Literature DB >> 17718569

Solid-state NMR structural measurements on the membrane-associated influenza fusion protein ectodomain.

Jaime Curtis-Fisk1, Casey Preston, Zhaoxiong Zheng, R Mark Worden, David P Weliky.   

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Year:  2007        PMID: 17718569     DOI: 10.1021/ja073644g

Source DB:  PubMed          Journal:  J Am Chem Soc        ISSN: 0002-7863            Impact factor:   15.419


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  12 in total

Review 1.  Towards revealing the structure of bacterial inclusion bodies.

Authors:  Lei Wang
Journal:  Prion       Date:  2009-07-25       Impact factor: 3.931

2.  HIV gp41 six-helix bundle constructs induce rapid vesicle fusion at pH 3.5 and little fusion at pH 7.0: understanding pH dependence of protein aggregation, membrane binding, and electrostatics, and implications for HIV-host cell fusion.

Authors:  Kelly Sackett; Allan TerBush; David P Weliky
Journal:  Eur Biophys J       Date:  2011-01-11       Impact factor: 1.733

3.  Closed and Semiclosed Interhelical Structures in Membrane vs Closed and Open Structures in Detergent for the Influenza Virus Hemagglutinin Fusion Peptide and Correlation of Hydrophobic Surface Area with Fusion Catalysis.

Authors:  Ujjayini Ghosh; Li Xie; Lihui Jia; Shuang Liang; David P Weliky
Journal:  J Am Chem Soc       Date:  2015-06-10       Impact factor: 15.419

4.  Solid-state nuclear magnetic resonance (NMR) spectroscopy of human immunodeficiency virus gp41 protein that includes the fusion peptide: NMR detection of recombinant Fgp41 in inclusion bodies in whole bacterial cells and structural characterization of purified and membrane-associated Fgp41.

Authors:  Erica P Vogel; Jaime Curtis-Fisk; Kaitlin M Young; David P Weliky
Journal:  Biochemistry       Date:  2011-10-31       Impact factor: 3.162

5.  Full-length trimeric influenza virus hemagglutinin II membrane fusion protein and shorter constructs lacking the fusion peptide or transmembrane domain: Hyperthermostability of the full-length protein and the soluble ectodomain and fusion peptide make significant contributions to fusion of membrane vesicles.

Authors:  Punsisi U Ratnayake; E A Prabodha Ekanayaka; Sweta S Komanduru; David P Weliky
Journal:  Protein Expr Purif       Date:  2015-08-19       Impact factor: 1.650

6.  Quantitation of recombinant protein in whole cells and cell extracts via solid-state NMR spectroscopy.

Authors:  Erica P Vogel; David P Weliky
Journal:  Biochemistry       Date:  2013-06-17       Impact factor: 3.162

7.  The final conformation of the complete ectodomain of the HA2 subunit of influenza hemagglutinin can by itself drive low pH-dependent fusion.

Authors:  Chang Sup Kim; Raquel F Epand; Eugenia Leikina; Richard M Epand; Leonid V Chernomordik
Journal:  J Biol Chem       Date:  2011-02-03       Impact factor: 5.157

8.  Detection of closed influenza virus hemagglutinin fusion peptide structures in membranes by backbone (13)CO- (15)N rotational-echo double-resonance solid-state NMR.

Authors:  Ujjayini Ghosh; Li Xie; David P Weliky
Journal:  J Biomol NMR       Date:  2013-01-18       Impact factor: 2.835

9.  The Stabilities of the Soluble Ectodomain and Fusion Peptide Hairpins of the Influenza Virus Hemagglutinin Subunit II Protein Are Positively Correlated with Membrane Fusion.

Authors:  Ahinsa Ranaweera; Punsisi U Ratnayake; David P Weliky
Journal:  Biochemistry       Date:  2018-09-05       Impact factor: 3.162

10.  Hairpin folding of HIV gp41 abrogates lipid mixing function at physiologic pH and inhibits lipid mixing by exposed gp41 constructs.

Authors:  Kelly Sackett; Matthew J Nethercott; Yechiel Shai; David P Weliky
Journal:  Biochemistry       Date:  2009-03-31       Impact factor: 3.162

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