PRIDEViewer: A novel user‐friendly interface to visualize PRIDE XML files
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Summary
PRIDEViewer is a novel Java‐based application that presents the information available in a PRIDE XML file in a user‐friendly manner, facilitating the interaction among end users as well as the understanding and evaluation of the compiled information.
- Type
- article
- Published
- 2011-01-01
- Cited by
- 8
- References
- 12
- OpenAlex
- https://openalex.org/W2010002969
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:38793533
Keywords
XML, Computer science, World Wide Web, Standardization, Interface (matter)
References
- Mass Spectrometer Output File Format mzML
- Proposal for a common nomenclature for sequence ions in mass spectra of peptides.
- Probability-based protein identification by searching sequence databases using mass spectrometry data
- The Proteomics Standards Initiative
- Letter from the Editors
- PRIDE: a public repository of protein and peptide identifications for the proteomics community
- PRIDE Converter: making proteomics data-sharing easy
- PRIDE: The proteomics identifications database
- The Proteomics Identifications database: 2010 update
- Proteomic data exchange and storage: the need for common standards and public repositories.
- Binding of RHOA G17V to p300 enhances its HAT activity: a new mechanism of epigenetic deregulation in TFH lymphoma
Cited by
- Access Guide to Human Proteinpedia
- ProteomeXchange provides globally co-ordinated proteomics data submission and dissemination
- A DIGE study on the effects of salbutamol on the rat muscle proteome - an exemplar of best practice for data sharing in proteomics
- PRIDE Inspector: a tool to visualize and validate MS proteomics data
- A guide for integration of proteomic data standards into laboratory workflows
- The ProteoRed MIAPE web toolkit: A User-friendly Framework to Connect and Share Proteomics Standards*
- Procesamiento automatizado de datos proteómicos: desde la espectrometría de masas al conocimiento biológico
- Pillar array columns for peptide separations in nanoscale reversed-phase chromatography.
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