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NSP5 is able to form homodimers, as seen in the porcine r...
| Class:Id | Summation:9821843 |
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| _displayName | NSP5 is able to form homodimers, as seen in the porcine r... |
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| _timestamp | 2025-12-15 15:38:39 |
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| created | [InstanceEdit:9821845] Stephan, Ralf, 2022-12-11 |
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| literatureReference | [LiteratureReference:9821841] The C-terminal domain of rotavirus NSP5 is essential for its multimerization, hyperphosphorylation and interaction with NSP6
[LiteratureReference:9821850] In vivo interactions among rotavirus nonstructural proteins
[LiteratureReference:9821659] In vivo and in vitro phosphorylation of rotavirus NSP5 correlates with its localization in viroplasms
[LiteratureReference:9822080] Recommendations for the classification of group A rotaviruses using all 11 genomic RNA segments |
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| modified | [InstanceEdit:9821869] Stephan, Ralf, 2022-12-12
[InstanceEdit:9824120] Stephan, Ralf, 2023-01-16
[InstanceEdit:9824627] Stephan, Ralf, 2023-01-21
[InstanceEdit:9976886] Orlic-Milacic, Marija, 2025-12-15 |
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| text | NSP5 is able to form homodimers, as seen in the porcine rotavirus YM and bovine RF strains (Poncet et al, 1997; González et al, 1998; Torres-Vega et al, 2000). The porcine YM strain of rotavirus has an NSP5 gene of genotype H1 (Matthijnssens et al, 2008). Therefore it is well suited to stand for NSP5 of genotype H1 from human strains like the curated D strain in experiments (González et al, 1998; Torres-Vega et al, 2000). Dimerization of NSP5 of genotype H3 has been shown in the bovine RF strain and might be presumed to occur in human strains with NSP5 of genotype H3 which have been reported in Poncet et al, 1997. |
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| (summation) | [Reaction:9821851] NSP5 forms a dimer [Homo sapiens] |
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NSP5 is able to form homodimers, as seen in the porcine r... (9821843)
