메뉴 건너뛰기




Volumn 287, Issue 29, 2012, Pages 24239-24254

Partial enzymatic deglycosylation preserves the structure of cleaved recombinant HIV-1 envelope glycoprotein trimers

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODIES; DISEASES; EPITOPES; GLYCOPROTEINS; POLYSACCHARIDES; VIRUSES;

EID: 84863788697     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.371898     Document Type: Article
Times cited : (45)

References (84)
  • 2
    • 0018265515 scopus 로고
    • The synthesis of complex-type oligosaccharides. II. Characterization of the processing intermediates in the synthesis of the complex oligosaccharide units of the vesicular stomatitis virus G protein
    • Kornfeld, S., Li, E., and Tabas, I. (1978) The synthesis of complex-type oligosaccharides. II. Characterization of the processing intermediates in the synthesis of the complex oligosaccharide units of the vesicular stomatitis virus G protein. J. Biol. Chem. 253, 7771-7778
    • (1978) J. Biol. Chem. , vol.253 , pp. 7771-7778
    • Kornfeld, S.1    Li, E.2    Tabas, I.3
  • 3
    • 45549101708 scopus 로고    scopus 로고
    • Glycosylation site-specific analysis of HIV envelope proteins (JR-FL and CON-S) reveals major differences in glycosylation site occupancy, glycoform profiles, and antigenic epitopes' accessibility
    • Go, E. P., Irungu, J., Zhang, Y., Dalpathado, D. S., Liao, H. X., Sutherland, L. L., Alam, S. M., Haynes, B. F., and Desaire, H. (2008) Glycosylation site-specific analysis of HIV envelope proteins (JR-FL and CON-S) reveals major differences in glycosylation site occupancy, glycoform profiles, and antigenic epitopes' accessibility. J. Proteome Res. 7, 1660-1674
    • (2008) J. Proteome Res. , vol.7 , pp. 1660-1674
    • Go, E.P.1    Irungu, J.2    Zhang, Y.3    Dalpathado, D.S.4    Liao, H.X.5    Sutherland, L.L.6    Alam, S.M.7    Haynes, B.F.8    Desaire, H.9
  • 5
    • 33748925430 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 V1-V2 envelope loop sequences expand and add glycosylation sites over the course of infection, and these modifications affect antibody neutralization sensitivity
    • DOI 10.1128/JVI.00141-06
    • Sagar, M., Wu, X., Lee, S., and Overbaugh, J. (2006) Human immunodeficiency virus type 1 V1-V2 envelope loop sequences expand and add glycosylation sites over the course of infection, and these modifications affect antibody neutralization sensitivity. J. Virol. 80, 9586-9598 (Pubitemid 44435633)
    • (2006) Journal of Virology , vol.80 , Issue.19 , pp. 9586-9598
    • Sagar, M.1    Wu, X.2    Lee, S.3    Overbaugh, J.4
  • 7
    • 0032520597 scopus 로고    scopus 로고
    • Role of gp41 glycosylation sites in the biological activity of human immunodeficiency virus type 1 envelope glycoprotein
    • DOI 10.1006/viro.1997.9016
    • Perrin, C., Fenouillet, E., and Jones, I. M. (1998) Role of gp41 glycosylation sites in the biological activity of human immunodeficiency virus type 1 envelope glycoprotein. Virology 242, 338-345 (Pubitemid 28414739)
    • (1998) Virology , vol.242 , Issue.2 , pp. 338-345
    • Perrin, C.1    Fenouillet, E.2    Jones, I.M.3
  • 8
    • 0024549386 scopus 로고
    • Role of N-linked glycans in the interaction between the envelope glycoprotein of human immunodeficiency virus and its CD4 cellular receptor. Structural enzymatic analysis
    • DOI 10.1084/jem.169.3.807
    • Fenouillet, E., Clerget-Raslain, B., Gluckman, J. C., Guétard, D., Montagnier, L., and Bahraoui, E. (1989) Role ofN-linked glycans in the interaction between the envelope glycoprotein of human immunodeficiency virus and its CD4 cellular receptor. Structural enzymatic analysis. J. Exp. Med. 169, 807-822 (Pubitemid 19085822)
    • (1989) Journal of Experimental Medicine , vol.169 , Issue.3 , pp. 807-822
    • Fenouillet, E.1    Clerget-Raslain, B.2    Gluckman, J.C.3    Guetard, D.4    Montagnier, L.5    Bahraoui, E.6
  • 9
    • 78650050006 scopus 로고    scopus 로고
    • Simian immunodeficiency virus from the sooty mangabey and rhesus macaque is modified with O-linked carbohydrate
    • Stansell, E., Canis, K., Haslam, S. M., Dell, A., and Desrosiers, R. C. (2011) Simian immunodeficiency virus from the sooty mangabey and rhesus macaque is modified with O-linked carbohydrate. J. Virol. 85, 582-595
    • (2011) J. Virol. , vol.85 , pp. 582-595
    • Stansell, E.1    Canis, K.2    Haslam, S.M.3    Dell, A.4    Desrosiers, R.C.5
  • 10
    • 79953134012 scopus 로고    scopus 로고
    • Functional contributions of carbohydrate on AIDS virus glycoprotein
    • Stansell, E., and Desrosiers, R. C. (2010) Functional contributions of carbohydrate on AIDS virus glycoprotein. Yale J. Biol. Med. 83, 201-208
    • (2010) Yale J. Biol. Med. , vol.83 , pp. 201-208
    • Stansell, E.1    Desrosiers, R.C.2
  • 11
    • 0028784556 scopus 로고
    • Sialic acid-binding lectins. Submolecular specificity and interaction with sialoglycoproteins and tumor cells
    • Fischer, E., and Brossmer, R. (1995) Sialic acid-binding lectins. Submolecular specificity and interaction with sialoglycoproteins and tumor cells. Glycoconj. J. 12, 707-713
    • (1995) Glycoconj. J. , vol.12 , pp. 707-713
    • Fischer, E.1    Brossmer, R.2
  • 12
    • 0025331559 scopus 로고
    • Role of N-linked glycans of envelope glycoproteins in infectivity of human immunodeficiency virus type 1
    • Fenouillet, E., Gluckman, J. C., and Bahraoui, E. (1990) Role of N-linked glycans of envelope glycoproteins in infectivity of human immunodeficiency virus type 1. J. Virol. 64, 2841-2848 (Pubitemid 20171274)
    • (1990) Journal of Virology , vol.64 , Issue.6 , pp. 2841-2848
    • Fenouillet, E.1    Gluckman, J.C.2    Bahraoui, E.3
  • 14
    • 77952001983 scopus 로고    scopus 로고
    • Role of complex carbohydrates in human immunodeficiency virus type 1 infection and resistance to antibody neutralization
    • Binley, J. M., Ban, Y. E., Crooks, E. T., Eggink, D., Osawa, K., Schief, W. R., and Sanders, R. W. (2010) Role of complex carbohydrates in human immunodeficiency virus type 1 infection and resistance to antibody neutralization. J. Virol. 84, 5637-5655
    • (2010) J. Virol. , vol.84 , pp. 5637-5655
    • Binley, J.M.1    Ban, Y.E.2    Crooks, E.T.3    Eggink, D.4    Osawa, K.5    Schief, W.R.6    Sanders, R.W.7
  • 16
    • 0027418038 scopus 로고
    • Complement-mediated binding of naturally glycosylated and glycosylation- modified human immunodeficiency virus type 1 to human CR2 (CD21)
    • Montefiori, D. C., Stewart, K., Ahearn, J. M., Zhou, J., and Zhou, J. (1993) Complement-mediated binding of naturally glycosylated and glycosylation-modified human immunodeficiency virus type 1 to human CR2 (CD21). J. Virol. 67, 2699-2706 (Pubitemid 23118867)
    • (1993) Journal of Virology , vol.67 , Issue.5 , pp. 2699-2706
    • Montefiori, D.C.1    Stewart, K.2    Ahearn, J.M.3    Zhou, J.4    Zhou, J.5
  • 17
    • 0034469405 scopus 로고    scopus 로고
    • Resistance of native, oligomeric envelope on simian immunodeficiency virus to digestion by glycosidases
    • DOI 10.1128/JVI.74.23.11181-11190.2000
    • Means, R. E., and Desrosiers, R. C. (2000) Resistance of native, oligomeric envelope on simian immunodeficiency virus to digestion by glycosidases. J. Virol. 74, 11181-11190 (Pubitemid 32223985)
    • (2000) Journal of Virology , vol.74 , Issue.23 , pp. 11181-11190
    • Means, R.E.1    Desrosiers, R.C.2
  • 18
    • 0034598934 scopus 로고    scopus 로고
    • Identification of DC-SIGN, a novel dendritic cell-specific ICAM-3 receptor that supports primary immune responses
    • Geijtenbeek, T. B., Torensma, R., van Vliet, S. J., van Duijnhoven, G. C., Adema, G. J., van Kooyk, Y., and Figdor, C. G. (2000) Identification of DC-SIGN, a novel dendritic cell-specific ICAM-3 receptor that supports primary immune responses. Cell 100, 575-585
    • (2000) Cell , vol.100 , pp. 575-585
    • Geijtenbeek, T.B.1    Torensma, R.2    Van Vliet, S.J.3    Van Duijnhoven, G.C.4    Adema, G.J.5    Van Kooyk, Y.6    Figdor, C.G.7
  • 19
    • 35548993574 scopus 로고    scopus 로고
    • Modulation of HIV and SIV neutralization sensitivity by DC-SIGN and mannose-binding lectin
    • DOI 10.1016/j.virol.2007.07.004, PII S0042682207004722
    • Marzi, A., Mitchell, D. A., Chaipan, C., Fisch, T., Doms, R. W., Carrington, M., Desrosiers, R. C., and Pöhlmann, S. (2007) Modulation of HIV and SIV neutralization sensitivity by DC-SIGN and mannose-binding lectin. Virology 368, 322-330 (Pubitemid 350016227)
    • (2007) Virology , vol.368 , Issue.2 , pp. 322-330
    • Marzi, A.1    Mitchell, D.A.2    Chaipan, C.3    Fisch, T.4    Doms, R.W.5    Carrington, M.6    Desrosiers, R.C.7    Pohlmann, S.8
  • 23
    • 0031749469 scopus 로고    scopus 로고
    • A role for carbohydrates in immune evasion in AIDS
    • DOI 10.1038/nm0698-679
    • Reitter, J. N., Means, R. E., and Desrosiers, R. C. (1998) A role for carbohydrates in immune evasion in AIDS. Nat. Med. 4, 679-684 (Pubitemid 28274667)
    • (1998) Nature Medicine , vol.4 , Issue.6 , pp. 679-684
    • Reitter, J.N.1    Means, R.E.2    Desrosiers, R.C.3
  • 24
    • 84863395948 scopus 로고    scopus 로고
    • How can HIV type 1-Env immunogenicity be improved to facilitate antibody-based vaccine development?
    • Klasse, P. J., Sanders, R. W., Cerutti, A., and Moore, J. P. (2012) How can HIV type 1-Env immunogenicity be improved to facilitate antibody-based vaccine development? AIDS Res. Hum. Retroviruses 28, 1-15
    • (2012) AIDS Res. Hum. Retroviruses , vol.28 , pp. 1-15
    • Klasse, P.J.1    Sanders, R.W.2    Cerutti, A.3    Moore, J.P.4
  • 27
    • 33646146379 scopus 로고    scopus 로고
    • GP120. Target for neutralizing HIV-1 antibodies
    • Pantophlet, R., and Burton, D. R. (2006) GP120. Target for neutralizing HIV-1 antibodies. Annu. Rev. Immunol. 24, 739-769
    • (2006) Annu. Rev. Immunol. , vol.24 , pp. 739-769
    • Pantophlet, R.1    Burton, D.R.2
  • 30
    • 77958115264 scopus 로고    scopus 로고
    • A limited number of antibody specificities mediate broad and potent serum neutralization in selected HIV-1 infected individuals
    • Walker, L. M., Simek, M. D., Priddy, F., Gach, J. S., Wagner, D., Zwick, M. B., Phogat, S. K., Poignard, P., Burton, D. R. (2010) A limited number of antibody specificities mediate broad and potent serum neutralization in selected HIV-1 infected individuals. PLoS Pathog. 6, e1001028
    • (2010) PLoS Pathog. , vol.6
    • Walker, L.M.1    Simek, M.D.2    Priddy, F.3    Gach, J.S.4    Wagner, D.5    Zwick, M.B.6    Phogat, S.K.7    Poignard, P.8    Burton, D.R.9
  • 33
    • 18244422922 scopus 로고    scopus 로고
    • The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of →132 mannose residues on the outer face of gp120
    • Scanlan, C. N., Pantophlet, R., Wormald, M. R., Ollmann Saphire, E., Stanfield, R., Wilson, I. A., Katinger, H., Dwek, R. A., Rudd, P. M., and Burton, D. R. (2002) The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of →132 mannose residues on the outer face of gp120. J. Virol. 76, 7306-7321
    • (2002) J. Virol. , vol.76 , pp. 7306-7321
    • Scanlan, C.N.1    Pantophlet, R.2    Wormald, M.R.3    Ollmann Saphire, E.4    Stanfield, R.5    Wilson, I.A.6    Katinger, H.7    Dwek, R.A.8    Rudd, P.M.9    Burton, D.R.10
  • 34
    • 0036637385 scopus 로고    scopus 로고
    • The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120
    • Sanders, R. W., Venturi, M., Schiffner, L., Kalyanaraman, R., Katinger, H., Lloyd, K. O., Kwong, P. D., and Moore, J. P. (2002) The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120. J. Virol. 76, 7293-7305
    • (2002) J. Virol. , vol.76 , pp. 7293-7305
    • Sanders, R.W.1    Venturi, M.2    Schiffner, L.3    Kalyanaraman, R.4    Katinger, H.5    Lloyd, K.O.6    Kwong, P.D.7    Moore, J.P.8
  • 35
    • 77957198704 scopus 로고    scopus 로고
    • Variable loop glycan dependency of the broad and potent HIV-1-neutralizing antibodies PG9 and PG16
    • Doores, K. J., and Burton, D. R. (2010) Variable loop glycan dependency of the broad and potent HIV-1-neutralizing antibodies PG9 and PG16. J. Virol. 84, 10510-10521
    • (2010) J. Virol. , vol.84 , pp. 10510-10521
    • Doores, K.J.1    Burton, D.R.2
  • 38
    • 0033548254 scopus 로고    scopus 로고
    • Probability analysis of variational crystallization and its application to gp120, the exterior envelope glycoprotein of type 1 human immunodeficiency virus (HIV-1)
    • Kwong, P. D., Wyatt, R., Desjardins, E., Robinson, J., Culp, J. S., Hellmig, B. D., Sweet, R. W., Sodroski, J., and Hendrickson, W. A. (1999) Probability analysis of variational crystallization and its application to gp120, the exterior envelope glycoprotein of type 1 human immunodeficiency virus (HIV-1). J. Biol. Chem. 274, 4115-4123
    • (1999) J. Biol. Chem. , vol.274 , pp. 4115-4123
    • Kwong, P.D.1    Wyatt, R.2    Desjardins, E.3    Robinson, J.4    Culp, J.S.5    Hellmig, B.D.6    Sweet, R.W.7    Sodroski, J.8    Hendrickson, W.A.9
  • 42
    • 79958086672 scopus 로고    scopus 로고
    • Enzyme digests eliminate nonfunctional Env from HIV-1 particle surfaces, leaving native Env trimers intact and viral infectivity unaffected
    • Crooks, E. T., Tong, T., Osawa, K., and Binley, J. M. (2011) Enzyme digests eliminate nonfunctional Env from HIV-1 particle surfaces, leaving native Env trimers intact and viral infectivity unaffected. J. Virol. 85, 5825-5839
    • (2011) J. Virol. , vol.85 , pp. 5825-5839
    • Crooks, E.T.1    Tong, T.2    Osawa, K.3    Binley, J.M.4
  • 44
    • 0033985999 scopus 로고    scopus 로고
    • A recombinant human immunodeficiency virus type 1 envelope glycoprotein complex stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion-associated structure
    • DOI 10.1128/JVI.74.2.627-643.2000
    • Binley, J. M., Sanders, R. W., Clas, B., Schuelke, N., Master, A., Guo, Y., Kajumo, F., Anselma, D. J., Maddon, P. J., Olson, W. C., and Moore, J. P. (2000) A recombinant human immunodeficiency virus type 1 envelope glycoprotein complex stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion-associated structure. J. Virol. 74, 627-643 (Pubitemid 30036198)
    • (2000) Journal of Virology , vol.74 , Issue.2 , pp. 627-643
    • Binley, J.M.1    Sanders, R.W.2    Clas, B.3    Schuelke, N.4    Master, A.5    Guo, Y.6    Kajumo, F.7    Anselma, D.J.8    Maddon, P.J.9    Olson, W.C.10    Moore, J.P.11
  • 47
    • 60349105588 scopus 로고    scopus 로고
    • Biochemical and biophysical comparison of cleaved and uncleaved soluble, trimeric HIV-1 envelope glycoproteins
    • Dey, A. K., David, K. B., Lu, M., and Moore, J. P. (2009) Biochemical and biophysical comparison of cleaved and uncleaved soluble, trimeric HIV-1 envelope glycoproteins. Virology 385, 275-281
    • (2009) Virology , vol.385 , pp. 275-281
    • Dey, A.K.1    David, K.B.2    Lu, M.3    Moore, J.P.4
  • 49
    • 33947590277 scopus 로고    scopus 로고
    • A comparative immunogenicity study in rabbits of disulfide-stabilized, proteolytically cleaved, soluble trimeric human immunodeficiency virus type 1 gp140, trimeric cleavage-defective gp140 and monomeric gp120
    • DOI 10.1016/j.virol.2006.10.032, PII S0042682206007884
    • Beddows, S., Franti, M., Dey, A. K., Kirschner, M., Iyer, S. P., Fisch, D. C., Ketas, T., Yuste, E., Desrosiers, R. C., Klasse, P. J., Maddon, P. J., Olson, W. C., and Moore, J. P. (2007) A comparative immunogenicity study in rabbits of disulfide-stabilized, proteolytically cleaved, soluble trimeric human immunodeficiency virus type 1 gp140, trimeric cleavage-defective gp140 and monomeric gp120. Virology 360, 329-340 (Pubitemid 46482615)
    • (2007) Virology , vol.360 , Issue.2 , pp. 329-340
    • Beddows, S.1    Franti, M.2    Dey, A.K.3    Kirschner, M.4    Iyer, S.P.N.5    Fisch, D.C.6    Ketas, T.7    Yuste, E.8    Desrosiers, R.C.9    Klasse, P.J.10    Maddon, P.J.11    Olson, W.C.12    Moore, J.P.13
  • 51
    • 21644445378 scopus 로고    scopus 로고
    • Evaluating the immunogenicity of a disulfide-stabilized, cleaved, trimeric form of the envelope glycoprotein complex of human immunodeficiency virus type 1
    • DOI 10.1128/JVI.79.14.8812-8827.2005
    • Beddows, S., Schülke, N., Kirschner, M., Barnes, K., Franti, M., Michael, E., Ketas, T., Sanders, R. W., Maddon, P. J., Olson, W. C., and Moore, J. P. (2005) Evaluating the immunogenicity of a disulfide-stabilized, cleaved, trimeric form of the envelope glycoprotein complex of human immunodeficiency virus type 1. J. Virol. 79, 8812-8827 (Pubitemid 40934792)
    • (2005) Journal of Virology , vol.79 , Issue.14 , pp. 8812-8827
    • Beddows, S.1    Schulke, N.2    Kirschner, M.3    Barnes, K.4    Franti, M.5    Michael, E.6    Ketas, T.7    Sanders, R.W.8    Maddon, P.J.9    Olson, W.C.10    Moore, J.P.11
  • 55
    • 0037109080 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: A tetracycline-inducible system in stable mammalian cell lines for high-level expression of opsin mutants
    • DOI 10.1073/pnas.212519199
    • Reeves, P. J., Kim, J. M., and Khorana, H. G. (2002) Structure and function in rhodopsin. A tetracycline-inducible system in stable mammalian cell lines for high-level expression of opsin mutants. Proc. Natl. Acad. Sci. U.S.A. 99, 13413-13418 (Pubitemid 35215395)
    • (2002) Proceedings of the National Academy of Sciences of the United States of America , vol.99 , Issue.21 , pp. 13413-13418
    • Reeves, P.J.1    Kim, J.-M.2    Khorana, H.G.3
  • 56
    • 33646867165 scopus 로고    scopus 로고
    • The production of cleaved, trimeric human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein vaccine antigens and infectious pseudoviruses using linear polyethylenimine as a transfection reagent
    • DOI 10.1016/j.pep.2006.02.017, PII S1046592806000702
    • Kirschner, M., Monrose, V., Paluch, M., Techodamrongsin, N., Rethwilm, A., and Moore, J. P. (2006) The production of cleaved, trimeric human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein vaccine antigens and infectious pseudoviruses using linear polyethylenimine as a transfection reagent. Protein Expr. Purif. 48, 61-68 (Pubitemid 43782633)
    • (2006) Protein Expression and Purification , vol.48 , Issue.1 , pp. 61-68
    • Kirschner, M.1    Monrose, V.2    Paluch, M.3    Techodamrongsin, N.4    Rethwilm, A.5    Moore, J.P.6
  • 57
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schägger, H., and von Jagow, G. (1991) Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem. 199, 223-231
    • (1991) Anal. Biochem. , vol.199 , pp. 223-231
    • Schägger, H.1    Von Jagow, G.2
  • 58
    • 0030571043 scopus 로고    scopus 로고
    • Size-exclusion chromatography with on-line light-scattering, absorbance, and refractive index detectors for studying proteins and their interactions
    • DOI 10.1006/abio.1996.0345
    • Wen, J., Arakawa, T., and Philo, J. S. (1996) Size-exclusion chromatography with on-line light-scattering, absorbance, and refractive index detectors for studying proteins and their interactions. Anal. Biochem. 240, 155-166 (Pubitemid 26304259)
    • (1996) Analytical Biochemistry , vol.240 , Issue.2 , pp. 155-166
    • Wen, J.1    Arakawa, T.2    Philo, J.S.3
  • 59
    • 0035894369 scopus 로고    scopus 로고
    • Determination of carbohydrate contents from excess light scattering
    • DOI 10.1006/abio.2001.5432
    • Arakawa, T., and Wen, J. (2001) Determination of carbohydrate contents from excess light scattering. Anal. Biochem. 299, 158-161 (Pubitemid 34053404)
    • (2001) Analytical Biochemistry , vol.299 , Issue.2 , pp. 158-161
    • Arakawa, T.1    Wen, J.2
  • 60
    • 0035894420 scopus 로고    scopus 로고
    • Online size-exclusion high-performance liquid chromatography light scattering and differential refractometry methods to determine degree of polymer conjugation to proteins and protein-protein or protein-ligand association states
    • DOI 10.1006/abio.2001.5411
    • Kendrick, B. S., Kerwin, B. A., Chang, B. S., and Philo, J. S. (2001) Online size-exclusion high-performance liquid chromatography light scattering and differential refractometry methods to determine degree of polymer conjugation to proteins and protein-protein or protein-ligand association states. Anal. Biochem. 299, 136-146 (Pubitemid 34053402)
    • (2001) Analytical Biochemistry , vol.299 , Issue.2 , pp. 136-146
    • Kendrick, B.S.1    Kerwin, B.A.2    Chang, B.S.3    Philo, J.S.4
  • 62
    • 63649113687 scopus 로고    scopus 로고
    • DoG Picker and TiltPicker. Software tools to facilitate particle selection in single particle electron microscopy
    • Voss, N. R., Yoshioka, C. K., Radermacher, M., Potter, C. S, and Carragher, B. (2009) DoG Picker and TiltPicker. Software tools to facilitate particle selection in single particle electron microscopy. J. Struct. Biol. 166, 205-213
    • (2009) J. Struct. Biol. , vol.166 , pp. 205-213
    • Voss, N.R.1    Yoshioka, C.K.2    Radermacher, M.3    Potter, C.S.4    Carragher, B.5
  • 63
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • DOI 10.1016/S1047-8477(03)00069-8
    • Mindell, J. A., and Grigorieff, N. (2003) Accurate determination of local defocus and specimen tilt in electron microscopy. J. Struct. Biol. 142, 334-347 (Pubitemid 36638267)
    • (2003) Journal of Structural Biology , vol.142 , Issue.3 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 64
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • DOI 10.1006/jsbi.1999.4174
    • Ludtke, S. J., Baldwin, P. R., and Chiu, W. (1999) EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol.128, 82-97 (Pubitemid 30013436)
    • (1999) Journal of Structural Biology , vol.128 , Issue.1 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 65
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: An extensible image processing suite for electron microscopy
    • DOI 10.1016/j.jsb.2006.05.009, PII S1047847706001894, Software Tools for Macromolecular Microscopy
    • Tang, G., Peng, L., Baldwin, P. R., Mann, D. S., Jiang, W., Rees, I., and Ludtke, S. J. (2007) EMAN2. An extensible image processing suite for electron microscopy. J. Struct. Biol. 157, 38-46 (Pubitemid 44880785)
    • (2007) Journal of Structural Biology , vol.157 , Issue.1 , pp. 38-46
    • Tang, G.1    Peng, L.2    Baldwin, P.R.3    Mann, D.S.4    Jiang, W.5    Rees, I.6    Ludtke, S.J.7
  • 70
    • 0028261414 scopus 로고
    • Enzymatic deglycosylation of asparagine-linked glycans. Purification, properties, and specificity of oligosaccharide-cleaving enzymes from Flavobacterium meningosepticum
    • Tarentino, A. L., and Plummer, T. H., Jr., (1994) Enzymatic deglycosylation of asparagine-linked glycans. Purification, properties, and specificity of oligosaccharide-cleaving enzymes from Flavobacterium meningosepticum. Methods Enzymol. 230, 44-57
    • (1994) Methods Enzymol. , vol.230 , pp. 44-57
    • Tarentino, A.L.1    Plummer Jr., T.H.2
  • 71
    • 0014370674 scopus 로고
    • Purification and properties of α-D-mannosidase from Jack bean meal
    • Snaith, S. M., and Levvy G. A. (1968) Purification and properties of α-D-mannosidase from Jack bean meal. Biochem. J. 110, 663-670
    • (1968) Biochem. J. , vol.110 , pp. 663-670
    • Snaith, S.M.1    Levvy, G.A.2
  • 72
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides. All of the theories are correct
    • Varki, A. (1993) Biological roles of oligosaccharides. All of the theories are correct. Glycobiology 3, 97-130
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 73
    • 80051550679 scopus 로고    scopus 로고
    • Methods development for analysis of partially deglycosylated proteins and application to an HIV envelope protein vaccine candidate
    • Go, E. P., Hewawasam, G. S., Ma, B. J., Liao, H. X., Haynes, B. F., and Desaire, H. (2011) Methods development for analysis of partially deglycosylated proteins and application to an HIV envelope protein vaccine candidate. Int. J. Mass Spectrom. 305, 209-216
    • (2011) Int. J. Mass Spectrom. , vol.305 , pp. 209-216
    • Go, E.P.1    Hewawasam, G.S.2    Ma, B.J.3    Liao, H.X.4    Haynes, B.F.5    Desaire, H.6
  • 75
    • 0037213247 scopus 로고    scopus 로고
    • Fine mapping of the interaction of neutralizing and nonneutralizing monoclonal antibodies with the CD4 binding site of human immunodeficiency virus type 1 gp120
    • DOI 10.1128/JVI.77.1.642-658.2003
    • Pantophlet, R., Ollmann Saphire, E., Poignard, P., Parren, P. W., Wilson, I. A., and Burton, D. R. (2003) Fine mapping of the interaction of neutralizing and nonneutralizing monoclonal antibodies with the CD4 binding site of human immunodeficiency virus type 1 gp120. J. Virol. 77, 642-658 (Pubitemid 36005001)
    • (2003) Journal of Virology , vol.77 , Issue.1 , pp. 642-658
    • Pantophlet, R.1    Ollmann, S.E.2    Poignard, P.3    Parren, P.W.H.I.4    Wilson, I.A.5    Burton, D.R.6
  • 77
    • 0028244285 scopus 로고
    • An N-glycan within the human immunodeficiency virus type 1 gp120 V3 loop affects virus neutralization
    • DOI 10.1006/viro.1994.1141
    • Back, N. K., Smit, L., De Jong, J. J., Keulen, W., Schutten, M., Goudsmit, J., and Tersmette, M. (1994) An N-glycan within the human immunodeficiency virus type 1 gp120 V3 loop affects virus neutralization. Virology 199, 431-438 (Pubitemid 24168981)
    • (1994) Virology , vol.199 , Issue.2 , pp. 431-438
    • Back, N.K.T.1    Smit, L.2    De Jong, J.-J.3    Keulen, W.4    Schutten, M.5    Goudsmit, J.6    Tersmette, M.7
  • 78
    • 0032991878 scopus 로고    scopus 로고
    • The N-linked glycan of the V3 region of HIV-1 gp120 and CXCR4-dependent multiplication of a human immunodeficiency virus type 1 lymphocyte-tropic variant
    • DOI 10.1016/S0014-5793(99)00740-1, PII S0014579399007401
    • Losman, B., Biller, M., Olofsson, S., Schønning, K., Lund, O. S., Svennerholm, B., Hansen, J. E., and Bolmstedt, A. (1999) The N-linked glycan of the V3 region of HIV-1 gp120 and CXCR4-dependent multiplication of a human immunodeficiency virus type 1 lymphocyte-tropic variant. FEBS Lett. 454, 47-52 (Pubitemid 29296923)
    • (1999) FEBS Letters , vol.454 , Issue.1-2 , pp. 47-52
    • Losman, B.1    Biller, M.2    Olofsson, S.3    Schonning, K.4    Lund, O.S.5    Svennerholm, B.6    Hansen, J.-E.S.7    Bolmstedt, A.8
  • 79
    • 0034469170 scopus 로고    scopus 로고
    • The N-terminal V3 loop glycan modulates the interaction of clade A and B human immunodeficiency virus type 1 envelopes with CD4 and chemokine receptors
    • DOI 10.1128/JVI.74.23.11008-11016.2000
    • Malenbaum, S. E., Yang, D., Cavacini, L., Posner, M., Robinson, J., and Cheng-Mayer, C. (2000) The N-terminal V3 loop glycan modulates the interaction of clade A and B human immunodeficiency virus type 1 envelopes with CD4 and chemokine receptors. J. Virol. 74, 11008-11016 (Pubitemid 32223966)
    • (2000) Journal of Virology , vol.74 , Issue.23 , pp. 11008-11016
    • Malenbaum, S.E.1    Yang, D.2    Cavacini, L.3    Posner, M.4    Robinson, J.5    Cheng-Mayer, C.6
  • 80
    • 1242351232 scopus 로고    scopus 로고
    • Structural Rationale for the Broad Neutralization of HIV-1 by Human Monoclonal Antibody 447-52D
    • DOI 10.1016/S0969-2126(04)00005-X
    • Stanfield, R. L., Gorny, M. K., Williams, C., Zolla-Pazner, S., and Wilson, I. A. (2004) Structural rationale for the broad neutralization of HIV-1 by human monoclonal antibody 447-52D. Structure 12, 193-204 (Pubitemid 38224543)
    • (2004) Structure , vol.12 , Issue.2 , pp. 193-204
    • Stanfield, R.L.1    Gorny, M.K.2    Williams, C.3    Zolla-Pazner, S.4    Wilson, I.A.5
  • 81
    • 0028908782 scopus 로고
    • A human monoclonal antibody to a complex epitope in the V3 region of gp120 of human immunodeficiency virus type 1 has broad reactivity within and outside clade B
    • Moore, J. P., Trkola, A., Korber, B., Boots, L. J., Kessler, J. A., 2nd, McCutchan, F. E., Mascola, J., Ho, D. D., Robinson, J., and Conley, A. J. (1995) A human monoclonal antibody to a complex epitope in the V3 region of gp120 of human immunodeficiency virus type 1 has broad reactivity within and outside clade B. J. Virol. 69, 122-130 (Pubitemid 24378785)
    • (1995) Journal of Virology , vol.69 , Issue.1 , pp. 122-130
    • Moore, J.P.1    Trkola, A.2    Korber, B.3    Boots, L.J.4    Kessler II, J.A.5    McCutchan, F.E.6    Mascola, J.7    Ho, D.D.8    Robinson, J.9    Conley, A.J.10
  • 82
    • 34247636624 scopus 로고    scopus 로고
    • Exploiting the defensive sugars of HIV-1 for drug and vaccine design
    • DOI 10.1038/nature05818, PII NATURE05818
    • Scanlan, C. N., Offer, J., Zitzmann, N., and Dwek, R. A.(2007) Exploiting the defensive sugars of HIV-1 for drug and vaccine design. Nature 446, 1038-1045 (Pubitemid 46676066)
    • (2007) Nature , vol.446 , Issue.7139 , pp. 1038-1045
    • Scanlan, C.N.1    Offer, J.2    Zitzmann, N.3    Dwek, R.A.4
  • 83
    • 0025292252 scopus 로고
    • Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells
    • Leonard, C. K., Spellman, M. W., Riddle, L., Harris, R. J., Thomas, J. N., and Gregory, T. J. (1990) Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells. J. Biol. Chem. 265, 10373-10382
    • (1990) J. Biol. Chem. , vol.265 , pp. 10373-10382
    • Leonard, C.K.1    Spellman, M.W.2    Riddle, L.3    Harris, R.J.4    Thomas, J.N.5    Gregory, T.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.