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Details on Person Tetrameric assembly of hGBP1 is crucial for both stimulated GMP formation and antiviral activity
| Class:Id | LiteratureReference:9953162 |
|---|---|
| _displayName | Tetrameric assembly of hGBP1 is crucial for both stimulated GMP formation and antiviral activity |
| _timestamp | 2025-05-28 19:08:33 |
| author | [Person:9953134] Pandita, Esha [Person:9953174] Rajan, Sudeepa [Person:9953132] Rahman, Safikur [Person:9953160] Mullick, Ranajoy [Person:9953153] Das, Saumitra [Person:9953149] Sau, Apurba Kumar |
| created | [InstanceEdit:9953154] Shamovsky, Veronica, 2025-05-28 |
| journal | Biochem J |
| pages | 1745-57 |
| pubMedIdentifier | 27071416 |
| title | Tetrameric assembly of hGBP1 is crucial for both stimulated GMP formation and antiviral activity |
| volume | 473 |
| year | 2016 |
| (literatureReference) | [Summation:9947897] Guanylate-binding protein 1 (GBP1) membrane binding, dimer f... [Summation:9962134] The human Guanylate Binding Proteins (GBPs) constitute a fam... |
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No pathways have been reviewed or authored by Tetrameric assembly of hGBP1 is crucial for both stimulated GMP formation and antiviral activity (9953162)
