FLASHIda enables intelligent data acquisition for top–down proteomics to boost proteoform identification counts

zu Verbundenen Objekten

Standort
Deutsche Nationalbibliothek Frankfurt am Main
ISSN
2041-1723
Umfang
Online-Ressource
Sprache
Englisch
Anmerkungen
online resource.

Erschienen in
FLASHIda enables intelligent data acquisition for top–down proteomics to boost proteoform identification counts ; volume:13 ; number:1 ; day:29 ; month:7 ; year:2022 ; pages:1-12 ; date:12.2022
Nature Communications ; 13, Heft 1 (29.7.2022), 1-12, 12.2022

Urheber
Jeong, Kyowon
Babović, Maša
Gorshkov, Vladimir
Kim, Jihyung
Jensen, Ole N.
Kohlbacher, Oliver
Beteiligte Personen und Organisationen
SpringerLink (Online service)

DOI
10.1038/s41467-022-31922-z
URN
urn:nbn:de:101:1-2022101517071420948875
Rechteinformation
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
Letzte Aktualisierung
15.08.2025, 07:37 MESZ

Datenpartner

Dieses Objekt wird bereitgestellt von:
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Original beim Datenpartner anzeigen

Beteiligte

  • Jeong, Kyowon
  • Babović, Maša
  • Gorshkov, Vladimir
  • Kim, Jihyung
  • Jensen, Ole N.
  • Kohlbacher, Oliver
  • SpringerLink (Online service)

Ähnliche Objekte (12)

Multidimensional separations in top–down proteomics

Multidimensional separations in top–down proteomics

The need for open and FAIR data in top‐down proteomics

The need for open and FAIR data in top‐down proteomics

The need for open and FAIR data in top‐down proteomics

The need for open and FAIR data in top‐down proteomics

quantms: a cloud-based pipeline for quantitative proteomics enables the reanalysis of public proteomics data

quantms: a cloud-based pipeline for quantitative proteomics enables the reanalysis of public proteomics data

EXCRETE workflow enables deep proteomics of the microbial extracellular environment

EXCRETE workflow enables deep proteomics of the microbial extracellular environment

Spectral averaging with outlier rejection algorithms to increase identifications in top‐down proteomics

Spectral averaging with outlier rejection algorithms to increase identifications in top‐down proteomics

Influence of different sample preparation approaches on proteoform identification by top-down proteomics

Influence of different sample preparation approaches on proteoform identification by top-down proteomics

Methodische Ansätze zur Analyse posttranslationaler Modifikationen mittels Top-Down und Bottom-Up Proteomics

Methodische Ansätze zur Analyse posttranslationaler Modifikationen mittels Top-Down und Bottom-Up Proteomics

Large‐scale top‐down proteomics of the Arabidopsis thaliana leaf and chloroplast proteomes

Large‐scale top‐down proteomics of the Arabidopsis thaliana leaf and chloroplast proteomes

Differential ultracentrifugation enables deep plasma proteomics through enrichment of extracellular vesicles

Differential ultracentrifugation enables deep plasma proteomics through enrichment of extracellular vesicles

Infrared Multiphoton Dissociation Enables Top‐Down Characterization of Membrane Protein Complexes and G Protein‐Coupled Receptors

Infrared Multiphoton Dissociation Enables Top‐Down Characterization of Membrane Protein Complexes and G Protein‐Coupled Receptors

Infrared Multiphoton Dissociation Enables Top‐Down Characterization of Membrane Protein Complexes and G Protein‐Coupled Receptors

Infrared Multiphoton Dissociation Enables Top‐Down Characterization of Membrane Protein Complexes and G Protein‐Coupled Receptors

Verbundene Objekte