PhosphoPep--a phosphoproteome resource for systems biology research in Drosophila Kc167 cells.

PhosphoPep--a phosphoproteome resource for systems biology research in Drosophila Kc167 cells. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

PhosphoPep--a phosphoproteome resource for systems biology research in Drosophila Kc167 cells. Abstract Text:

Bernd Bodenmiller,Johan Malmstrom,Bertran Gerrits,David Campbell,Henry Lam,Alexander Schmidt,Oliver Rinner,Lukas N Mueller,Paul T Shannon,Patrick G Pedrioli,Christian Panse,Hoo-Keun Lee,Ralph Schlapbach,Ruedi Aebersold,

The ability to analyze and understand the mechanisms by which cells process information is a key question of systems biology research. Such mechanisms critically depend on reversible phosphorylation of cellular proteins, a process that is catalyzed by protein kinases and phosphatases. Here, we present PhosphoPep, a database containing more than 10 000 unique high-confidence phosphorylation sites mapping to nearly 3500 gene models and 4600 distinct phosphoproteins of the Drosophila melanogaster Kc167 cell line. This constitutes the most comprehensive phosphorylation map of any single source to date. To enhance the utility of PhosphoPep, we also provide an array of software tools that allow users to browse through phosphorylation sites on single proteins or pathways, to easily integrate the data with other, external data types such as protein-protein interactions and to search the database via spectral matching. Finally, all data can be readily exported, for example, for targeted proteomics approaches and the data thus generated can be again validated using PhosphoPep, supporting iterative cycles of experimentation and analysis that are typical for systems biology research.

PhosphoPep--a phosphoproteome resource for systems biology research in Drosophila Kc167 cells. Publishing Authors By Initials

B Bodenmiller,J Malmstrom,B Gerrits,D Campbell,H Lam,A Schmidt,O Rinner,LN Mueller,PT Shannon,PG Pedrioli,C Panse,HK Lee,R Schlapbach,R Aebersold,

For similar abstracts research abstracts see: abstracts research

PUBMED ID PMID:

MEDLINE DATE:

PhosphoPep--a phosphoproteome resource for systems biology research in Drosophila Kc167 cells. Journal Published:

PUBLICATION TYPE: Review

Journal: Molecular systems biology

VOLUME: 3

Page Numbers: 139

Journal Abbreviation: Mol. Syst. Biol.

ISSN: 1744-4292

DAY: 16

MONTH: 10

YEAR: 2007

PhosphoPep--a phosphoproteome resource for systems biology research in Drosophila Kc167 cells. Information

Number of References: 59

LANGUAGE: eng

NlmUniqueID: 101235389

PhosphoPep--a phosphoproteome resource for systems biology research in Drosophila Kc167 cells. Keywords Mesh Terms:

KEYWORDS:

MESH TERMS:

Chemical & Substance for Abstract: PhosphoPep--a phosphoproteome resource for systems biology research in Drosophila Kc167 cells. Information

Substance Name:

Registry Number:

Grant and Affiliation Information for PhosphoPep--a phosphoproteome resource for systems biology research in Drosophila Kc167 cells.

AFFILIATION: Institute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland.

Country: England

AGENCY: United States NHLBI

GRANT: N01-HV-28179

ACRONYM: HV

MEDLINETA: Mol Syst Biol

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

PhosphoPep--a phosphoproteome resource for systems biology research in Drosophila Kc167 cells Related Publications

• A high-quality catalog of the Drosophila melanogaster proteome.
• A statistical method for chromatographic alignment of LC-MS data.
• Advances in proteomic workflows for systems biology.
• Analysis of protein complexes using mass spectrometry.
• Analysis of the Saccharomyces cerevisiae proteome with PeptideAtlas.
• Building consensus spectral libraries for peptide identification in proteomics.
• Chemical synthesis, purification, and characterization of two inflammatory proteins, neutrophil activating peptide 1 (interleukin-8) and neutrophil activating peptide.
• Comparative evaluation of current peptide production platforms used in absolute quantification in proteomics.
• Development and validation of a spectral library searching method for peptide identification from MS/MS.
• High-accuracy proteome maps of human body fluids.
• Identification of cross-linked peptides from large sequence databases.
• Isotopes for medicine.
• Mass spectrometric detection of tissue proteins in plasma.
• Optimized peptide separation and identification for mass spectrometry based proteomics via free-flow electrophoresis.
• PeptideAtlas: a resource for target selection for emerging targeted proteomics workflows.
• PhosphoPep--a phosphoproteome resource for systems biology research in Drosophila Kc167 cells.
• Prevention of radiochemotherapy-induced toxicity with amifostine in patients with malignant orbital tumors involving the lacrimal gland: a pilot study.
• Progress against cancer with radioisotopes.
• Quantitative proteomic analysis of protein complexes: concurrent identification of interactors and their state of phosphorylation.
• Quantitative proteomic analysis of the budding yeast cell cycle using acid-cleavable isotope-coded affinity tag reagents.
• Quantitative proteomic analysis to profile dynamic changes in the spatial distribution of cellular proteins.
• Reproducible isolation of distinct, overlapping segments of the phosphoproteome.
• Selected reaction monitoring for quantitative proteomics: a tutorial.
• Targeted quantitative analysis of Streptococcus pyogenes virulence factors by multiple reaction monitoring.
• The role of the Atomic Energy Commission in the future work with isotopes.
• UniPep--a database for human N-linked glycosites: a resource for biomarker discovery.
• Using stable isotope tagging and mass spectrometry to characterize protein complexes and to detect changes in their composition.
• [AIDS--care--sexuality]
• [Angiogenesis as prognostic factor in malignant tumors]
• [Radiotherapy of the prostate gland--old wine in a new bottle?]