From protein interactions to functional annotation: graph alignment in Herpes
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F08%3A00337896" target="_blank" >RIV/68378050:_____/08:00337896 - isvavai.cz</a>
Výsledek na webu
—
DOI - Digital Object Identifier
—
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
From protein interactions to functional annotation: graph alignment in Herpes
Popis výsledku v původním jazyce
Sequence alignment is a prolific basis of functional annotation, but remains a challenging problem in the twilight zone of high sequence divergence or short gene length. We demonstrate how information on gene interactions can resolve ambiguous sequence alignments. We compare two distant Herpes viruses by constructing a graph alignment based jointly on the similarity of their protein interaction networks and on sequence similarity. This hybrid method provides functional associations between proteins of the two organisms that cannot be obtained from sequence or interaction data alone. We find proteins where interaction similarity and sequence similarity are individually weak but together provide evidence of orthology. There are also proteins with high interaction similarity and no detectable sequence similarity, providing evidence of functional association beyond sequence homology. The predictions derived from our alignment are consistent with genomic position and gene expression data.
Název v anglickém jazyce
From protein interactions to functional annotation: graph alignment in Herpes
Popis výsledku anglicky
Sequence alignment is a prolific basis of functional annotation, but remains a challenging problem in the twilight zone of high sequence divergence or short gene length. We demonstrate how information on gene interactions can resolve ambiguous sequence alignments. We compare two distant Herpes viruses by constructing a graph alignment based jointly on the similarity of their protein interaction networks and on sequence similarity. This hybrid method provides functional associations between proteins of the two organisms that cannot be obtained from sequence or interaction data alone. We find proteins where interaction similarity and sequence similarity are individually weak but together provide evidence of orthology. There are also proteins with high interaction similarity and no detectable sequence similarity, providing evidence of functional association beyond sequence homology. The predictions derived from our alignment are consistent with genomic position and gene expression data.
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
EB - Genetika a molekulární biologie
OECD FORD obor
—
Návaznosti výsledku
Projekt
—
Návaznosti
Z - Vyzkumny zamer (s odkazem do CEZ)
Ostatní
Rok uplatnění
2008
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
BMC Sytems Biology
ISSN
1752-0509
e-ISSN
—
Svazek periodika
2
Číslo periodika v rámci svazku
90
Stát vydavatele periodika
GB - Spojené království Velké Británie a Severního Irska
Počet stran výsledku
10
Strana od-do
—
Kód UT WoS článku
000262308800001
EID výsledku v databázi Scopus
—