ArticleJournal of biomedical science2008
Interactions between M protein and other structural proteins of severe, acute respiratory syndrome-associated coronavirus.
Article in Journal of biomedical science, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 1 of them a synthesis that pooled it.
What it found
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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
25 citing papers in PubMed, 1 synthesis or guideline pooled it, 40 citations in OpenAlex.
- Molecular diagnosis of COVID-19 in different biologic matrix, their diagnostic validity and clinical relevance: A systematic review.Life sciences · 2020Pooled it
- The structure and function of membrane protein in coronavirus infection and its applications in the development of vaccines and therapeutic drugs.Frontiers in microbiology · 2026Review
- Classification, replication, and transcription ofFrontiers in microbiology · 2023Review
- Seasonal effects decouple SARS-CoV-2 haplotypes worldwide.F1000Research · 2023Article
- The envelope proteins from SARS-CoV-2 and SARS-CoV potently reduce the infectivity of human immunodeficiency virus type 1 (HIV-1).Retrovirology · 2022Article
- Unique mutations in SARS-CoV-2 Omicron subvariants' non-spike proteins: Potential impacts on viral pathogenesis and host immune evasion.Microbial pathogenesis · 2022Review
- The emergence of SARS-CoV-2 variants of concern in Australia by haplotype coalescence reveals a continental link to COVID-19 seasonality.Methods in microbiology · 2022Article
- The highly conserved RNA-binding specificity of nucleocapsid protein facilitates the identification of drugs with broad anti-coronavirus activity.Computational and structural biotechnology journal · 2022Article
- Refinement of SARS-CoV-2 envelope protein structure in a native-like environment by molecular dynamics simulations.Frontiers in molecular biosciences · 2022Article
- Molecular interactions of the M and E integral membrane proteins of SARS-CoV-2.Faraday discussions · 2021Article
- Article
- Antibodies Targeting Two Epitopes in SARS-CoV-2 Neutralize Pseudoviruses with the Spike Proteins from Different Variants.Pathogens (Basel, Switzerland) · 2021Article
- SARS-CoV-2: Insights into its structural intricacies and functional aspects for drug and vaccine development.International journal of biological macromolecules · 2021Review
- Control Measures for SARS-CoV-2: A Review on Light-Based Inactivation of Single-Stranded RNA Viruses.Pathogens (Basel, Switzerland) · 2020Review
- A recent origin of Orf3a from M protein across the coronavirus lineage arising by sharp divergence.Computational and structural biotechnology journal · 2020Article
- Article
- Characterization of an Immunodominant Epitope in the Endodomain of the Coronavirus Membrane Protein.Viruses · 2016Article
- Studying coronavirus-host protein interactions.Methods in molecular biology (Clifton, N.J.) · 2015Article
- SARS-CoV nucleocapsid protein interacts with cellular pyruvate kinase protein and inhibits its activity.Archives of virology · 2012Article
- Coronavirus pathogenesis.Advances in virus research · 2011Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Severe acute respiratory syndrome-associated coronavirus (SARS-CoV) structural proteins (S, E, M, and NC) localize in different subcellular positions when expressed individually. However, SARS-CoV M protein is co-localized almost entirely with S, E, or NC protein when co-expressed in the cells. On the other hand, only partial co-localization was observed when S and E, S and NC, or E and NC were co-expressed in the cells. Interactions between SARS-CoV M and other structural proteins but not interactions between S and E, S and NC, or E and NC were further demonstrated by co-immunoprecipitation assay. These results indicate that SARS-CoV M protein, similar to the M proteins of other coronaviruses, plays a pivotal role in virus assembly. The cytoplasmic C-terminus domain of SARS-CoV M protein was responsible for binding to NC protein. Multiple regions of M protein interacted with E and S proteins. A model for the interactions between SARS-CoV M protein and other structural proteins is proposed. This study helps us better understand protein-protein interactions during viral assembly of SARS-CoV.
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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.