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
Description
ISSN:2375-2548
DOI:10.1126/sciadv.adl6144