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ProteomicsDirect lipid interactions control SARS-CoV-2 M protein conformational dynamics and virus assembly
M is the most abundant structural membrane protein in coronaviruses and is essential for the formation of infectious virus particles. SARS-CoV-2 M adopts two conformations, Mshort and Mlong, and regulated transition between states is hypothesized to coordinate viral assembly and budding. However, th...
ORGANISM(S): Severe acute respiratory syndrome coronavirus 2 Homo sapiens (Human) 
2026-07-09 | PXD079401 | Pride
Hdxms Sars-cov-2 Lipid interaction 
UnknownDirect lipid interactions control SARS-CoV-2 M protein conformational dynamics and virus assembly.
Not available
S-EPMC11580925 | biostudies-literature
UnknownFirst transcriptome analysis of bryozoan <i>Fredericella sultana</i>, the primary host of myxozoan parasite <i>Tetracapsuloides bryosalmonae</i>.
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S-EPMC7194087 | biostudies-literature
UnknownTranscriptome Analysis Elucidates the Key Responses of Bryozoan <i>Fredericella sultana</i> during the Development of <i>Tetracapsuloides bryosalmonae</i> (Myxozoa).
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S-EPMC7460649 | biostudies-literature
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UnknownImpact of hepatitis C virus core mutations on the response to interferon-based treatment in chronic hepatitis C.
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S-EPMC5055871 | biostudies-literature
UnknownDual Inhibitors of Main Protease (MPro) and Cathepsin L as Potent Antivirals against SARS-CoV2.
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UnknownMental health outcomes of quarantine and isolation for infection prevention: a systematic umbrella review of the global evidence.
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S-EPMC7644933 | biostudies-literature
UnknownStock assessment of barred spiny eel, <i>Macrognathus pancalus</i> (Hamilton, 1822) in a wetland ecosystem, northwestern Bangladesh: A fundamental approach to ensure sustainability and conservation.
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S-EPMC11636827 | biostudies-literature
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