A new algorithm can predict the propensity of proteins to aggregate.
This is a preview of subscription content, access via your institution
Relevant articles
Open Access articles citing this article.
-
The Host-Pathogen interaction of human cyclophilin A and HIV-1 Vpr requires specific N-terminal and novel C-terminal domains
BMC Structural Biology Open Access 20 December 2011
Access options
Subscribe to this journal
Receive 12 print issues and online access
$259.00 per year
only $21.58 per issue
Buy this article
- Purchase on SpringerLink
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout

Bob Crimi
References
Bucciantini, M. et al. Nature 416, 507–511 (2002).
Fernandez-Escamilla, A. et al. Nat. Biotechnol. 22, xx–xx (2004).
Kayed, R. et al. Science 300, 486–489 (2003).
Munoz, V. & Serrano, L. Nat. Struct. Biol. 1, 399–409 (1994).
Lambert, M.P. et al. Proc. Natl. Acad. Sci. USA 95, 6448–6453 (1998).
Lambert, M.P. et al. J. Neurochem. 79, 595–605 (2001).
Guerois, R., Nielsen, J.E. & Serrano, L. J. Mol. Biol. 320, 369–387 (2002).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Pande, V. A universal TANGO?. Nat Biotechnol 22, 1240–1241 (2004). https://doi.org/10.1038/nbt1004-1240
Issue date:
DOI: https://doi.org/10.1038/nbt1004-1240
This article is cited by
-
Aggregation hot spots in the SARS-CoV-2 proteome may constitute potential therapeutic targets for the suppression of the viral replication and multiplication
Journal of Proteins and Proteomics (2021)
-
The Host-Pathogen interaction of human cyclophilin A and HIV-1 Vpr requires specific N-terminal and novel C-terminal domains
BMC Structural Biology (2011)