EconPapers    
Economics at your fingertips  
 

Capturing variation impact on molecular interactions in the IMEx Consortium mutations data set

N. del-Toro, M. Duesbury, M. Koch, L. Perfetto, A. Shrivastava, D. Ochoa, O. Wagih, J. Piñero, M. Kotlyar, C. Pastrello, P. Beltrao, L. I. Furlong, I. Jurisica, H. Hermjakob, S. Orchard and P. Porras ()
Additional contact information
N. del-Toro: European Molecular Biology Laboratory
M. Duesbury: European Molecular Biology Laboratory
M. Koch: European Molecular Biology Laboratory
L. Perfetto: European Molecular Biology Laboratory
A. Shrivastava: European Molecular Biology Laboratory
D. Ochoa: European Molecular Biology Laboratory
O. Wagih: European Molecular Biology Laboratory
J. Piñero: Universitat Pompeu Fabra (UPF)
M. Kotlyar: Data Science Discovery Centre for Chronic Diseases
C. Pastrello: Data Science Discovery Centre for Chronic Diseases
P. Beltrao: European Molecular Biology Laboratory
L. I. Furlong: Universitat Pompeu Fabra (UPF)
I. Jurisica: Data Science Discovery Centre for Chronic Diseases
H. Hermjakob: European Molecular Biology Laboratory
S. Orchard: European Molecular Biology Laboratory
P. Porras: European Molecular Biology Laboratory

Nature Communications, 2019, vol. 10, issue 1, 1-14

Abstract: Abstract The current wealth of genomic variation data identified at nucleotide level presents the challenge of understanding by which mechanisms amino acid variation affects cellular processes. These effects may manifest as distinct phenotypic differences between individuals or result in the development of disease. Physical interactions between molecules are the linking steps underlying most, if not all, cellular processes. Understanding the effects that sequence variation has on a molecule’s interactions is a key step towards connecting mechanistic characterization of nonsynonymous variation to phenotype. We present an open access resource created over 14 years by IMEx database curators, featuring 28,000 annotations describing the effect of small sequence changes on physical protein interactions. We describe how this resource was built, the formats in which the data is provided and offer a descriptive analysis of the data set. The data set is publicly available through the IntAct website and is enhanced with every monthly release.

Date: 2019
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-018-07709-6 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-018-07709-6

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-018-07709-6

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().

 
Page updated 2025-03-19
Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-018-07709-6