Skip to content
DraconiticResearch
Search Sources API
203,234 studies31 sourcesUpdated 15 min ago
Peer-reviewedCC BY-NC-ND 4.0Journal of Biological Chemistry

N-Glycosylation in the Receptor Binding Domain serves as aggregation gatekeeper of the SARS CoV2 Spike glycoprotein folding

Related

  1. Acute profound thrombocytopenia associated with glycoprotein IIb/IIIa receptor inhibitor after percutaneous coronary intervention: a single-center 6-year case series and therapy insights
    Yue Wu, Kaiyue Feng, Lei Liu +1
    BMC Cardiovascular DisordersPeer-reviewedCC BY-NC-ND 4.0Full textCardiovascular medicinePMC
  2. Receptor Binding Drives Toxicokinetic Processes: Insights from Two Amphipod Species Exposed to Insecticides Targeting the Nicotinic Acetylcholine Receptor
    Clarissa von Au, Natsumi Maeda, Johannes Raths +1
    Environmental Science & TechnologyPeer-reviewedCC BY 4.0Full textPharmacology & toxicologyPMC
  3. The chemokine receptor‐like fourth extracellular loop of the apelin receptor differentially regulates apelin and elabela binding and signalling
    Chloé Bonef, Hela Bouhsine, Carine Huynh +9
    British Journal of PharmacologyPeer-reviewedCC BY 4.0Full textGeneral biochemistryGeneral biologyHAL
  4. Fas receptor binding is a key determinant of the enhanced aggressiveness of the novel recombinant Echovirus 11.
    Leonardo Sclavi, Giulia Venneri, Antonella Bugatti +6
    Emerging microbes & infectionsPeer-reviewedCC BY-NCFull textCardiovascular medicineEurope PMC
  5. Binding of a Novel 11β-Hydroxysteroid to the Apelin Receptor (APLNR) and Its Possible Role in Regulating Skeletal Muscle Health in Mice
    Marcos González-Pérez, Citlali Gómez-Márquez, Miguel Ortiz-Flores +3
    International Journal of Molecular SciencesPeer-reviewedCC BY 4.0Full textPharmacology & toxicologyCrossrefEurope PMC
BibTeX
@article{kumari2026nglycosylation,
  title = {{N-Glycosylation in the Receptor Binding Domain serves as aggregation gatekeeper of the SARS CoV2 Spike glycoprotein folding}},
  author = {Anita Kumari and Beena Krishnan},
  journal = {Journal of Biological Chemistry},
  year = {2026},
  month = oct,
  doi = {10.1016/j.jbc.2026.113681},
  url = {https://linkinghub.elsevier.com/retrieve/pii/S0021925826025536},
  note = {CC BY-NC-ND 4.0},
}
RIS
TY  - JOUR
TI  - N-Glycosylation in the Receptor Binding Domain serves as aggregation gatekeeper of the SARS CoV2 Spike glycoprotein folding
AU  - Anita Kumari
AU  - Beena Krishnan
PY  - 2026
DA  - 2026/10/01
JO  - Journal of Biological Chemistry
DO  - 10.1016/j.jbc.2026.113681
UR  - https://linkinghub.elsevier.com/retrieve/pii/S0021925826025536
SN  - 0021-9258
ER  -