V
Vincent Gerard Francis
Researcher at Indian Institute of Technology Madras
Publications - 13
Citations - 157
Vincent Gerard Francis is an academic researcher from Indian Institute of Technology Madras. The author has contributed to research in topics: Phospholipid scramblase & Biology. The author has an hindex of 7, co-authored 9 publications receiving 126 citations. Previous affiliations of Vincent Gerard Francis include Montreal Neurological Institute and Hospital.
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SARS-CoV-2 infects cells following viral entry via clathrin-mediated endocytosis
TL;DR: It is demonstrated that following engagement with the plasma membrane, SARS-CoV-2 undergoes rapid clathrin-mediated endocytosis, which suggests that transfer of viral RNA to the cell cytosol occurs from the lumen of the endosomal system, and importantly clATHrin-heavy chain knockdown, which blocks clathin-mediatedendocytotic, reduces viral infectivity.
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The single C-terminal helix of human phospholipid scramblase 1 is required for membrane insertion and scrambling activity.
TL;DR: The CTH domain is deleted and it is concluded that CTH is required for membrane insertion and Ca2+ coordination and also plays an important role in the functional conformation of hPLSCR1.
Journal Article
SARS-CoV-2 infects cells following viral entry via clathrin-mediated endocytosis.
TL;DR: The authors showed that SARS-CoV-2 uses clathrin-mediated endocytosis to gain access into cells and suggests that this process is a key aspect of virus infectivity, which suggests that transfer of viral RNA to the cell cytosol occurs from the lumen of the endosomal system.
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Recovery of functionally active recombinant human phospholipid scramblase 1 from inclusion bodies using N-lauroyl sarcosine
TL;DR: A method to purify recombinant membrane protein with higher yield than previously described methods involving renaturation techniques is described and revealed that the secondary structure of protein is predominantly an α-helix, and under nondenaturing conditions, the protein exists as a monomer.
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N-terminal proline-rich domain is required for scrambling activity of human phospholipid scramblases.
TL;DR: It is concluded that scramblases exhibit Ca2+-dependent scrambling activity by aggregation of protein, and the results suggest that PRD is crucial for the function of the protein.