The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Proteome survey reveals modularity of the yeast cell machinery
Abstract
Protein complexes are key molecular entities that integrate multiple gene products to perform cellular functions. Here we report the first genome-wide screen for complexes in an organism, budding yeast, using affinity purification and mass spectrometry. Through systematic tagging of open reading frames (ORFs), the majority of complexes were purified several times, suggesting screen saturation. The richness of the data set enabled a de novo characterization of the composition and organization of the cellular machinery. The ensemble of cellular proteins partitions into 491 complexes, of which 257 are novel, that differentially combine with additional attachment proteins or protein modules to enable a diversification of potential functions. Support for this modular organization of the proteome comes from integration with available data on expression, localization, function, evolutionary conservation, protein structure and binary interactions. This study provides the largest collection of physically determined eukaryotic cellular machines so far and a platform for biological data integration and modelling.
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A comprehensive analysis of protein–protein interactions in Saccharomyces cerevisiae
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Global analysis of protein localization in budding yeast
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Global analysis of protein expression in yeast
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Interaction network containing conserved and essential protein complexes in Escherichia coli
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Systems Biology and New Technologies Enable Predictive and Preventative Medicine
Hood, L., Heath, J. R., Phelps, M. E., & Lin, B. (2004) · Science · doi:10.1126/science.1104635 · Cited by 1,108
Systematic interpretation of genetic interactions using protein networks
Kelley, R., & Ideker, T. (2005) · Nature Biotechnology · doi:10.1038/nbt1096 · Cited by 437
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Metadata
- Authors
- Gavin, A.-C., Aloy, P., Grandi, P., Krause, R., Boesche, M., Marzioch, M., Rau, C., Jensen, L. J., Bastuck, S., Dümpelfeld, B., Edelmann, A., Heurtier, M.-A., Hoffman, V., Hoefert, C., Klein, K., Hudak, M., Michon, A.-M., Schelder, M., Schirle, M., Remor, M., Rudi, T., Hooper, S., Bauer, A., Bouwmeester, T., Casari, G., Drewes, G., Neubauer, G., Rick, J. M., Kuster, B., Bork, P., Russell, R. B., & Superti-Furga, G.
- Venue
- Nature
- Published
- 2006-01-22
- Volume
- 440
- Issue
- 7084
- Pages
- 631-636
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2050721857
- Cited by
- 2,575
- References
- 6
- FWCI
- 92.70
- Type
- journal article
- Language
- en
- Open access
- closed
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- Gavin, A.-C., Aloy, P., Grandi, P., Krause, R., Boesche, M., Marzioch, M., Rau, C., Jensen, L. J., Bastuck, S., Dümpelfeld, B., Edelmann, A., Heurtier, M.-A., Hoffman, V., Hoefert, C., Klein, K., Hudak, M., Michon, A.-M., Schelder, M., Schirle, M., . . . Superti-Furga, G. (2006). Proteome survey reveals modularity of the yeast cell machinery. Nature. https://doi.org/10.1038/nature04532
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