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Niess et al

Niess et al - CX3CR1-Mediated Dendritic Cell Access to the...

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DOI: 10.1126/science.1102901 , 254 (2005); 307 Science et al. Jan Hendrik Niess, Intestinal Lumen and Bacterial Clearance CR1-Mediated Dendritic Cell Access to the 3 CX www.sciencemag.org (this information is current as of March 8, 2008 ): The following resources related to this article are available online at http://www.sciencemag.org/cgi/content/full/307/5707/254 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/307/5707/254/DC1 can be found at: Supporting Online Material found at: can be related to this article A list of selected additional articles on the Science Web sites http://www.sciencemag.org/cgi/content/full/307/5707/254#related-content http://www.sciencemag.org/cgi/content/full/307/5707/254#otherarticles , 11 of which can be accessed for free: cites 18 articles This article 193 article(s) on the ISI Web of Science. cited by This article has been http://www.sciencemag.org/cgi/content/full/307/5707/254#otherarticles 62 articles hosted by HighWire Press; see: cited by This article has been http://www.sciencemag.org/cgi/collection/immunology Immunology : 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 2005 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 March 8, 2008 www.sciencemag.org Downloaded from
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stimulates phosphorylation of KaiC hexamer progressively, and then the phosphorylated KaiC hexamer forms a complex with KaiA. This KaiA binding likely triggers the binding of phos- phorylated KaiC-KaiA complexes to KaiB, an attenuator of KaiC autophosphorylation, to shift KaiC from a phosphorylation-dominating state to a dephosphorylation-dominating state. Reduction in the KaiC phosphorylation level would, in turn, accelerate phosphorylation re- actions and/or inhibit dephosphorylation with as-yet-unknown nonlinear processes, whereby both states alternate periodically. Such auto- regulatory posttranslational dynamics of the Kai proteins would be the core to generating the temperature-compensated, self-sustaining KaiC phosphorylation cycle as a minimal circadian circuit during DD (Fig. 4). The genome-wide transcriptional control exerted by KaiC that occurs during LL ( 6 , 7 ) may connect to the minimal oscillator to form an extended feedback loop that further amplifies and sta- bilizes the posttranslational oscillatory process and serves as a major source of physiologi- cally functional rhythm outputs (Fig. 4). Post- translational biochemical oscillation would
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