Clues to quality of journals
Open Access Policy of Helmholtz Association 2016
CC Licencences
Publication Metrics
Home
Deutsch
New EVA Application
Advanced Search
Browse by ...
Publication overview
Statistics (last 5 years)
OA Publications
Submit Publication
Import publication from...
Report missing publication
Contact persons
Help
Text
Endnote (RIS)
BibTeX
Publ. Version/Full Text
DOI
PMC
 |
Open Access Gold |
as soon as is submitted to ZB.
Proteome-wide protein interaction measurements of bacterial proteins of unknown function.
Proc. Natl. Acad. Sci. U.S.A. 110, 477-482 (2013)
Despite the enormous proliferation of bacterial genome data, surprisingly persistent collections of bacterial proteins have resisted functional annotation. In a typical genome, roughly 30% of genes have no assigned function. Many of these proteins are conserved across a large number of bacterial genomes. To assign a putative function to these conserved proteins of unknown function, we created a physical interaction map by measuring biophysical interaction of these proteins. Binary protein--protein interactions in the model organism Streptococcus pneumoniae (TIGR4) are measured with a microfluidic high-throughput assay technology. In some cases, informatic analysis was used to restrict the space of potential binding partners. In other cases, we performed in vitro proteome-wide interaction screens. We were able to assign putative functions to 50 conserved proteins of unknown function that we studied with this approach.
Impact Factor
Scopus SNIP
Scopus
Cited By
Cited By
Altmetric
0.000
2.641
33
Annotations
Special Publikation
Hide on homepage
Publication type
Article: Journal article
Document type
Scientific Article
Language
Publication Year
2013
HGF-reported in Year
2013
ISSN (print) / ISBN
0027-8424
e-ISSN
1091-6490
Quellenangaben
Volume: 110,
Issue: 2,
Pages: 477-482
Publisher
National Academy of Sciences
Reviewing status
Peer reviewed
Institute(s)
Helmholtz Pioneer Campus (HPC)
PubMed ID
23267104
Erfassungsdatum
2019-01-17