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171 related items for PubMed ID: 34435771
1. Stability of HA2 Prefusion Structure and pH-Induced Conformational Changes in the HA2 Domain of H3N2 Hemagglutinin. Eller MW, Siaw HMH, Dyer RB. Biochemistry; 2021 Sep 07; 60(35):2623-2636. PubMed ID: 34435771 [Abstract] [Full Text] [Related]
2. Intermonomer Interactions in Hemagglutinin Subunits HA1 and HA2 Affecting Hemagglutinin Stability and Influenza Virus Infectivity. Wang W, DeFeo CJ, Alvarado-Facundo E, Vassell R, Weiss CD. J Virol; 2015 Oct 07; 89(20):10602-11. PubMed ID: 26269180 [Abstract] [Full Text] [Related]
3. Direct Visualization of the Conformational Dynamics of Single Influenza Hemagglutinin Trimers. Das DK, Govindan R, Nikić-Spiegel I, Krammer F, Lemke EA, Munro JB. Cell; 2018 Aug 09; 174(4):926-937.e12. PubMed ID: 29961575 [Abstract] [Full Text] [Related]
4. The final conformation of the complete ectodomain of the HA2 subunit of influenza hemagglutinin can by itself drive low pH-dependent fusion. Kim CS, Epand RF, Leikina E, Epand RM, Chernomordik LV. J Biol Chem; 2011 Apr 15; 286(15):13226-34. PubMed ID: 21292763 [Abstract] [Full Text] [Related]
5. Structural characterization of an early fusion intermediate of influenza virus hemagglutinin. Xu R, Wilson IA. J Virol; 2011 May 15; 85(10):5172-82. PubMed ID: 21367895 [Abstract] [Full Text] [Related]
6. The Stabilities of the Soluble Ectodomain and Fusion Peptide Hairpins of the Influenza Virus Hemagglutinin Subunit II Protein Are Positively Correlated with Membrane Fusion. Ranaweera A, Ratnayake PU, Weliky DP. Biochemistry; 2018 Sep 18; 57(37):5480-5493. PubMed ID: 30141905 [Abstract] [Full Text] [Related]
7. pH-induced conformational changes of membrane-bound influenza hemagglutinin and its effect on target lipid bilayers. Gray C, Tamm LK. Protein Sci; 1998 Nov 18; 7(11):2359-73. PubMed ID: 9828002 [Abstract] [Full Text] [Related]
8. Hydrogen-Deuterium Exchange Supports Independent Membrane-Interfacial Fusion Peptide and Transmembrane Domains in Subunit 2 of Influenza Virus Hemagglutinin Protein, a Structured and Aqueous-Protected Connection between the Fusion Peptide and Soluble Ectodomain, and the Importance of Membrane Apposition by the Trimer-of-Hairpins Structure. Ranaweera A, Ratnayake PU, Ekanayaka EAP, Declercq R, Weliky DP. Biochemistry; 2019 May 14; 58(19):2432-2446. PubMed ID: 31008587 [Abstract] [Full Text] [Related]
9. A nonfusogenic antigen mimic of influenza hemagglutinin glycoproteins constituted with soluble full-length HA1 and truncated HA2 proteins expressed in E. coli. Kim CS, Park YJ. Mol Biotechnol; 2015 Feb 14; 57(2):128-37. PubMed ID: 25288022 [Abstract] [Full Text] [Related]
10. A histidine residue of the influenza virus hemagglutinin controls the pH dependence of the conformational change mediating membrane fusion. Mair CM, Meyer T, Schneider K, Huang Q, Veit M, Herrmann A. J Virol; 2014 Nov 14; 88(22):13189-200. PubMed ID: 25187542 [Abstract] [Full Text] [Related]
11. Structural insights into the membrane fusion mechanism mediated by influenza virus hemagglutinin. Ni F, Chen X, Shen J, Wang Q. Biochemistry; 2014 Feb 11; 53(5):846-54. PubMed ID: 24433110 [Abstract] [Full Text] [Related]
13. Probing the metastable state of influenza hemagglutinin. Kingsley CN, Antanasijevic A, Palka-Hamblin H, Durst M, Ramirez B, Lavie A, Caffrey M. J Biol Chem; 2017 Dec 29; 292(52):21590-21597. PubMed ID: 29127198 [Abstract] [Full Text] [Related]
14. Energetics of the loop-to-helix transition leading to the coiled-coil structure of influenza virus hemagglutinin HA2 subunits. Huang Q, Korte T, Rachakonda PS, Knapp EW, Herrmann A. Proteins; 2009 Feb 01; 74(2):291-303. PubMed ID: 18618705 [Abstract] [Full Text] [Related]
15. A soluble domain of the membrane-anchoring chain of influenza virus hemagglutinin (HA2) folds in Escherichia coli into the low-pH-induced conformation. Chen J, Wharton SA, Weissenhorn W, Calder LJ, Hughson FM, Skehel JJ, Wiley DC. Proc Natl Acad Sci U S A; 1995 Dec 19; 92(26):12205-9. PubMed ID: 8618870 [Abstract] [Full Text] [Related]
16. Dynamic changes during acid-induced activation of influenza hemagglutinin. Garcia NK, Guttman M, Ebner JL, Lee KK. Structure; 2015 Apr 07; 23(4):665-76. PubMed ID: 25773144 [Abstract] [Full Text] [Related]
17. Structural monitoring of a transient intermediate in the hemagglutinin fusion machinery on influenza virions. Benhaim MA, Mangala Prasad V, Garcia NK, Guttman M, Lee KK. Sci Adv; 2020 May 07; 6(18):eaaz8822. PubMed ID: 32494683 [Abstract] [Full Text] [Related]
18. Hemagglutinin Cleavability, Acid Stability, and Temperature Dependence Optimize Influenza B Virus for Replication in Human Airways. Laporte M, Stevaert A, Raeymaekers V, Boogaerts T, Nehlmeier I, Chiu W, Benkheil M, Vanaudenaerde B, Pöhlmann S, Naesens L. J Virol; 2019 Dec 12; 94(1):. PubMed ID: 31597759 [Abstract] [Full Text] [Related]
19. Conserved neutralizing epitope at globular head of hemagglutinin in H3N2 influenza viruses. Iba Y, Fujii Y, Ohshima N, Sumida T, Kubota-Koketsu R, Ikeda M, Wakiyama M, Shirouzu M, Okada J, Okuno Y, Kurosawa Y, Yokoyama S. J Virol; 2014 Jul 12; 88(13):7130-44. PubMed ID: 24719430 [Abstract] [Full Text] [Related]
20. Exploring the early stages of the pH-induced conformational change of influenza hemagglutinin. Zhou Y, Wu C, Zhao L, Huang N. Proteins; 2014 Oct 12; 82(10):2412-28. PubMed ID: 24854389 [Abstract] [Full Text] [Related] Page: [Next] [New Search]