Biochemical, conformational, and immunogenic analysis of soluble trimeric forms of henipavirus fusion glycoproteins

• المؤلفون الرئيسيون: Chan, Y.-P, Lu, M, Dutta, S, Yan, L, Barr, J, Flora, M, Feng, Y.-R, Xu, K, Nikolov, D.B, Wang, L.-F, Skiniotis, G, Broder, C.C
• مؤلفون آخرون: DUKE-NUS MEDICAL SCHOOL
• التنسيق: مقال
• منشور في: 2020
• الموضوعات: glycosylphosphatidylinositol; hybrid protein; monoclonal antibody; neutralizing antibody; peptide; phospholipase D; protein antibody; protein precursor; proteinase; sF glycoprotein; unclassified drug; virus antibody; virus glycoprotein; virus vaccine; amino acid sequence; animal experiment; antibody specificity; article; biochemistry; bioengineering; carboxy terminal sequence; cell membrane; controlled study; cross reaction; cytoplasm; Hendra virus; Hendra virus infection; Henipavirus; human; human cell; immunological procedures; in vitro study; mouse; Nipah virus; Nipah virus infection; nonhuman; priority journal; protein cleavage; protein conformation; protein depletion; protein domain; protein structure; protein synthesis; vaccine production; virus recombinant; Animals; Antibodies, Monoclonal; Antibodies, Neutralizing; Antibodies, Viral; Cross Reactions; HeLa Cells; Humans; Mice; Microscopy, Electron; Protein Conformation; Recombinant Proteins; Viral Fusion Proteins; Animalia; Mus
• الوصول للمادة أونلاين: https://scholarbank.nus.edu.sg/handle/10635/180818
• المؤسسة: National University of Singapore

10.1128/JVI.01318-12