231 related articles for article (PubMed ID: 9628890)
1. Specific single or double proline substitutions in the "spring-loaded" coiled-coil region of the influenza hemagglutinin impair or abolish membrane fusion activity.
Qiao H; Pelletier SL; Hoffman L; Hacker J; Armstrong RT; White JM
J Cell Biol; 1998 Jun; 141(6):1335-47. PubMed ID: 9628890
[TBL] [Abstract][Full Text] [Related]
2. New insights into the spring-loaded conformational change of influenza virus hemagglutinin.
Gruenke JA; Armstrong RT; Newcomb WW; Brown JC; White JM
J Virol; 2002 May; 76(9):4456-66. PubMed ID: 11932412
[TBL] [Abstract][Full Text] [Related]
3. A specific point mutant at position 1 of the influenza hemagglutinin fusion peptide displays a hemifusion phenotype.
Qiao H; Armstrong RT; Melikyan GB; Cohen FS; White JM
Mol Biol Cell; 1999 Aug; 10(8):2759-69. PubMed ID: 10436026
[TBL] [Abstract][Full Text] [Related]
4. Reversible structural changes in the influenza hemagglutinin precursor at membrane fusion pH.
Garcia-Moro E; Zhang J; Calder LJ; Brown NR; Gamblin SJ; Skehel JJ; Rosenthal PB
Proc Natl Acad Sci U S A; 2022 Aug; 119(33):e2208011119. PubMed ID: 35939703
[TBL] [Abstract][Full Text] [Related]
5. 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; 88(22):13189-200. PubMed ID: 25187542
[TBL] [Abstract][Full Text] [Related]
6. The 1-127 HA2 construct of influenza virus hemagglutinin induces cell-cell hemifusion.
Leikina E; LeDuc DL; Macosko JC; Epand R; Epand R; Shin YK; Chernomordik LV
Biochemistry; 2001 Jul; 40(28):8378-86. PubMed ID: 11444985
[TBL] [Abstract][Full Text] [Related]
7. 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; 89(20):10602-11. PubMed ID: 26269180
[TBL] [Abstract][Full Text] [Related]
8. Amino acid residues in the fusion peptide pocket regulate the pH of activation of the H5N1 influenza virus hemagglutinin protein.
Reed ML; Yen HL; DuBois RM; Bridges OA; Salomon R; Webster RG; Russell CJ
J Virol; 2009 Apr; 83(8):3568-80. PubMed ID: 19193808
[TBL] [Abstract][Full Text] [Related]
9. Expression of influenza B virus hemagglutinin containing multibasic residue cleavage sites.
Brassard DL; Lamb RA
Virology; 1997 Sep; 236(2):234-48. PubMed ID: 9325231
[TBL] [Abstract][Full Text] [Related]
10. 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; 286(15):13226-34. PubMed ID: 21292763
[TBL] [Abstract][Full Text] [Related]
11. 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; 74(2):291-303. PubMed ID: 18618705
[TBL] [Abstract][Full Text] [Related]
12. Analysis of residues near the fusion peptide in the influenza hemagglutinin structure for roles in triggering membrane fusion.
Thoennes S; Li ZN; Lee BJ; Langley WA; Skehel JJ; Russell RJ; Steinhauer DA
Virology; 2008 Jan; 370(2):403-14. PubMed ID: 17936324
[TBL] [Abstract][Full Text] [Related]
13. Studies of the membrane fusion activities of fusion peptide mutants of influenza virus hemagglutinin.
Steinhauer DA; Wharton SA; Skehel JJ; Wiley DC
J Virol; 1995 Nov; 69(11):6643-51. PubMed ID: 7474073
[TBL] [Abstract][Full Text] [Related]
14. pH-induced conformational changes of membrane-bound influenza hemagglutinin and its effect on target lipid bilayers.
Gray C; Tamm LK
Protein Sci; 1998 Nov; 7(11):2359-73. PubMed ID: 9828002
[TBL] [Abstract][Full Text] [Related]
15. 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; 57(37):5480-5493. PubMed ID: 30141905
[TBL] [Abstract][Full Text] [Related]
16. Structural transitions in influenza haemagglutinin at membrane fusion pH.
Benton DJ; Gamblin SJ; Rosenthal PB; Skehel JJ
Nature; 2020 Jul; 583(7814):150-153. PubMed ID: 32461688
[TBL] [Abstract][Full Text] [Related]
17. Fusion peptide of influenza hemagglutinin requires a fixed angle boomerang structure for activity.
Lai AL; Park H; White JM; Tamm LK
J Biol Chem; 2006 Mar; 281(9):5760-70. PubMed ID: 16407195
[TBL] [Abstract][Full Text] [Related]
18. 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; 174(4):926-937.e12. PubMed ID: 29961575
[TBL] [Abstract][Full Text] [Related]
19. 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; 60(35):2623-2636. PubMed ID: 34435771
[TBL] [Abstract][Full Text] [Related]
20. Factors determining vesicular lipid mixing induced by shortened constructs of influenza hemagglutinin.
LeDuc DL; Shin YK; Epand RF; Epand RM
Biochemistry; 2000 Mar; 39(10):2733-9. PubMed ID: 10704225
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
