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

to related objects

Location: Deutsche Nationalbibliothek Frankfurt am Main

ISSN: 2041-1723

Extent: Online-Ressource

Language: Englisch

Notes: online resource.

Bibliographic citation: 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

Creator: Jeong, Kyowon
Babović, Maša
Gorshkov, Vladimir
Kim, Jihyung
Jensen, Ole N.
Kohlbacher, Oliver

Contributor: SpringerLink (Online service)

DOI: 10.1038/s41467-022-31922-z

URN: urn:nbn:de:101:1-2022101517071420948875

Rights: Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 15.08.2025, 7:37 AM CEST

Data provider

This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.

Show original at data provider

Associated

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

Other Objects (12)

Multidimensional separations 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

EXCRETE workflow enables deep proteomics of the microbial extracellular environment

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

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

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

Multidimensional separations 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

EXCRETE workflow enables deep proteomics of the microbial extracellular environment

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

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

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

Multidimensional separations 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

EXCRETE workflow enables deep proteomics of the microbial extracellular environment

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

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

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

Cultural heritage institutions wishing to register will find more information here.

Fields marked * need to be filled in.

Username*

Please enter your username

Email*

Please enter your email address

Please do not fill this field

First name

Last name

Password*

Please enter your password

Confirm password*

Please enter the same password

I have read the terms of use and the privacy policy for the collection of personal data and accept them. *

This field is required.

I would like to subscribe to the newsletter of the Deutsche Digitale Bibliothek. See newsletter subscription info.

Account created

Your "My DDB" account has been successfully created. Before you can log in to your account, you must click the confirmation link in the message we just sent to the email address you provided.

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

Object Details

References and Relationships

Contributors, Places and Time

Further information

Data provider

Associated

Other Objects (12)

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

Related objects

Reset password