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Metabolomics13C-glucose tracing analysis of IFN-treated A549 cells expressing wild-type SARS-CoV-2 Nsp3-4 or a deISGylation-defective Nsp3-4 mutant protein

Interferon (IFN)-stimulated gene 15 (ISG15) regulates diverse cellular processes, including antiviral immunity, through its conjugation to target proteins (ISGylation). Increasing evidence suggests that ISGylation can also reshape cellular metabolism; however, how viruses counteract ISGylation-me...

2026-05-05 | MTBLS14030 | MetaboLights
TranscriptomicsStrigolactone biosynthesis requires the symbiotic GRAS-type transcription factors NSP1 and NSP2
Legume GRAS-type transcription factors NSP1 and NSP2 are essential for Rhizobium Nod factor-induced nodulation. Both proteins are considered to be Nod factor response factors regulating gene expression upon symbiotic signalling. However, legume NSP1 and NSP2 can be functionally replaced by non-legum...
ORGANISM(S): Medicago truncatula 
2011-11-01 | E-GEOD-26548 | biostudies-arrayexpress
GenomicsNitrosospira sp. Nsp2
Nitrosospira sp. 2 Nsp2 genome sequencing
PRJNA332079 | ENA
GenomicsNitrosospira sp. Nsp2
Nitrosospira sp. Nsp2 Genome sequencing and assembly
PRJNA444084 | ENA
ProteomicsCryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes
Using structural analysis together with affinity tagged purification mass spectrometry experiments, we identify Nsp2 mutants that are unable to interact with key host proteins and processes.
ORGANISM(S): Homo sapiens (Human) 
2022-01-20 | PXD025817 | Pride
Apms Artificial intelligence Sars-cov-2 Protein-protein interactions Cryoem Nsp2 
ProteomicsSARS-CoV-2 Nsp2 recruits GIGYF2 near viral replication sites and supports viral protein production
The SARS-CoV-2 genome encodes 16 non-structural proteins (Nsps), with Nsp2 being the least conserved and least understood. In this study, we found a crucial role of Nsp2 in the SARS-CoV-2 life cycle and demonstrated its interaction with GIGYF2, which causes the relocation of GIGYF2 to near double me...
ORGANISM(S): Homo sapiens (Human) 
2025-07-26 | PXD052138 | Pride
Sars-cov-2 Gigyf2 Virus Nsp2 
ProteomicsHydrogen-deuterium exchange mass spectrometry of rotavirus NSP2/NSP5 biomolecular condensates
Biomolecular condensates selectively compartmentalise and organise biomolecules within the crowded cellular milieu, and are instrumental in some disease mechanisms, including aiding RNA virus replication. Upon infection, many RNA viruses form biomolecular condensates that are often referred to as vi...
ORGANISM(S): Bovine rotavirus strain RF 
2025-06-23 | PXD058097 | Pride
Rotavirus Nsp2 Hdx Nsp5 
ProteomicsNsp1 and Nsp2 interactome and proteome
The samples represent pulldowns of protein Nsp1 and Nsp2 from SARS-CoV and SARS-CoV2, as well its unfunctional mutants. Additionally, total proteomes of corresponding samples were analyzed.
ORGANISM(S): Homo sapiens (Human) 
2022-05-10 | PXD024480 | Pride
Extracellular vesicle Cerebrospinal fluid Traumatic brain injury 
TranscriptomicsStrigolactone biosynthesis requires the symbiotic GRAS-type transcription factors NSP1 and NSP2
Legume GRAS-type transcription factors NSP1 and NSP2 are essential for Rhizobium Nod factor-induced nodulation. Both proteins are considered to be Nod factor response factors regulating gene expression upon symbiotic signalling. However, legume NSP1 and NSP2 can be functionally replaced by non-legum...
ORGANISM(S): Medicago sativa Medicago truncatula Sinorhizobium meliloti 
2011-11-01 | GSE26548 | GEO
OtherSARS-CoV-2 Nsp2 recruits GIGYF2 near viral replication sites and supports viral protein production
The SARS-CoV-2 genome encodes 16 non-structural proteins (Nsps), with Nsp2 being the least conserved and least understood. In this study, we found a crucial role of Nsp2 in the SARS-CoV-2 life cycle and demonstrated its interaction with GIGYF2, which causes the relocation of GIGYF2 to near double me...
ORGANISM(S): Homo sapiens 
2025-07-30 | GSE269563 | GEO
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