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Details on Person SARS-CoV-2 nucleocapsid protein (N) can undergo liquid-liqui...

Class:IdSummation:9694535
_displayNameSARS-CoV-2 nucleocapsid protein (N) can undergo liquid-liqui...
_timestamp2022-02-08 09:14:41
created[InstanceEdit:9694660] Cook, Justin, 2020-07-07
literatureReference[LiteratureReference:9683962] Phosphorylation of the arginine/serine dipeptide-rich motif of the severe acute respiratory syndrome coronavirus nucleocapsid protein modulates its multimerization, translation inhibitory activity and cellular localization
[LiteratureReference:9683975] Structure of the N-terminal RNA-binding domain of the SARS CoV nucleocapsid protein
[LiteratureReference:9683984] Structure of the SARS coronavirus nucleocapsid protein RNA-binding dimerization domain suggests a mechanism for helical packaging of viral RNA
[LiteratureReference:9683969] Solution structure of the c-terminal dimerization domain of SARS coronavirus nucleocapsid protein solved by the SAIL-NMR method
[LiteratureReference:9683990] The SARS coronavirus nucleocapsid protein--forms and functions
[LiteratureReference:9683948] Modular organization of SARS coronavirus nucleocapsid protein
[LiteratureReference:9683953] Multiple nucleic acid binding sites and intrinsic disorder of severe acute respiratory syndrome coronavirus nucleocapsid protein: implications for ribonucleocapsid protein packaging
[LiteratureReference:9683934] Analysis of multimerization of the SARS coronavirus nucleocapsid protein
[LiteratureReference:9683940] Carboxyl terminus of severe acute respiratory syndrome coronavirus nucleocapsid protein: self-association analysis and nucleic acid binding characterization
[LiteratureReference:9683993] The dimer interface of the SARS coronavirus nucleocapsid protein adapts a porcine respiratory and reproductive syndrome virus-like structure
[LiteratureReference:9682783] The nucleocapsid protein of the SARS coronavirus is capable of self-association through a C-terminal 209 amino acid interaction domain
[LiteratureReference:9683966] Recombinant severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein forms a dimer through its C-terminal domain
[LiteratureReference:9683069] Transient oligomerization of the SARS-CoV N protein--implication for virus ribonucleoprotein packaging
[LiteratureReference:9683992] The SARS-CoV nucleocapsid protein: a protein with multifarious activities
[LiteratureReference:9682961] The severe acute respiratory syndrome coronavirus nucleocapsid protein is phosphorylated and localizes in the cytoplasm by 14-3-3-mediated translocation
modified[InstanceEdit:9699090] Cook, Justin, 2020-09-10
[InstanceEdit:9763968] Stephan, Ralf, 2022-02-08
textSARS-CoV-2 nucleocapsid protein (N) can undergo liquid-liquid phase separation (LLPS) with RNA. The mutual interactions between N dimers, and those between N dimers and viral RNA drive a polymerization process leading to compaction of long genomic RNA molecules which is key for viral packaging (Wang S et al. 2021; Cubuk J et al. 2021; Jack et al, 2021; Zhao et al, 2021). The LLPS is robust and binds the SARS-CoV-2 membrane protein (M) (Lu S et al, 2021). It also interacts with the stress granule protein G3BP1, and the TAK1 and IKK complexes, the key kinases of NF-κB signaling, to enhance NF-κB activation (Lu S et al, 2021; Wu Y et al, 2021).
(summation)[Reaction:9694455] SUMO-p-N protein dimer binds genomic RNA [Homo sapiens]
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