메뉴 건너뛰기




Volumn 21, Issue 6, 2017, Pages 742-753.e8

Erratum: Diversity of Functionally Permissive Sequences in the Receptor-Binding Site of Influenza Hemagglutinin (Cell Host & Microbe (2017) 21(6) (742–753.e8) (S1931312817302044)(10.1016/j.chom.2017.05.011));Diversity of Functionally Permissive Sequences in the Receptor-Binding Site of Influenza Hemagglutinin

Author keywords

deep mutational scanning; epistasis; evolution; hemagglutinin; immune escape; influenza A virus; receptor binding site; sequence diversity; X ray crystallography

Indexed keywords

INFLUENZA VIRUS HEMAGGLUTININ; NEUTRALIZING ANTIBODY; VIRUS ANTIBODY; VIRUS ANTIGEN; VIRUS RECEPTOR;

EID: 85020729753     PISSN: 19313128     EISSN: 19346069     Source Type: Journal    
DOI: 10.1016/j.chom.2017.07.001     Document Type: Erratum
Times cited : (50)

References (72)
  • 1
    • 70849113337 scopus 로고    scopus 로고
    • Mutations in H5N1 influenza virus hemagglutinin that confer binding to human tracheal airway epithelium
    • Ayora-Talavera, G., Shelton, H., Scull, M.A., Ren, J., Jones, I.M., Pickles, R.J., Barclay, W.S., Mutations in H5N1 influenza virus hemagglutinin that confer binding to human tracheal airway epithelium. PLoS One, 4, 2009, e7836.
    • (2009) PLoS One , vol.4 , pp. e7836
    • Ayora-Talavera, G.1    Shelton, H.2    Scull, M.A.3    Ren, J.4    Jones, I.M.5    Pickles, R.J.6    Barclay, W.S.7
  • 2
    • 80052153094 scopus 로고    scopus 로고
    • The genomic rate of molecular adaptation of the human influenza A virus
    • Bhatt, S., Holmes, E.C., Pybus, O.G., The genomic rate of molecular adaptation of the human influenza A virus. Mol. Biol. Evol. 28 (2011), 2443–2451.
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 2443-2451
    • Bhatt, S.1    Holmes, E.C.2    Pybus, O.G.3
  • 3
    • 84905001681 scopus 로고    scopus 로고
    • An experimentally determined evolutionary model dramatically improves phylogenetic fit
    • Bloom, J.D., An experimentally determined evolutionary model dramatically improves phylogenetic fit. Mol. Biol. Evol. 31 (2014), 1956–1978.
    • (2014) Mol. Biol. Evol. , vol.31 , pp. 1956-1978
    • Bloom, J.D.1
  • 5
    • 84863774072 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies present new prospects to counter highly antigenically diverse viruses
    • Burton, D.R., Poignard, P., Stanfield, R.L., Wilson, I.A., Broadly neutralizing antibodies present new prospects to counter highly antigenically diverse viruses. Science 337 (2012), 183–186.
    • (2012) Science , vol.337 , pp. 183-186
    • Burton, D.R.1    Poignard, P.2    Stanfield, R.L.3    Wilson, I.A.4
  • 7
    • 0027988832 scopus 로고
    • Receptor specificity in human, avian, and equine H2 and H3 influenza virus isolates
    • Connor, R.J., Kawaoka, Y., Webster, R.G., Paulson, J.C., Receptor specificity in human, avian, and equine H2 and H3 influenza virus isolates. Virology 205 (1994), 17–23.
    • (1994) Virology , vol.205 , pp. 17-23
    • Connor, R.J.1    Kawaoka, Y.2    Webster, R.G.3    Paulson, J.C.4
  • 8
    • 84973131100 scopus 로고    scopus 로고
    • Accurate measurement of the effects of all amino-acid mutations on influenza hemagglutinin
    • Doud, M.B., Bloom, J.D., Accurate measurement of the effects of all amino-acid mutations on influenza hemagglutinin. Viruses, 8, 2016, E155.
    • (2016) Viruses , vol.8 , pp. E155
    • Doud, M.B.1    Bloom, J.D.2
  • 9
    • 40849097775 scopus 로고    scopus 로고
    • Rates of evolutionary change in viruses: patterns and determinants
    • Duffy, S., Shackelton, L.A., Holmes, E.C., Rates of evolutionary change in viruses: patterns and determinants. Nat. Rev. Genet. 9 (2008), 267–276.
    • (2008) Nat. Rev. Genet. , vol.9 , pp. 267-276
    • Duffy, S.1    Shackelton, L.A.2    Holmes, E.C.3
  • 13
    • 84905217368 scopus 로고    scopus 로고
    • Deep mutational scanning: a new style of protein science
    • Fowler, D.M., Fields, S., Deep mutational scanning: a new style of protein science. Nat. Methods 11 (2014), 801–807.
    • (2014) Nat. Methods , vol.11 , pp. 801-807
    • Fowler, D.M.1    Fields, S.2
  • 15
    • 30044433592 scopus 로고    scopus 로고
    • Evolution of the receptor binding phenotype of influenza A (H5) viruses
    • Gambaryan, A., Tuzikov, A., Pazynina, G., Bovin, N., Balish, A., Klimov, A., Evolution of the receptor binding phenotype of influenza A (H5) viruses. Virology 344 (2006), 432–438.
    • (2006) Virology , vol.344 , pp. 432-438
    • Gambaryan, A.1    Tuzikov, A.2    Pazynina, G.3    Bovin, N.4    Balish, A.5    Klimov, A.6
  • 18
    • 84884206086 scopus 로고    scopus 로고
    • Improving influenza virus backbones by including terminal regions of MDCK-adapted strains on hemagglutinin and neuraminidase gene segments
    • Gomila, R.C., Suphaphiphat, P., Judge, C., Spencer, T., Ferrari, A., Wen, Y., Palladino, G., Dormitzer, P.R., Mason, P.W., Improving influenza virus backbones by including terminal regions of MDCK-adapted strains on hemagglutinin and neuraminidase gene segments. Vaccine 31 (2013), 4736–4743.
    • (2013) Vaccine , vol.31 , pp. 4736-4743
    • Gomila, R.C.1    Suphaphiphat, P.2    Judge, C.3    Spencer, T.4    Ferrari, A.5    Wen, Y.6    Palladino, G.7    Dormitzer, P.R.8    Mason, P.W.9
  • 19
    • 84968903135 scopus 로고    scopus 로고
    • Coming of age: ten years of next-generation sequencing technologies
    • Goodwin, S., McPherson, J.D., McCombie, W.R., Coming of age: ten years of next-generation sequencing technologies. Nat. Rev. Genet. 17 (2016), 333–351.
    • (2016) Nat. Rev. Genet. , vol.17 , pp. 333-351
    • Goodwin, S.1    McPherson, J.D.2    McCombie, W.R.3
  • 20
    • 0035949581 scopus 로고    scopus 로고
    • X-ray structures of H5 avian and H9 swine influenza virus hemagglutinins bound to avian and human receptor analogs
    • Ha, Y., Stevens, D.J., Skehel, J.J., Wiley, D.C., X-ray structures of H5 avian and H9 swine influenza virus hemagglutinins bound to avian and human receptor analogs. Proc. Natl. Acad. Sci. USA 98 (2001), 11181–11186.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11181-11186
    • Ha, Y.1    Stevens, D.J.2    Skehel, J.J.3    Wiley, D.C.4
  • 21
    • 78650248582 scopus 로고    scopus 로고
    • Improved haemagglutinin antigen content in H5N1 candidate vaccine viruses with chimeric haemagglutinin molecules
    • Harvey, R., Nicolson, C., Johnson, R.E., Guilfoyle, K.A., Major, D.L., Robertson, J.S., Engelhardt, O.G., Improved haemagglutinin antigen content in H5N1 candidate vaccine viruses with chimeric haemagglutinin molecules. Vaccine 28 (2010), 8008–8014.
    • (2010) Vaccine , vol.28 , pp. 8008-8014
    • Harvey, R.1    Nicolson, C.2    Johnson, R.E.3    Guilfoyle, K.A.4    Major, D.L.5    Robertson, J.S.6    Engelhardt, O.G.7
  • 22
    • 79958156054 scopus 로고    scopus 로고
    • Improved antigen yield in pandemic H1N1 (2009) candidate vaccine viruses with chimeric hemagglutinin molecules
    • Harvey, R., Guilfoyle, K.A., Roseby, S., Robertson, J.S., Engelhardt, O.G., Improved antigen yield in pandemic H1N1 (2009) candidate vaccine viruses with chimeric hemagglutinin molecules. J. Virol. 85 (2011), 6086–6090.
    • (2011) J. Virol. , vol.85 , pp. 6086-6090
    • Harvey, R.1    Guilfoyle, K.A.2    Roseby, S.3    Robertson, J.S.4    Engelhardt, O.G.5
  • 23
    • 84921847141 scopus 로고    scopus 로고
    • Structural characterization of viral epitopes recognized by broadly cross-reactive antibodies
    • Lee, P.S., Wilson, I.A., Structural characterization of viral epitopes recognized by broadly cross-reactive antibodies. Curr. Top. Microbiol. Immunol. 386 (2015), 323–341.
    • (2015) Curr. Top. Microbiol. Immunol. , vol.386 , pp. 323-341
    • Lee, P.S.1    Wilson, I.A.2
  • 24
    • 84867641531 scopus 로고    scopus 로고
    • Heterosubtypic antibody recognition of the influenza virus hemagglutinin receptor binding site enhanced by avidity
    • Lee, P.S., Yoshida, R., Ekiert, D.C., Sakai, N., Suzuki, Y., Takada, A., Wilson, I.A., Heterosubtypic antibody recognition of the influenza virus hemagglutinin receptor binding site enhanced by avidity. Proc. Natl. Acad. Sci. USA 109 (2012), 17040–17045.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 17040-17045
    • Lee, P.S.1    Yoshida, R.2    Ekiert, D.C.3    Sakai, N.4    Suzuki, Y.5    Takada, A.6    Wilson, I.A.7
  • 25
    • 84931049237 scopus 로고    scopus 로고
    • Design and structure of an engineered disulfide-stabilized influenza virus hemagglutinin trimer
    • Lee, P.S., Zhu, X., Yu, W., Wilson, I.A., Design and structure of an engineered disulfide-stabilized influenza virus hemagglutinin trimer. J. Virol. 89 (2015), 7417–7420.
    • (2015) J. Virol. , vol.89 , pp. 7417-7420
    • Lee, P.S.1    Zhu, X.2    Yu, W.3    Wilson, I.A.4
  • 26
    • 0024292833 scopus 로고
    • Aromatic rings act as hydrogen bond acceptors
    • Levitt, M., Perutz, M.F., Aromatic rings act as hydrogen bond acceptors. J. Mol. Biol. 201 (1988), 751–754.
    • (1988) J. Mol. Biol. , vol.201 , pp. 751-754
    • Levitt, M.1    Perutz, M.F.2
  • 27
    • 77953315080 scopus 로고    scopus 로고
    • Neuraminidase receptor binding variants of human influenza A(H3N2) viruses resulting from substitution of aspartic acid 151 in the catalytic site: a role in virus attachment?
    • Lin, Y.P., Gregory, V., Collins, P., Kloess, J., Wharton, S., Cattle, N., Lackenby, A., Daniels, R., Hay, A., Neuraminidase receptor binding variants of human influenza A(H3N2) viruses resulting from substitution of aspartic acid 151 in the catalytic site: a role in virus attachment?. J. Virol. 84 (2010), 6769–6781.
    • (2010) J. Virol. , vol.84 , pp. 6769-6781
    • Lin, Y.P.1    Gregory, V.2    Collins, P.3    Kloess, J.4    Wharton, S.5    Cattle, N.6    Lackenby, A.7    Daniels, R.8    Hay, A.9
  • 31
    • 0030748536 scopus 로고    scopus 로고
    • Avian influenza A viruses differ from human viruses by recognition of sialyloligosaccharides and gangliosides and by a higher conservation of the HA receptor-binding site
    • Matrosovich, M.N., Gambaryan, A.S., Teneberg, S., Piskarev, V.E., Yamnikova, S.S., Lvov, D.K., Robertson, J.S., Karlsson, K.A., Avian influenza A viruses differ from human viruses by recognition of sialyloligosaccharides and gangliosides and by a higher conservation of the HA receptor-binding site. Virology 233 (1997), 224–234.
    • (1997) Virology , vol.233 , pp. 224-234
    • Matrosovich, M.N.1    Gambaryan, A.S.2    Teneberg, S.3    Piskarev, V.E.4    Yamnikova, S.S.5    Lvov, D.K.6    Robertson, J.S.7    Karlsson, K.A.8
  • 32
    • 0033856695 scopus 로고    scopus 로고
    • Early alterations of the receptor-binding properties of H1, H2, and H3 avian influenza virus hemagglutinins after their introduction into mammals
    • Matrosovich, M., Tuzikov, A., Bovin, N., Gambaryan, A., Klimov, A., Castrucci, M.R., Donatelli, I., Kawaoka, Y., Early alterations of the receptor-binding properties of H1, H2, and H3 avian influenza virus hemagglutinins after their introduction into mammals. J. Virol. 74 (2000), 8502–8512.
    • (2000) J. Virol. , vol.74 , pp. 8502-8512
    • Matrosovich, M.1    Tuzikov, A.2    Bovin, N.3    Gambaryan, A.4    Klimov, A.5    Castrucci, M.R.6    Donatelli, I.7    Kawaoka, Y.8
  • 33
    • 1842585032 scopus 로고    scopus 로고
    • Human and avian influenza viruses target different cell types in cultures of human airway epithelium
    • Matrosovich, M.N., Matrosovich, T.Y., Gray, T., Roberts, N.A., Klenk, H.D., Human and avian influenza viruses target different cell types in cultures of human airway epithelium. Proc. Natl. Acad. Sci. USA 101 (2004), 4620–4624.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 4620-4624
    • Matrosovich, M.N.1    Matrosovich, T.Y.2    Gray, T.3    Roberts, N.A.4    Klenk, H.D.5
  • 35
    • 0034099655 scopus 로고    scopus 로고
    • Balanced hemagglutinin and neuraminidase activities are critical for efficient replication of influenza A virus
    • Mitnaul, L.J., Matrosovich, M.N., Castrucci, M.R., Tuzikov, A.B., Bovin, N.V., Kobasa, D., Kawaoka, Y., Balanced hemagglutinin and neuraminidase activities are critical for efficient replication of influenza A virus. J. Virol. 74 (2000), 6015–6020.
    • (2000) J. Virol. , vol.74 , pp. 6015-6020
    • Mitnaul, L.J.1    Matrosovich, M.N.2    Castrucci, M.R.3    Tuzikov, A.B.4    Bovin, N.V.5    Kobasa, D.6    Kawaoka, Y.7
  • 39
    • 84923249936 scopus 로고    scopus 로고
    • A comprehensive biophysical description of pairwise epistasis throughout an entire protein domain
    • Olson, C.A., Wu, N.C., Sun, R., A comprehensive biophysical description of pairwise epistasis throughout an entire protein domain. Curr. Biol. 24 (2014), 2643–2651.
    • (2014) Curr. Biol. , vol.24 , pp. 2643-2651
    • Olson, C.A.1    Wu, N.C.2    Sun, R.3
  • 40
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., Minor, W., Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997), 307–326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 44
    • 77953718211 scopus 로고    scopus 로고
    • Sequence space and the ongoing expansion of the protein universe
    • Povolotskaya, I.S., Kondrashov, F.A., Sequence space and the ongoing expansion of the protein universe. Nature 465 (2010), 922–926.
    • (2010) Nature , vol.465 , pp. 922-926
    • Povolotskaya, I.S.1    Kondrashov, F.A.2
  • 45
    • 0020595851 scopus 로고
    • Single amino acid substitutions in influenza haemagglutinin change receptor binding specificity
    • Rogers, G.N., Paulson, J.C., Daniels, R.S., Skehel, J.J., Wilson, I.A., Wiley, D.C., Single amino acid substitutions in influenza haemagglutinin change receptor binding specificity. Nature 304 (1983), 76–78.
    • (1983) Nature , vol.304 , pp. 76-78
    • Rogers, G.N.1    Paulson, J.C.2    Daniels, R.S.3    Skehel, J.J.4    Wilson, I.A.5    Wiley, D.C.6
  • 46
    • 84885674874 scopus 로고    scopus 로고
    • Structures and receptor binding of hemagglutinins from human-infecting H7N9 influenza viruses
    • Shi, Y., Zhang, W., Wang, F., Qi, J., Wu, Y., Song, H., Gao, F., Bi, Y., Zhang, Y., Fan, Z., et al. Structures and receptor binding of hemagglutinins from human-infecting H7N9 influenza viruses. Science 342 (2013), 243–247.
    • (2013) Science , vol.342 , pp. 243-247
    • Shi, Y.1    Zhang, W.2    Wang, F.3    Qi, J.4    Wu, Y.5    Song, H.6    Gao, F.7    Bi, Y.8    Zhang, Y.9    Fan, Z.10
  • 47
    • 84911455217 scopus 로고    scopus 로고
    • Enabling the ‘host jump’: structural determinants of receptor-binding specificity in influenza A viruses
    • Shi, Y., Wu, Y., Zhang, W., Qi, J., Gao, G.F., Enabling the ‘host jump’: structural determinants of receptor-binding specificity in influenza A viruses. Nat. Rev. Microbiol. 12 (2014), 822–831.
    • (2014) Nat. Rev. Microbiol. , vol.12 , pp. 822-831
    • Shi, Y.1    Wu, Y.2    Zhang, W.3    Qi, J.4    Gao, G.F.5
  • 48
    • 33645278326 scopus 로고    scopus 로고
    • Avian flu: influenza virus receptors in the human airway
    • Shinya, K., Ebina, M., Yamada, S., Ono, M., Kasai, N., Kawaoka, Y., Avian flu: influenza virus receptors in the human airway. Nature 440 (2006), 435–436.
    • (2006) Nature , vol.440 , pp. 435-436
    • Shinya, K.1    Ebina, M.2    Yamada, S.3    Ono, M.4    Kasai, N.5    Kawaoka, Y.6
  • 49
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin
    • Skehel, J.J., Wiley, D.C., Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu. Rev. Biochem. 69 (2000), 531–569.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 50
    • 29444433087 scopus 로고    scopus 로고
    • Glycan microarray analysis of the hemagglutinins from modern and pandemic influenza viruses reveals different receptor specificities
    • Stevens, J., Blixt, O., Glaser, L., Taubenberger, J.K., Palese, P., Paulson, J.C., Wilson, I.A., Glycan microarray analysis of the hemagglutinins from modern and pandemic influenza viruses reveals different receptor specificities. J. Mol. Biol. 355 (2006), 1143–1155.
    • (2006) J. Mol. Biol. , vol.355 , pp. 1143-1155
    • Stevens, J.1    Blixt, O.2    Glaser, L.3    Taubenberger, J.K.4    Palese, P.5    Paulson, J.C.6    Wilson, I.A.7
  • 51
    • 33645981586 scopus 로고    scopus 로고
    • Structure and receptor specificity of the hemagglutinin from an H5N1 influenza virus
    • Stevens, J., Blixt, O., Tumpey, T.M., Taubenberger, J.K., Paulson, J.C., Wilson, I.A., Structure and receptor specificity of the hemagglutinin from an H5N1 influenza virus. Science 312 (2006), 404–410.
    • (2006) Science , vol.312 , pp. 404-410
    • Stevens, J.1    Blixt, O.2    Tumpey, T.M.3    Taubenberger, J.K.4    Paulson, J.C.5    Wilson, I.A.6
  • 52
    • 84905197658 scopus 로고    scopus 로고
    • The inherent mutational tolerance and antigenic evolvability of influenza hemagglutinin
    • Thyagarajan, B., Bloom, J.D., The inherent mutational tolerance and antigenic evolvability of influenza hemagglutinin. eLife, 3, 2014, e03300.
    • (2014) eLife , vol.3 , pp. e03300
    • Thyagarajan, B.1    Bloom, J.D.2
  • 54
    • 0031820967 scopus 로고    scopus 로고
    • The role of influenza A virus hemagglutinin residues 226 and 228 in receptor specificity and host range restriction
    • Vines, A., Wells, K., Matrosovich, M., Castrucci, M.R., Ito, T., Kawaoka, Y., The role of influenza A virus hemagglutinin residues 226 and 228 in receptor specificity and host range restriction. J. Virol. 72 (1998), 7626–7631.
    • (1998) J. Virol. , vol.72 , pp. 7626-7631
    • Vines, A.1    Wells, K.2    Matrosovich, M.3    Castrucci, M.R.4    Ito, T.5    Kawaoka, Y.6
  • 55
    • 84930871274 scopus 로고    scopus 로고
    • Adaptation of avian influenza A (H6N1) virus from avian to human receptor-binding preference
    • Wang, F., Qi, J., Bi, Y., Zhang, W., Wang, M., Zhang, B., Wang, M., Liu, J., Yan, J., Shi, Y., Gao, G.F., Adaptation of avian influenza A (H6N1) virus from avian to human receptor-binding preference. EMBO J. 34 (2015), 1661–1673.
    • (2015) EMBO J. , vol.34 , pp. 1661-1673
    • Wang, F.1    Qi, J.2    Bi, Y.3    Zhang, W.4    Wang, M.5    Zhang, B.6    Wang, M.7    Liu, J.8    Yan, J.9    Shi, Y.10    Gao, G.F.11
  • 56
    • 0141856265 scopus 로고    scopus 로고
    • Exploitation of nucleic acid packaging signals to generate a novel influenza virus-based vector stably expressing two foreign genes
    • Watanabe, T., Watanabe, S., Noda, T., Fujii, Y., Kawaoka, Y., Exploitation of nucleic acid packaging signals to generate a novel influenza virus-based vector stably expressing two foreign genes. J. Virol. 77 (2003), 10575–10583.
    • (2003) J. Virol. , vol.77 , pp. 10575-10583
    • Watanabe, T.1    Watanabe, S.2    Noda, T.3    Fujii, Y.4    Kawaoka, Y.5
  • 57
    • 21044435697 scopus 로고    scopus 로고
    • Perspective: sign epistasis and genetic constraint on evolutionary trajectories
    • Weinreich, D.M., Watson, R.A., Chao, L., Perspective: sign epistasis and genetic constraint on evolutionary trajectories. Evolution 59 (2005), 1165–1174.
    • (2005) Evolution , vol.59 , pp. 1165-1174
    • Weinreich, D.M.1    Watson, R.A.2    Chao, L.3
  • 58
    • 0023915219 scopus 로고
    • Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid
    • Weis, W., Brown, J.H., Cusack, S., Paulson, J.C., Skehel, J.J., Wiley, D.C., Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid. Nature 333 (1988), 426–431.
    • (1988) Nature , vol.333 , pp. 426-431
    • Weis, W.1    Brown, J.H.2    Cusack, S.3    Paulson, J.C.4    Skehel, J.J.5    Wiley, D.C.6
  • 59
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution
    • Wilson, I.A., Skehel, J.J., Wiley, D.C., Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution. Nature 289 (1981), 366–373.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 61
    • 84938795335 scopus 로고    scopus 로고
    • Functional constraint profiling of a viral protein reveals discordance of evolutionary conservation and functionality
    • Wu, N.C., Olson, C.A., Du, Y., Le, S., Tran, K., Remenyi, R., Gong, D., Al-Mawsawi, L.Q., Qi, H., Wu, T.T., Sun, R., Functional constraint profiling of a viral protein reveals discordance of evolutionary conservation and functionality. PLoS Genet., 11, 2015, e1005310.
    • (2015) PLoS Genet. , vol.11 , pp. e1005310
    • Wu, N.C.1    Olson, C.A.2    Du, Y.3    Le, S.4    Tran, K.5    Remenyi, R.6    Gong, D.7    Al-Mawsawi, L.Q.8    Qi, H.9    Wu, T.T.10    Sun, R.11
  • 62
    • 77951466468 scopus 로고    scopus 로고
    • Influenza H1N1 A/Solomon Island/3/06 virus receptor binding specificity correlates with virus pathogenicity, antigenicity, and immunogenicity in ferrets
    • Xu, Q., Wang, W., Cheng, X., Zengel, J., Jin, H., Influenza H1N1 A/Solomon Island/3/06 virus receptor binding specificity correlates with virus pathogenicity, antigenicity, and immunogenicity in ferrets. J. Virol. 84 (2010), 4936–4945.
    • (2010) J. Virol. , vol.84 , pp. 4936-4945
    • Xu, Q.1    Wang, W.2    Cheng, X.3    Zengel, J.4    Jin, H.5
  • 63
    • 75449093578 scopus 로고    scopus 로고
    • Structure, receptor binding, and antigenicity of influenza virus hemagglutinins from the 1957 H2N2 pandemic
    • Xu, R., McBride, R., Paulson, J.C., Basler, C.F., Wilson, I.A., Structure, receptor binding, and antigenicity of influenza virus hemagglutinins from the 1957 H2N2 pandemic. J. Virol. 84 (2010), 1715–1721.
    • (2010) J. Virol. , vol.84 , pp. 1715-1721
    • Xu, R.1    McBride, R.2    Paulson, J.C.3    Basler, C.F.4    Wilson, I.A.5
  • 64
    • 84856875534 scopus 로고    scopus 로고
    • Structural characterization of the hemagglutinin receptor specificity from the 2009 H1N1 influenza pandemic
    • Xu, R., McBride, R., Nycholat, C.M., Paulson, J.C., Wilson, I.A., Structural characterization of the hemagglutinin receptor specificity from the 2009 H1N1 influenza pandemic. J. Virol. 86 (2012), 982–990.
    • (2012) J. Virol. , vol.86 , pp. 982-990
    • Xu, R.1    McBride, R.2    Nycholat, C.M.3    Paulson, J.C.4    Wilson, I.A.5
  • 65
    • 84866181427 scopus 로고    scopus 로고
    • Functional balance of the hemagglutinin and neuraminidase activities accompanies the emergence of the 2009 H1N1 influenza pandemic
    • Xu, R., Zhu, X., McBride, R., Nycholat, C.M., Yu, W., Paulson, J.C., Wilson, I.A., Functional balance of the hemagglutinin and neuraminidase activities accompanies the emergence of the 2009 H1N1 influenza pandemic. J. Virol. 86 (2012), 9221–9232.
    • (2012) J. Virol. , vol.86 , pp. 9221-9232
    • Xu, R.1    Zhu, X.2    McBride, R.3    Nycholat, C.M.4    Yu, W.5    Paulson, J.C.6    Wilson, I.A.7
  • 68
    • 78149344653 scopus 로고    scopus 로고
    • Structures of receptor complexes of a North American H7N2 influenza hemagglutinin with a loop deletion in the receptor binding site
    • Yang, H., Chen, L.M., Carney, P.J., Donis, R.O., Stevens, J., Structures of receptor complexes of a North American H7N2 influenza hemagglutinin with a loop deletion in the receptor binding site. PLoS Pathog., 6, 2010, e1001081.
    • (2010) PLoS Pathog. , vol.6 , pp. e1001081
    • Yang, H.1    Chen, L.M.2    Carney, P.J.3    Donis, R.O.4    Stevens, J.5
  • 69
    • 84921482027 scopus 로고    scopus 로고
    • Structure and receptor binding preferences of recombinant human A(H3N2) virus hemagglutinins
    • Yang, H., Carney, P.J., Chang, J.C., Guo, Z., Villanueva, J.M., Stevens, J., Structure and receptor binding preferences of recombinant human A(H3N2) virus hemagglutinins. Virology 477 (2015), 18–31.
    • (2015) Virology , vol.477 , pp. 18-31
    • Yang, H.1    Carney, P.J.2    Chang, J.C.3    Guo, Z.4    Villanueva, J.M.5    Stevens, J.6
  • 70
    • 63449125762 scopus 로고    scopus 로고
    • Cross-protective potential of a novel monoclonal antibody directed against antigenic site B of the hemagglutinin of influenza A viruses
    • Yoshida, R., Igarashi, M., Ozaki, H., Kishida, N., Tomabechi, D., Kida, H., Ito, K., Takada, A., Cross-protective potential of a novel monoclonal antibody directed against antigenic site B of the hemagglutinin of influenza A viruses. PLoS Pathog., 5, 2009, e1000350.
    • (2009) PLoS Pathog. , vol.5 , pp. e1000350
    • Yoshida, R.1    Igarashi, M.2    Ozaki, H.3    Kishida, N.4    Tomabechi, D.5    Kida, H.6    Ito, K.7    Takada, A.8
  • 71
    • 84957868538 scopus 로고    scopus 로고
    • A benchmark study on error-correction by read-pairing and tag-clustering in amplicon-based deep sequencing
    • Zhang, T.H., Wu, N.C., Sun, R., A benchmark study on error-correction by read-pairing and tag-clustering in amplicon-based deep sequencing. BMC Genomics, 17, 2016, 108.
    • (2016) BMC Genomics , vol.17 , pp. 108
    • Zhang, T.H.1    Wu, N.C.2    Sun, R.3
  • 72
    • 84952871165 scopus 로고    scopus 로고
    • Structural basis for a switch in receptor binding specificity of two H5N1 hemagglutinin mutants
    • Zhu, X., Viswanathan, K., Raman, R., Yu, W., Sasisekharan, R., Wilson, I.A., Structural basis for a switch in receptor binding specificity of two H5N1 hemagglutinin mutants. Cell Rep. 13 (2015), 1683–1691.
    • (2015) Cell Rep. , vol.13 , pp. 1683-1691
    • Zhu, X.1    Viswanathan, K.2    Raman, R.3    Yu, W.4    Sasisekharan, R.5    Wilson, I.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.