Lipman2003 - Single-Molecule Measurement of Protein Folding...

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DOI: 10.1126/science.1085399 , 1233 (2003); 301 Science et al. Everett A. Lipman, Kinetics Single-Molecule Measurement of Protein Folding www.sciencemag.org (this information is current as of September 4, 2009 ): The following resources related to this article are available online at http://www.sciencemag.org/cgi/content/full/301/5637/1233 version of this article at: including high-resolution figures, can be found in the online Updated information and services, http://www.sciencemag.org/cgi/content/full/301/5637/1233/DC1 can be found at: Supporting Online Material http://www.sciencemag.org/cgi/content/full/301/5637/1233#otherarticles , 11 of which can be accessed for free: cites 19 articles This article 152 article(s) on the ISI Web of Science. cited by This article has been http://www.sciencemag.org/cgi/content/full/301/5637/1233#otherarticles 17 articles hosted by HighWire Press; see: cited by This article has been http://www.sciencemag.org/cgi/collection/biochem Biochemistry : subject collections This article appears in the following http://www.sciencemag.org/about/permissions.dtl in whole or in part can be found at: this article permission to reproduce of this article or about obtaining reprints Information about obtaining registered trademark of AAAS. is a Science 2003 by the American Association for the Advancement of Science; all rights reserved. The title Copyright American Association for the Advancement of Science, 1200 New York Avenue NW, Washington, DC 20005. (print ISSN 0036-8075; online ISSN 1095-9203) is published weekly, except the last week in December, by the Science on September 4, 2009 www.sciencemag.org Downloaded from
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which suggests that different R proteins are activated by different mechanisms or that intermediate signaling steps are still to be identified that would lead to a similar mode of activation. A key common point in these models is that pathogen virulence proteins are recognized as a consequence of their virulence function, rather than by direct interaction with a plant R protein. Such indirect recognition would be expected to significantly constrain the coevolution of patho- gens and their plant hosts, as evasion of detec- tion would require modification of virulence functions. Furthermore, by recognizing patho- gen virulence proteins based on their enzymatic activity rather than their shape, plants could likely detect a large number of pathogen effec- tors with a limited number of R proteins. Al- though the extent of this mechanism is un- known [only three R genes are known to have dual specificity ( 24 26 )], this seems an attrac- tive strategy for the plant to maximize its sur- veillance capacity against the multitude of po- tential pathogen effectors. This may be a critical aspect of the plant immune system, as, unlike vertebrates, plants cannot generate a diversity of antibodies via somatic recombination.
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Lipman2003 - Single-Molecule Measurement of Protein Folding...

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