acquisition in metabolomics | Nature Communications
DIAMetAlyzer allows automated false-discovery rate-controlled analysis for data-independent acquisition in metabolomics | Nature Communications

Benchmarking of analysis strategies for data-independent acquisition  proteomics using a large-scale dataset comprising inter-patient  heterogeneity | Nature Communications
Benchmarking of analysis strategies for data-independent acquisition proteomics using a large-scale dataset comprising inter-patient heterogeneity | Nature Communications

Robust, reproducible and quantitative analysis of thousands of proteomes by  micro-flow LC–MS/MS | Nature Communications
Robust, reproducible and quantitative analysis of thousands of proteomes by micro-flow LC–MS/MS | Nature Communications

Deep representation features from DreamDIAXMBD improve the analysis of  data-independent acquisition proteomics | Communications Biology
Deep representation features from DreamDIAXMBD improve the analysis of data-independent acquisition proteomics | Communications Biology

Quantifying Plant Dynamic Proteomes by SWATH-based Mass Spectrometry:  Trends in Plant Science
Quantifying Plant Dynamic Proteomes by SWATH-based Mass Spectrometry: Trends in Plant Science

MaxDIA enables library-based and library-free data-independent acquisition  proteomics | Nature Biotechnology
MaxDIA enables library-based and library-free data-independent acquisition proteomics | Nature Biotechnology

DIA-Umpire: comprehensive computational framework for data-independent  acquisition proteomics | Nature Methods
DIA-Umpire: comprehensive computational framework for data-independent acquisition proteomics | Nature Methods

Mass-spectrometric exploration of proteome structure and function | Nature
Mass-spectrometric exploration of proteome structure and function | Nature

Prosit: proteome-wide prediction of peptide tandem mass spectra by deep  learning | Nature Methods
Prosit: proteome-wide prediction of peptide tandem mass spectra by deep learning | Nature Methods

Data-independent acquisition mass spectrometry (DIA-MS) for proteomic  applications in oncology - Molecular Omics (RSC Publishing)  DOI:10.1039/D0MO00072H
Data-independent acquisition mass spectrometry (DIA-MS) for proteomic applications in oncology - Molecular Omics (RSC Publishing) DOI:10.1039/D0MO00072H

Time-resolved in vivo ubiquitinome profiling by DIA-MS reveals USP7 targets  on a proteome-wide scale | Nature Communications
Time-resolved in vivo ubiquitinome profiling by DIA-MS reveals USP7 targets on a proteome-wide scale | Nature Communications

New Nature Communications publication by Mann & Theis Groups harnesses the  benefits of large-scale peptide
New Nature Communications publication by Mann & Theis Groups harnesses the benefits of large-scale peptide

Hybrid-DIA: intelligent data acquisition integrates targeted and discovery  proteomics to analyze phospho-signaling in single spheroids | Nature  Communications
Hybrid-DIA: intelligent data acquisition integrates targeted and discovery proteomics to analyze phospho-signaling in single spheroids | Nature Communications

Use of Hybrid Data-Dependent and -Independent Acquisition Spectral  Libraries Empowers Dual-Proteome Profiling | Journal of Proteome Research
Use of Hybrid Data-Dependent and -Independent Acquisition Spectral Libraries Empowers Dual-Proteome Profiling | Journal of Proteome Research

DIA-NN: neural networks and interference correction enable deep proteome  coverage in high throughput | Nature Methods
DIA-NN: neural networks and interference correction enable deep proteome coverage in high throughput | Nature Methods

Quantitative shotgun proteome analysis by direct infusion | Nature Methods
Quantitative shotgun proteome analysis by direct infusion | Nature Methods

Data-independent acquisition mass spectrometry (DIA-MS) for proteomic  applications in oncology - Molecular Omics (RSC Publishing)  DOI:10.1039/D0MO00072H
Data-independent acquisition mass spectrometry (DIA-MS) for proteomic applications in oncology - Molecular Omics (RSC Publishing) DOI:10.1039/D0MO00072H

DDA and DIA are the common data acquisition strategies in shotgun... |  Download Scientific Diagram
DDA and DIA are the common data acquisition strategies in shotgun... | Download Scientific Diagram

Deep Proteomics Using Two Dimensional Data Independent Acquisition Mass  Spectrometry | Analytical Chemistry
Deep Proteomics Using Two Dimensional Data Independent Acquisition Mass Spectrometry | Analytical Chemistry

Prioritized mass spectrometry increases the depth, sensitivity and data  completeness of single-cell proteomics | Nature Methods
Prioritized mass spectrometry increases the depth, sensitivity and data completeness of single-cell proteomics | Nature Methods

Chromatogram libraries improve peptide detection and quantification by data  independent acquisition mass spectrometry | Nature Communications
Chromatogram libraries improve peptide detection and quantification by data independent acquisition mass spectrometry | Nature Communications

Group-DIA: analyzing multiple data-independent acquisition mass spectrometry  data files | Nature Methods
Group-DIA: analyzing multiple data-independent acquisition mass spectrometry data files | Nature Methods

Frontiers | Recent Developments in Data Independent Acquisition (DIA) Mass  Spectrometry: Application of Quantitative Analysis of the Brain Proteome
Frontiers | Recent Developments in Data Independent Acquisition (DIA) Mass Spectrometry: Application of Quantitative Analysis of the Brain Proteome

Rapid and site-specific deep phosphoproteome profiling by data-independent  acquisition without the need for spectral libraries | Nature Communications
Rapid and site-specific deep phosphoproteome profiling by data-independent acquisition without the need for spectral libraries | Nature Communications