The immune-evasive proline-283 substitution in influenza nucleoprotein increases aggregation propensity without altering the native structure.

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Title: The immune-evasive proline-283 substitution in influenza nucleoprotein increases aggregation propensity without altering the native structure.
Authors: Yoon J; Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, USA., Zhang YM; Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, USA., Her C; Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, USA., Grant RA; Department of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA., Ponomarenko AI; Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, USA., Ackermann BE; Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, USA., Hui T; Department of Chemistry, Tufts University, Medford, MA, USA., Lin YS; Department of Chemistry, Tufts University, Medford, MA, USA., Debelouchina GT; Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, USA., Shoulders MD; Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, USA.; Broad Institute of MIT and Harvard, Cambridge, MA, USA.; Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, MA, USA.
Source: Science advances [Sci Adv] 2024 Apr 19; Vol. 10 (16), pp. eadl6144. Date of Electronic Publication: 2024 Apr 19.
Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
Journal Info: Publisher: American Association for the Advancement of Science Country of Publication: United States NLM ID: 101653440 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 2375-2548 (Electronic) Linking ISSN: 23752548 NLM ISO Abbreviation: Sci Adv Subsets: MEDLINE
Database: MEDLINE Ultimate
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  Data: The immune-evasive proline-283 substitution in influenza nucleoprotein increases aggregation propensity without altering the native structure.
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  Data: <searchLink fieldCode="AU" term="%22Yoon+J%22">Yoon J</searchLink>; Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, USA.<br /><searchLink fieldCode="AU" term="%22Zhang+YM%22">Zhang YM</searchLink>; Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, USA.<br /><searchLink fieldCode="AU" term="%22Her+C%22">Her C</searchLink>; Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, USA.<br /><searchLink fieldCode="AU" term="%22Grant+RA%22">Grant RA</searchLink>; Department of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA.<br /><searchLink fieldCode="AU" term="%22Ponomarenko+AI%22">Ponomarenko AI</searchLink>; Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, USA.<br /><searchLink fieldCode="AU" term="%22Ackermann+BE%22">Ackermann BE</searchLink>; Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, USA.<br /><searchLink fieldCode="AU" term="%22Hui+T%22">Hui T</searchLink>; Department of Chemistry, Tufts University, Medford, MA, USA.<br /><searchLink fieldCode="AU" term="%22Lin+YS%22">Lin YS</searchLink>; Department of Chemistry, Tufts University, Medford, MA, USA.<br /><searchLink fieldCode="AU" term="%22Debelouchina+GT%22">Debelouchina GT</searchLink>; Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, USA.<br /><searchLink fieldCode="AU" term="%22Shoulders+MD%22">Shoulders MD</searchLink>; Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, USA.; Broad Institute of MIT and Harvard, Cambridge, MA, USA.; Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, MA, USA.
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              Text: 2024 Apr 19
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