ArticleJournal of virology2005
Structural genomics of the severe acute respiratory syndrome coronavirus: nuclear magnetic resonance structure of the protein nsP7.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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.
The 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.
Who cites it
40 citing papers in PubMed.
- Are Viruses Taxonomic Units? A Protein Domain and Loop-Centric Phylogenomic Assessment.Viruses · 2024Review
- Review
- Selenoprotein S Interacts with the Replication and Transcription Complex of SARS-CoV-2 by Binding nsp7.Journal of molecular biology · 2023Article
- Drug-Repurposing Screening Identifies a Gallic Acid Binding Site on SARS-CoV-2 Non-structural Protein 7.ACS pharmacology & translational science · 2023Article
- Genomics and pathogenesis of the avian coronavirus infectious bronchitis virus.Australian veterinary journal · 2022Review
- The impact of the suppression of highly connected protein interactions on the corona virus infection.Scientific reports · 2022Article
- Molecular docking-assisted investigation of Pd(II) complexes carrying "SNS" pincer-type pyridine-thioether ligand as potential drug candidates against COVID-19.Computers in biology and medicine · 2022Article
- Porcine Epidemic Diarrhea Virus nsp7 Inhibits Interferon-Induced JAK-STAT Signaling through Sequestering the Interaction between KPNA1 and STAT1.Journal of virology · 2022Article
- Structural insights into SARS-CoV-2 proteins.Journal of molecular biology · 2021Review
- The recent outbreaks of human coronaviruses: A medicinal chemistry perspective.Medicinal research reviews · 2021Review
- Mass spectrometric based detection of protein nucleotidylation in the RNA polymerase of SARS-CoV-2.Communications chemistry · 2021Article
- Structural and functional insights into non-structural proteins of coronaviruses.Microbial pathogenesis · 2021Review
- A perspective on potential target proteins of COVID-19: Comparison with SARS-CoV for designing new small molecules.Bioorganic chemistry · 2020Review
- Insights into SARS-CoV-2 genome, structure, evolution, pathogenesis and therapies: Structural genomics approach.Biochimica et biophysica acta. Molecular basis of disease · 2020Review
- Structural basis for inhibition of the RNA-dependent RNA polymerase from SARS-CoV-2 by remdesivir.Science (New York, N.Y.) · 2020Article
- A Structural View of SARS-CoV-2 RNA Replication Machinery: RNA Synthesis, Proofreading and Final Capping.Cells · 2020Review
- Porcine Epidemic Diarrhea Virus and the Host Innate Immune Response.Pathogens (Basel, Switzerland) · 2020Review
- The Nonstructural Proteins Directing Coronavirus RNA Synthesis and Processing.Advances in virus research · 2016Review
- Atlas of coronavirus replicase structure.Virus research · 2014Review
- From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses.Antiviral research · 2013Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors.
Funding
Abstract
Here, we report the three-dimensional structure of severe acute respiratory syndrome coronavirus (SARS-CoV) nsP7, a component of the SARS-CoV replicase polyprotein. The coronavirus replicase carries out regulatory tasks involved in the maintenance, transcription, and replication of the coronavirus genome. nsP7 was found to assume a compact architecture in solution, which is comprised primarily of helical secondary structures. Three helices (alpha2 to alpha4) form a flat up-down-up antiparallel alpha-helix sheet. The N-terminal segment of residues 1 to 22, containing two turns of alpha-helix and one turn of 3(10)-helix, is packed across the surface of alpha2 and alpha3 in the helix sheet, with the alpha-helical region oriented at a 60 degrees angle relative to alpha2 and alpha3. The surface charge distribution is pronouncedly asymmetrical, with the flat surface of the helical sheet showing a large negatively charged region adjacent to a large hydrophobic patch and the opposite side containing a positively charged groove that extends along the helix alpha1. Each of these three areas is thus implicated as a potential site for protein-protein interactions.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.