ArticlebioRxiv : the preprint server for biology2023
Assembly reactions of SARS-CoV-2 nucleocapsid protein with nucleic acid.
Huaying Zhao, Abdullah M Syed, Mir M Khalid, Ai Nguyen, Alison Ciling, Di Wu, Wai-Ming Yau, Sanjana Srinivasan, Dominic Esposito, Jennifer A Doudna and 3 more
Open access · greenAbstract readPreprint
In one paragraphArticle in bioRxiv : the preprint server for biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
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What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
2 · The registryThe trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
3 · Its place in the literatureWho cites it
0 citing papers in PubMed, 5 citations in OpenAlex.
No citing paper in PubMed yet.
4 · The recordCorrections and comments
5 · Who and what moneyAuthors and funding
13 authors at 4 institutions in 1 country.
Huaying ZhaoLaboratory of Dynamics of Macromolecular Assembly, National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health, Bethesda, MD 20892.ORCID 0000-0002-8827-6639 Abdullah M SyedGladstone Institutes, San Francisco, CA 94158.
Mir M KhalidGladstone Institutes, San Francisco, CA 94158.
Ai NguyenLaboratory of Dynamics of Macromolecular Assembly, National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health, Bethesda, MD 20892.
Alison CilingGladstone Institutes, San Francisco, CA 94158.
Di WuBiophysics Core Facility, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892.
Wai-Ming YauLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.
Sanjana SrinivasanLaboratory of Dynamics of Macromolecular Assembly, National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health, Bethesda, MD 20892.
Dominic EspositoProtein Expression Laboratory, Frederick National Laboratory for Cancer Research, Frederick, MD 21702.
Grzegorz PiszczekBiophysics Core Facility, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892.ORCID 0000-0002-5270-3678 Melanie OttGladstone Institutes, San Francisco, CA 94158.
Peter SchuckLaboratory of Dynamics of Macromolecular Assembly, National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health, Bethesda, MD 20892.ORCID 0000-0002-8859-6966 National Institutes of Health · USGladstone Institutes · USProtein Express (United States) · USQB3 · US
Funding
WORK ORDER 126643 B539 EXPAND IC SUITE75N91019D00024 · NIAID · LEIDOS BIOMEDICAL RESEARCH, INC. · PI BRISCOE, LYNN · 2019 to 2025
$3932.6MRESEARCH PROJECT 2U19AI135990 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI Melanie Maria Ott · 2018 to 2026
$21.4MNCI NIH HHS 75N91019D00024NIAID NIH HHS U19 AI135990
6 · The paper itselfAbstract
The viral genome of SARS-CoV-2 is packaged by the nucleocapsid (N-) protein into ribonucleoprotein particles (RNPs), 38±10 of which are contained in each virion. Their architecture has remained unclear due to the pleomorphism of RNPs, the high flexibility of N-protein intrinsically disordered regions, and highly multivalent interactions between viral RNA and N-protein binding sites in both N-terminal (NTD) and C-terminal domain (CTD). Here we explore critical interaction motifs of RNPs by applying a combination of biophysical techniques to mutant proteins binding different nucleic acids in an
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PMID38045338
PMCPMC10690241
OpenAlexW4388933820
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