메뉴 건너뛰기




Volumn 21, Issue 1, 2014, Pages 51-66

Chemical and chemoenzymatic synthesis of glycoproteins for deciphering functions

Author keywords

[No Author keywords available]

Indexed keywords

GLYCAN; GLYCOPEPTIDE; GLYCOPROTEIN; IMMUNOGLOBULIN G ANTIBODY; POLYPEPTIDE; ENZYME;

EID: 84892662416     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2014.01.001     Document Type: Review
Times cited : (133)

References (149)
  • 1
    • 27144449009 scopus 로고    scopus 로고
    • Monoclonal antibody therapy of cancer
    • DOI 10.1038/nbt1137, PII N1137
    • G.P. Adams, and L.M. Weiner Monoclonal antibody therapy of cancer Nat. Biotechnol. 23 2005 1147 1157 (Pubitemid 41486396)
    • (2005) Nature Biotechnology , vol.23 , Issue.9 , pp. 1147-1157
    • Adams, G.P.1    Weiner, L.M.2
  • 3
    • 83255165688 scopus 로고    scopus 로고
    • What's fueling the biotech engine - 2010 to 2011
    • S. Aggarwal What's fueling the biotech engine - 2010 to 2011 Nat. Biotechnol. 29 2011 1083 1089
    • (2011) Nat. Biotechnol. , vol.29 , pp. 1083-1089
    • Aggarwal, S.1
  • 5
    • 40849097885 scopus 로고    scopus 로고
    • EndoS from Streptococcus pyogenes is hydrolyzed by the cysteine proteinase SpeB and requires glutamic acid 235 and tryptophans for IgG glycan-hydrolyzing activity
    • M. Allhorn, A. Olsén, and M. Collin EndoS from Streptococcus pyogenes is hydrolyzed by the cysteine proteinase SpeB and requires glutamic acid 235 and tryptophans for IgG glycan-hydrolyzing activity BMC Microbiol. 8 2008 3
    • (2008) BMC Microbiol. , vol.8 , pp. 3
    • Allhorn, M.1    Olsén, A.2    Collin, M.3
  • 6
    • 80052597309 scopus 로고    scopus 로고
    • Convergent synthesis of homogeneous Glc1Man9GlcNAc2-protein and derivatives as ligands of molecular chaperones in protein quality control
    • M.N. Amin, W. Huang, R.M. Mizanur, and L.X. Wang Convergent synthesis of homogeneous Glc1Man9GlcNAc2-protein and derivatives as ligands of molecular chaperones in protein quality control J. Am. Chem. Soc. 133 2011 14404 14417
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 14404-14417
    • Amin, M.N.1    Huang, W.2    Mizanur, R.M.3    Wang, L.X.4
  • 8
    • 42349085035 scopus 로고    scopus 로고
    • Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc
    • DOI 10.1126/science.1154315
    • R.M. Anthony, F. Nimmerjahn, D.J. Ashline, V.N. Reinhold, J.C. Paulson, and J.V. Ravetch Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc Science 320 2008 373 376 (Pubitemid 351555659)
    • (2008) Science , vol.320 , Issue.5874 , pp. 373-376
    • Anthony, R.M.1    Nimmerjahn, F.2    Ashline, D.J.3    Reinhold, V.N.4    Paulson, J.C.5    Ravetch, J.V.6
  • 9
    • 58149378347 scopus 로고    scopus 로고
    • Identification of a receptor required for the anti-inflammatory activity of IVIG
    • R.M. Anthony, F. Wermeling, M.C. Karlsson, and J.V. Ravetch Identification of a receptor required for the anti-inflammatory activity of IVIG Proc. Natl. Acad. Sci. USA 105 2008 19571 19578
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 19571-19578
    • Anthony, R.M.1    Wermeling, F.2    Karlsson, M.C.3    Ravetch, J.V.4
  • 10
    • 84883531336 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of the immunoglobulin domain of Tim-3 carrying a complex-type N-glycan by using a one-pot ligation
    • Y. Asahina, S. Kamitori, T. Takao, N. Nishi, and H. Hojo Chemoenzymatic synthesis of the immunoglobulin domain of Tim-3 carrying a complex-type N-glycan by using a one-pot ligation Angew. Chem. Int. Ed. Engl. 52 2013 9733 9737
    • (2013) Angew. Chem. Int. Ed. Engl. , vol.52 , pp. 9733-9737
    • Asahina, Y.1    Kamitori, S.2    Takao, T.3    Nishi, N.4    Hojo, H.5
  • 11
    • 84857383999 scopus 로고    scopus 로고
    • Total synthesis of the α-subunit of human glycoprotein hormones: Toward fully synthetic homogeneous human follicle-stimulating hormone
    • B. Aussedat, B. Fasching, E. Johnston, N. Sane, P. Nagorny, and S.J. Danishefsky Total synthesis of the α-subunit of human glycoprotein hormones: toward fully synthetic homogeneous human follicle-stimulating hormone J. Am. Chem. Soc. 134 2012 3532 3541
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 3532-3541
    • Aussedat, B.1    Fasching, B.2    Johnston, E.3    Sane, N.4    Nagorny, P.5    Danishefsky, S.J.6
  • 13
    • 80052938385 scopus 로고    scopus 로고
    • Analysis of a clonal lineage of HIV-1 envelope V2/V3 conformational epitope-specific broadly neutralizing antibodies and their inferred unmutated common ancestors
    • M. Bonsignori, K.K. Hwang, X. Chen, C.Y. Tsao, L. Morris, E. Gray, D.J. Marshall, J.A. Crump, S.H. Kapiga, and N.E. Sam et al. Analysis of a clonal lineage of HIV-1 envelope V2/V3 conformational epitope-specific broadly neutralizing antibodies and their inferred unmutated common ancestors J. Virol. 85 2011 9998 10009
    • (2011) J. Virol. , vol.85 , pp. 9998-10009
    • Bonsignori, M.1    Hwang, K.K.2    Chen, X.3    Tsao, C.Y.4    Morris, L.5    Gray, E.6    Marshall, D.J.7    Crump, J.A.8    Kapiga, S.H.9    Sam, N.E.10
  • 15
    • 33747873262 scopus 로고    scopus 로고
    • Glycopeptides as versatile tools for glycobiology
    • DOI 10.1093/glycob/cwj125
    • T. Buskas, S. Ingale, and G.J. Boons Glycopeptides as versatile tools for glycobiology Glycobiology 16 2006 113R 136R (Pubitemid 44288233)
    • (2006) Glycobiology , vol.16 , Issue.8
    • Buskas, T.1    Ingale, S.2    Boons, G.-J.3
  • 16
    • 84863012157 scopus 로고    scopus 로고
    • Variation of the glycosylation pattern in MUC1 glycopeptide BSA vaccines and its influence on the immune response
    • H. Cai, Z.H. Huang, L. Shi, Z.Y. Sun, Y.F. Zhao, H. Kunz, and Y.M. Li Variation of the glycosylation pattern in MUC1 glycopeptide BSA vaccines and its influence on the immune response Angew. Chem. Int. Ed. Engl. 51 2012 1719 1723
    • (2012) Angew. Chem. Int. Ed. Engl. , vol.51 , pp. 1719-1723
    • Cai, H.1    Huang, Z.H.2    Shi, L.3    Sun, Z.Y.4    Zhao, Y.F.5    Kunz, H.6    Li, Y.M.7
  • 17
    • 34249076359 scopus 로고    scopus 로고
    • Introducing genetically encoded aldehydes into proteins
    • DOI 10.1038/nchembio878, PII NCHEMBIO878
    • I.S. Carrico, B.L. Carlson, and C.R. Bertozzi Introducing genetically encoded aldehydes into proteins Nat. Chem. Biol. 3 2007 321 322 (Pubitemid 46789266)
    • (2007) Nature Chemical Biology , vol.3 , Issue.6 , pp. 321-322
    • Carrico, I.S.1    Carlson, B.L.2    Bertozzi, C.R.3
  • 18
    • 84866037634 scopus 로고    scopus 로고
    • Glyco-engineering in plants to produce human-like N-glycan structures
    • A. Castilho, and H. Steinkellner Glyco-engineering in plants to produce human-like N-glycan structures Biotechnol. J. 7 2012 1088 1098
    • (2012) Biotechnol. J. , vol.7 , pp. 1088-1098
    • Castilho, A.1    Steinkellner, H.2
  • 19
    • 80052995647 scopus 로고    scopus 로고
    • A "tag-and-modify" approach to site-selective protein modification
    • J.M. Chalker, G.J. Bernardes, and B.G. Davis A "tag-and-modify" approach to site-selective protein modification Acc. Chem. Res. 44 2011 730 741
    • (2011) Acc. Chem. Res. , vol.44 , pp. 730-741
    • Chalker, J.M.1    Bernardes, G.J.2    Davis, B.G.3
  • 20
    • 34248232580 scopus 로고    scopus 로고
    • From peptide to protein: Comparative analysis of the substrate specificity of N-linked glycosylation in C jejuni
    • DOI 10.1021/bi602633n
    • M.M. Chen, K.J. Glover, and B. Imperiali From peptide to protein: comparative analysis of the substrate specificity of N-linked glycosylation in C. jejuni Biochemistry 46 2007 5579 5585 (Pubitemid 46717280)
    • (2007) Biochemistry , vol.46 , Issue.18 , pp. 5579-5585
    • Chen, M.M.1    Glover, K.J.2    Imperiali, B.3
  • 21
    • 0035875889 scopus 로고    scopus 로고
    • EndoS, a novel secreted protein from Streptococcus pyogenes with endoglycosidase activity on human IgG
    • DOI 10.1093/emboj/20.12.3046
    • M. Collin, and A. Olsén EndoS, a novel secreted protein from Streptococcus pyogenes with endoglycosidase activity on human IgG EMBO J. 20 2001 3046 3055 (Pubitemid 32611992)
    • (2001) EMBO Journal , vol.20 , Issue.12 , pp. 3046-3055
    • Collin, M.1    Olsen, A.2
  • 22
    • 0033791223 scopus 로고    scopus 로고
    • Synthesis of native proteins by chemical ligation
    • P.E. Dawson, and S.B. Kent Synthesis of native proteins by chemical ligation Annu. Rev. Biochem. 69 2000 923 960
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 923-960
    • Dawson, P.E.1    Kent, S.B.2
  • 23
    • 0027944205 scopus 로고
    • Synthesis of proteins by native chemical ligation
    • P.E. Dawson, T.W. Muir, I. Clark-Lewis, and S.B. Kent Synthesis of proteins by native chemical ligation Science 266 1994 776 779 (Pubitemid 24359280)
    • (1994) Science , vol.266 , Issue.5186 , pp. 776-779
    • Dawson, P.E.1    Muir, T.W.2    Clark-Lewis, I.3    Kent, S.B.H.4
  • 24
    • 0036899975 scopus 로고    scopus 로고
    • Oligosaccharyl transferase: Gatekeeper to the secretory pathway
    • DOI 10.1016/S1367-5931(02)00390-3
    • R.E. Dempski Jr.; and B. Imperiali Oligosaccharyl transferase: gatekeeper to the secretory pathway Curr. Opin. Chem. Biol. 6 2002 844 850 (Pubitemid 35449346)
    • (2002) Current Opinion in Chemical Biology , vol.6 , Issue.6 , pp. 844-850
    • Dempski Jr., R.E.1    Imperiali, B.2
  • 25
    • 77957198704 scopus 로고    scopus 로고
    • Variable loop glycan dependency of the broad and potent HIV-1-neutralizing antibodies PG9 and PG16
    • K.J. Doores, and D.R. Burton Variable loop glycan dependency of the broad and potent HIV-1-neutralizing antibodies PG9 and PG16 J. Virol. 84 2010 10510 10521
    • (2010) J. Virol. , vol.84 , pp. 10510-10521
    • Doores, K.J.1    Burton, D.R.2
  • 26
    • 20844437106 scopus 로고    scopus 로고
    • Glycans in cancer and inflammation - Potential for therapeutics and diagnostics
    • DOI 10.1038/nrd1751
    • D.H. Dube, and C.R. Bertozzi Glycans in cancer and inflammation - potential for therapeutics and diagnostics Nat. Rev. Drug Discov. 4 2005 477 488 (Pubitemid 40861990)
    • (2005) Nature Reviews Drug Discovery , vol.4 , Issue.6 , pp. 477-488
    • Dube, D.H.1    Bertozzi, C.R.2
  • 27
    • 0001094662 scopus 로고    scopus 로고
    • Glycobiology: Toward understanding the function of sugars
    • R.A. Dwek Glycobiology: Toward understanding the function of sugars Chem. Rev. 96 1996 683 720 (Pubitemid 126649163)
    • (1996) Chemical Reviews , vol.96 , Issue.2 , pp. 683-720
    • Dwek, R.A.1
  • 29
    • 84859486843 scopus 로고    scopus 로고
    • Remarkable transglycosylation activity of glycosynthase mutants of endo-D, an endo-β-N-acetylglucosaminidase from Streptococcus pneumoniae
    • S.Q. Fan, W. Huang, and L.X. Wang Remarkable transglycosylation activity of glycosynthase mutants of endo-D, an endo-β-N-acetylglucosaminidase from Streptococcus pneumoniae J. Biol. Chem. 287 2012 11272 11281
    • (2012) J. Biol. Chem. , vol.287 , pp. 11272-11281
    • Fan, S.Q.1    Huang, W.2    Wang, L.X.3
  • 33
    • 0035801838 scopus 로고    scopus 로고
    • A novel disaccharide substrate having 1,2-oxazoline moiety for detection of transglycosylating activity of endoglycosidases
    • DOI 10.1016/S0304-4165(01)00164-7, PII S0304416501001647
    • M. Fujita, S. Shoda, K. Haneda, T. Inazu, K. Takegawa, and K. Yamamoto A novel disaccharide substrate having 1,2-oxazoline moiety for detection of transglycosylating activity of endoglycosidases Biochim. Biophys. Acta 1528 2001 9 14 (Pubitemid 32763144)
    • (2001) Biochimica et Biophysica Acta - General Subjects , vol.1528 , Issue.1 , pp. 9-14
    • Fujita, M.1    Shoda, S.-I.2    Haneda, K.3    Inazu, T.4    Takegawa, K.5    Yamamoto, K.6
  • 34
    • 84876898171 scopus 로고    scopus 로고
    • The development of synthetic antitumour vaccines from mucin glycopeptide antigens
    • N. Gaidzik, U. Westerlind, and H. Kunz The development of synthetic antitumour vaccines from mucin glycopeptide antigens Chem. Soc. Rev. 42 2013 4421 4442
    • (2013) Chem. Soc. Rev. , vol.42 , pp. 4421-4442
    • Gaidzik, N.1    Westerlind, U.2    Kunz, H.3
  • 36
    • 28844508716 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of glycopeptides with PglB, a bacterial oligosaccharyl transferase from Campylobacter jejuni
    • K.J. Glover, E. Weerapana, S. Numao, and B. Imperiali Chemoenzymatic synthesis of glycopeptides with PglB, a bacterial oligosaccharyl transferase from Campylobacter jejuni Chem. Biol. 12 2005 1311 1315
    • (2005) Chem. Biol. , vol.12 , pp. 1311-1315
    • Glover, K.J.1    Weerapana, E.2    Numao, S.3    Imperiali, B.4
  • 38
    • 0035997381 scopus 로고    scopus 로고
    • Homogeneous glycopeptides and glycoproteins for biological investigation
    • DOI 10.1146/annurev.biochem.71.110601.135334
    • M.J. Grogan, M.R. Pratt, L.A. Marcaurelle, and C.R. Bertozzi Homogeneous glycopeptides and glycoproteins for biological investigation Annu. Rev. Biochem. 71 2002 593 634 (Pubitemid 34800231)
    • (2002) Annual Review of Biochemistry , vol.71 , pp. 593-634
    • Grogan, M.J.1    Pratt, M.R.2    Marcaurelle, L.A.3    Bertozzi, C.R.4
  • 39
    • 26844522027 scopus 로고    scopus 로고
    • Glycopeptide and glycoprotein synthesis involving unprotected carbohydrate building blocks
    • DOI 10.1002/med.20033
    • Z. Guo, and N. Shao Glycopeptide and glycoprotein synthesis involving unprotected carbohydrate building blocks Med. Res. Rev. 25 2005 655 678 (Pubitemid 41447147)
    • (2005) Medicinal Research Reviews , vol.25 , Issue.6 , pp. 655-678
    • Guo, Z.1    Shao, N.2
  • 40
    • 3943056897 scopus 로고    scopus 로고
    • Role of glycosylation in development
    • DOI 10.1146/annurev.biochem.73.011303.074043
    • R.S. Haltiwanger, and J.B. Lowe Role of glycosylation in development Annu. Rev. Biochem. 73 2004 491 537 (Pubitemid 39050378)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 491-537
    • Haltiwanger, R.S.1    Lowe, J.B.2
  • 41
    • 36149001292 scopus 로고    scopus 로고
    • Glycosylation engineering in yeast: The advent of fully humanized yeast
    • DOI 10.1016/j.copbio.2007.09.001, PII S0958166907001139, Expression Technologies / Tissue and Cell Engineering
    • S.R. Hamilton, and T.U. Gerngross Glycosylation engineering in yeast: the advent of fully humanized yeast Curr. Opin. Biotechnol. 18 2007 387 392 (Pubitemid 350116586)
    • (2007) Current Opinion in Biotechnology , vol.18 , Issue.5 , pp. 387-392
    • Hamilton, S.R.1    Gerngross, T.U.2
  • 42
    • 0034823319 scopus 로고    scopus 로고
    • Chemoselective approaches to glycoprotein assembly
    • DOI 10.1021/ar9901570
    • H.C. Hang, and C.R. Bertozzi Chemoselective approaches to glycoprotein assembly Acc. Chem. Res. 34 2001 727 736 (Pubitemid 32884838)
    • (2001) Accounts of Chemical Research , vol.34 , Issue.9 , pp. 727-736
    • Hang, H.C.1    Bertozzi, C.R.2
  • 43
    • 79251489778 scopus 로고    scopus 로고
    • Glycomics hits the big time
    • G.W. Hart, and R.J. Copeland Glycomics hits the big time Cell 143 2010 672 676
    • (2010) Cell , vol.143 , pp. 672-676
    • Hart, G.W.1    Copeland, R.J.2
  • 44
    • 79959381299 scopus 로고    scopus 로고
    • Cross talk between O-GlcNAcylation and phosphorylation: Roles in signaling, transcription, and chronic disease
    • G.W. Hart, C. Slawson, G. Ramirez-Correa, and O. Lagerlof Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease Annu. Rev. Biochem. 80 2011 825 858
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 825-858
    • Hart, G.W.1    Slawson, C.2    Ramirez-Correa, G.3    Lagerlof, O.4
  • 45
    • 0035937505 scopus 로고    scopus 로고
    • Intracellular functions of N-linked glycans
    • DOI 10.1126/science.291.5512.2364
    • A. Helenius, and M. Aebi Intracellular functions of N-linked glycans Science 291 2001 2364 2369 (Pubitemid 32231791)
    • (2001) Science , vol.291 , Issue.5512 , pp. 2364-2369
    • Helenius, A.1    Aebi, M.2
  • 46
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • DOI 10.1146/annurev.biochem.73.011303.073752
    • A. Helenius, and M. Aebi Roles of N-linked glycans in the endoplasmic reticulum Annu. Rev. Biochem. 73 2004 1019 1049 (Pubitemid 39050393)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 47
    • 0026702568 scopus 로고
    • Role of sugar chains in the expression of the biological activity of human erythropoietin
    • M. Higuchi, M. Oh-eda, H. Kuboniwa, K. Tomonoh, Y. Shimonaka, and N. Ochi Role of sugar chains in the expression of the biological activity of human erythropoietin J. Biol. Chem. 267 1992 7703 7709
    • (1992) J. Biol. Chem. , vol.267 , pp. 7703-7709
    • Higuchi, M.1    Oh-Eda, M.2    Kuboniwa, H.3    Tomonoh, K.4    Shimonaka, Y.5    Ochi, N.6
  • 48
    • 73249150910 scopus 로고    scopus 로고
    • Design and synthesis of a homogeneous erythropoietin analogue with two human complex-type sialyloligosaccharides: Combined use of chemical and bacterial protein expression methods
    • K. Hirano, D. Macmillan, K. Tezuka, T. Tsuji, and Y. Kajihara Design and synthesis of a homogeneous erythropoietin analogue with two human complex-type sialyloligosaccharides: combined use of chemical and bacterial protein expression methods Angew. Chem. Int. Ed. Engl. 48 2009 9557 9560
    • (2009) Angew. Chem. Int. Ed. Engl. , vol.48 , pp. 9557-9560
    • Hirano, K.1    Macmillan, D.2    Tezuka, K.3    Tsuji, T.4    Kajihara, Y.5
  • 49
    • 34247473463 scopus 로고    scopus 로고
    • Recent progress in the field of glycopeptide synthesis
    • DOI 10.1002/bip.20699
    • H. Hojo, and Y. Nakahara Recent progress in the field of glycopeptide synthesis Biopolymers 88 2007 308 324 (Pubitemid 46657996)
    • (2007) Biopolymers - Peptide Science Section , vol.88 , Issue.2 , pp. 308-324
    • Hojo, H.1    Nakahara, Y.2
  • 52
    • 67650507291 scopus 로고    scopus 로고
    • Enzymatic glycosylation of triazole-linked GlcNAc/Glc-peptides: Synthesis, stability and anti-HIV activity of triazole-linked HIV-1 gp41 glycopeptide C34 analogues
    • W. Huang, S. Groothuys, A. Heredia, B.H. Kuijpers, F.P. Rutjes, F.L. van Delft, and L.X. Wang Enzymatic glycosylation of triazole-linked GlcNAc/Glc-peptides: synthesis, stability and anti-HIV activity of triazole-linked HIV-1 gp41 glycopeptide C34 analogues ChemBioChem 10 2009 1234 1242
    • (2009) ChemBioChem , vol.10 , pp. 1234-1242
    • Huang, W.1    Groothuys, S.2    Heredia, A.3    Kuijpers, B.H.4    Rutjes, F.P.5    Van Delft, F.L.6    Wang, L.X.7
  • 53
    • 67749122310 scopus 로고    scopus 로고
    • Glycosynthases enable a highly efficient chemoenzymatic synthesis of N-glycoproteins carrying intact natural N-glycans
    • W. Huang, C. Li, B. Li, M. Umekawa, K. Yamamoto, X. Zhang, and L.X. Wang Glycosynthases enable a highly efficient chemoenzymatic synthesis of N-glycoproteins carrying intact natural N-glycans J. Am. Chem. Soc. 131 2009 2214 2223
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 2214-2223
    • Huang, W.1    Li, C.2    Li, B.3    Umekawa, M.4    Yamamoto, K.5    Zhang, X.6    Wang, L.X.7
  • 54
    • 77954362047 scopus 로고    scopus 로고
    • Arthrobacter endo-beta-N-acetylglucosaminidase shows transglycosylation activity on complex-type N-glycan oxazolines: One-pot conversion of ribonuclease B to sialylated ribonuclease C
    • W. Huang, Q. Yang, M. Umekawa, K. Yamamoto, and L.X. Wang Arthrobacter endo-beta-N-acetylglucosaminidase shows transglycosylation activity on complex-type N-glycan oxazolines: one-pot conversion of ribonuclease B to sialylated ribonuclease C ChemBioChem 11 2010 1350 1355
    • (2010) ChemBioChem , vol.11 , pp. 1350-1355
    • Huang, W.1    Yang, Q.2    Umekawa, M.3    Yamamoto, K.4    Wang, L.X.5
  • 55
    • 78049326742 scopus 로고    scopus 로고
    • Expeditious chemoenzymatic synthesis of CD52 glycopeptide antigens
    • W. Huang, X. Zhang, T. Ju, R.D. Cummings, and L.X. Wang Expeditious chemoenzymatic synthesis of CD52 glycopeptide antigens Org. Biomol. Chem. 8 2010 5224 5233
    • (2010) Org. Biomol. Chem. , vol.8 , pp. 5224-5233
    • Huang, W.1    Zhang, X.2    Ju, T.3    Cummings, R.D.4    Wang, L.X.5
  • 56
    • 84864238717 scopus 로고    scopus 로고
    • Chemoenzymatic glycoengineering of intact IgG antibodies for gain of functions
    • W. Huang, J. Giddens, S.Q. Fan, C. Toonstra, and L.X. Wang Chemoenzymatic glycoengineering of intact IgG antibodies for gain of functions J. Am. Chem. Soc. 134 2012 12308 12318
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 12308-12318
    • Huang, W.1    Giddens, J.2    Fan, S.Q.3    Toonstra, C.4    Wang, L.X.5
  • 57
    • 80053524815 scopus 로고    scopus 로고
    • Protein glycoengineering enabled by the versatile synthesis of aminooxy glycans and the genetically encoded aldehyde tag
    • J.E. Hudak, H.H. Yu, and C.R. Bertozzi Protein glycoengineering enabled by the versatile synthesis of aminooxy glycans and the genetically encoded aldehyde tag J. Am. Chem. Soc. 133 2011 16127 16135
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 16127-16135
    • Hudak, J.E.1    Yu, H.H.2    Bertozzi, C.R.3
  • 58
    • 0029610991 scopus 로고
    • Asparagine-linked glycosylation: Specificity and function of oligosaccharyl transferase
    • DOI 10.1016/0968-0896(95)00142-5
    • B. Imperiali, and T.L. Hendrickson Asparagine-linked glycosylation: specificity and function of oligosaccharyl transferase Bioorg. Med. Chem. 3 1995 1565 1578 (Pubitemid 26022435)
    • (1995) Bioorganic and Medicinal Chemistry , vol.3 , Issue.12 , pp. 1565-1578
    • Imperiali, B.1    Hendrickson, T.L.2
  • 59
    • 25844454688 scopus 로고    scopus 로고
    • Structural approaches to the study of oligosaccharides in glycoprotein quality control
    • DOI 10.1016/j.sbi.2005.08.012, PII S0959440X05001600, Carbohydrates and Glycoconjugates/Biophysical Methods
    • Y. Ito, S. Hagihara, I. Matsuo, and K. Totani Structural approaches to the study of oligosaccharides in glycoprotein quality control Curr. Opin. Struct. Biol. 15 2005 481 489 (Pubitemid 41393478)
    • (2005) Current Opinion in Structural Biology , vol.15 , Issue.5 , pp. 481-489
    • Ito, Y.1    Hagihara, S.2    Matsuo, I.3    Totani, K.4
  • 60
    • 84870050270 scopus 로고    scopus 로고
    • Reconstructed glycan profile for evaluation of operating status of the endoplasmic reticulum glycoprotein quality control
    • S. Iwamoto, M. Isoyama, M. Hirano, K. Yamaya, Y. Ito, I. Matsuo, and K. Totani Reconstructed glycan profile for evaluation of operating status of the endoplasmic reticulum glycoprotein quality control Glycobiology 23 2013 121 131
    • (2013) Glycobiology , vol.23 , pp. 121-131
    • Iwamoto, S.1    Isoyama, M.2    Hirano, M.3    Yamaya, K.4    Ito, Y.5    Matsuo, I.6    Totani, K.7
  • 61
    • 84860802199 scopus 로고    scopus 로고
    • Chemical synthesis of intentionally misfolded homogeneous glycoprotein: A unique approach for the study of glycoprotein quality control
    • M. Izumi, Y. Makimura, S. Dedola, A. Seko, A. Kanamori, M. Sakono, Y. Ito, and Y. Kajihara Chemical synthesis of intentionally misfolded homogeneous glycoprotein: a unique approach for the study of glycoprotein quality control J. Am. Chem. Soc. 134 2012 7238 7241
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 7238-7241
    • Izumi, M.1    Makimura, Y.2    Dedola, S.3    Seko, A.4    Kanamori, A.5    Sakono, M.6    Ito, Y.7    Kajihara, Y.8
  • 62
    • 61449242817 scopus 로고    scopus 로고
    • Engineering complex-type N-glycosylation in Pichia pastoris using GlycoSwitch technology
    • P.P. Jacobs, S. Geysens, W. Vervecken, R. Contreras, and N. Callewaert Engineering complex-type N-glycosylation in Pichia pastoris using GlycoSwitch technology Nat. Protoc. 4 2009 58 70
    • (2009) Nat. Protoc. , vol.4 , pp. 58-70
    • Jacobs, P.P.1    Geysens, S.2    Vervecken, W.3    Contreras, R.4    Callewaert, N.5
  • 63
    • 61649087668 scopus 로고    scopus 로고
    • Glycosylation as a strategy to improve antibody-based therapeutics
    • R. Jefferis Glycosylation as a strategy to improve antibody-based therapeutics Nat. Rev. Drug Discov. 8 2009 226 234
    • (2009) Nat. Rev. Drug Discov. , vol.8 , pp. 226-234
    • Jefferis, R.1
  • 65
    • 1542288845 scopus 로고    scopus 로고
    • Prompt chemoenzymatic synthesis of diverse complex-type oligosaccharides and its application to the solid-phase synthesis of a glycopeptide with Asn-linked sialyl-undeca- and asialo-nonasaccharides
    • Y. Kajihara, Y. Suzuki, N. Yamamoto, K. Sasaki, T. Sakakibara, and L.R. Juneja Prompt chemoenzymatic synthesis of diverse complex-type oligosaccharides and its application to the solid-phase synthesis of a glycopeptide with Asn-linked sialyl-undeca- and asialo-nonasaccharides Chemistry 10 2004 971 985
    • (2004) Chemistry , vol.10 , pp. 971-985
    • Kajihara, Y.1    Suzuki, Y.2    Yamamoto, N.3    Sasaki, K.4    Sakakibara, T.5    Juneja, L.R.6
  • 66
    • 33746888249 scopus 로고    scopus 로고
    • Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation
    • DOI 10.1126/science.1129594
    • Y. Kaneko, F. Nimmerjahn, and J.V. Ravetch Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation Science 313 2006 670 673 (Pubitemid 44201145)
    • (2006) Science , vol.313 , Issue.5787 , pp. 670-673
    • Kaneko, Y.1    Nimmerjahn, F.2    Ravetch, J.V.3
  • 67
    • 84880101535 scopus 로고    scopus 로고
    • Top-down chemoenzymatic approach to a high-mannose-type glycan library: Synthesis of a common precursor and its enzymatic trimming
    • A. Koizumi, I. Matsuo, M. Takatani, A. Seko, M. Hachisu, Y. Takeda, and Y. Ito Top-down chemoenzymatic approach to a high-mannose-type glycan library: synthesis of a common precursor and its enzymatic trimming Angew. Chem. Int. Ed. Engl. 52 2013 7426 7431
    • (2013) Angew. Chem. Int. Ed. Engl. , vol.52 , pp. 7426-7431
    • Koizumi, A.1    Matsuo, I.2    Takatani, M.3    Seko, A.4    Hachisu, M.5    Takeda, Y.6    Ito, Y.7
  • 68
    • 33751215862 scopus 로고    scopus 로고
    • N-linked glycosylation of folded proteins by the bacterial oligosaccharyltransferase
    • DOI 10.1126/science.1134351
    • M. Kowarik, S. Numao, M.F. Feldman, B.L. Schulz, N. Callewaert, E. Kiermaier, I. Catrein, and M. Aebi N-linked glycosylation of folded proteins by the bacterial oligosaccharyltransferase Science 314 2006 1148 1150 (Pubitemid 44789045)
    • (2006) Science , vol.314 , Issue.5802 , pp. 1148-1150
    • Kowarik, M.1    Numao, S.2    Feldman, M.F.3    Schulz, B.L.4    Callewaert, N.5    Kiermaier, E.6    Catrein, I.7    Aebi, M.8
  • 69
    • 22144450662 scopus 로고    scopus 로고
    • Highly efficient endoglycosidase-catalyzed synthesis of glycopeptides using oligosaccharide oxazolines as donor substrates
    • DOI 10.1021/ja051715a
    • B. Li, Y. Zeng, S. Hauser, H. Song, and L.X. Wang Highly efficient endoglycosidase-catalyzed synthesis of glycopeptides using oligosaccharide oxazolines as donor substrates J. Am. Chem. Soc. 127 2005 9692 9693 (Pubitemid 40981526)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.27 , pp. 9692-9693
    • Li, B.1    Zeng, Y.2    Hauser, S.3    Song, H.4    Wang, L.-X.5
  • 70
    • 28044431841 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of HIV-1 V3 glycopeptides carrying two N-glycans and effects of glycosylation on the peptide domain
    • DOI 10.1021/jo051729z
    • H. Li, B. Li, H. Song, L. Breydo, I.V. Baskakov, and L.X. Wang Chemoenzymatic synthesis of HIV-1 V3 glycopeptides carrying two N-glycans and effects of glycosylation on the peptide domain J. Org. Chem. 70 2005 9990 9996 (Pubitemid 41689165)
    • (2005) Journal of Organic Chemistry , vol.70 , Issue.24 , pp. 9990-9996
    • Li, H.1    Li, B.2    Song, H.3    Breydo, L.4    Baskakov, I.V.5    Wang, L.-X.6
  • 71
    • 33746608497 scopus 로고    scopus 로고
    • A highly efficient chemoenzymatic approach toward glycoprotein synthesis
    • DOI 10.1021/ol061056m
    • B. Li, H. Song, S. Hauser, and L.X. Wang A highly efficient chemoenzymatic approach toward glycoprotein synthesis Org. Lett. 8 2006 3081 3084 (Pubitemid 44154435)
    • (2006) Organic Letters , vol.8 , Issue.14 , pp. 3081-3084
    • Li, B.1    Song, H.2    Hauser, S.3    Wang, L.-X.4
  • 73
    • 79959191882 scopus 로고    scopus 로고
    • X-ray structure of a bacterial oligosaccharyltransferase
    • C. Lizak, S. Gerber, S. Numao, M. Aebi, and K.P. Locher X-ray structure of a bacterial oligosaccharyltransferase Nature 474 2011 350 355
    • (2011) Nature , vol.474 , pp. 350-355
    • Lizak, C.1    Gerber, S.2    Numao, S.3    Aebi, M.4    Locher, K.P.5
  • 75
    • 84890248142 scopus 로고    scopus 로고
    • Context and complexity: The next big thing in synthetic glycobiology
    • T. Lowary Context and complexity: The next big thing in synthetic glycobiology Curr. Opin. Chem. Biol. 17 2013 990 996
    • (2013) Curr. Opin. Chem. Biol. , vol.17 , pp. 990-996
    • Lowary, T.1
  • 76
    • 3543108674 scopus 로고    scopus 로고
    • Modular assembly of glycoproteins: Towards the synthesis of GlyCAM-1 by using expressed protein ligation
    • DOI 10.1002/anie.200352673
    • D. Macmillan, and C.R. Bertozzi Modular assembly of glycoproteins: towards the synthesis of GlyCAM-1 by using expressed protein ligation Angew. Chem. Int. Ed. Engl. 43 2004 1355 1359 (Pubitemid 39257913)
    • (2004) Angewandte Chemie - International Edition , vol.43 , Issue.11 , pp. 1355-1359
    • Macmillan, D.1    Bertozzi, C.R.2
  • 77
    • 0035057706 scopus 로고    scopus 로고
    • Selective in vitro glycosylation of recombinant proteins: Semi-synthesis of novel homogeneous glycoforms of human erythropoietin
    • DOI 10.1016/S1074-5521(00)90065-6, PII S107455210000065X
    • D. Macmillan, R.M. Bill, K.A. Sage, D. Fern, and S.L. Flitsch Selective in vitro glycosylation of recombinant proteins: semi-synthesis of novel homogeneous glycoforms of human erythropoietin Chem. Biol. 8 2001 133 145 (Pubitemid 32300208)
    • (2001) Chemistry and Biology , vol.8 , Issue.2 , pp. 133-145
    • Macmillan, D.1    Bill, R.M.2    Sage, K.A.3    Fern, D.4    Flitsch, S.L.5
  • 78
    • 84868578412 scopus 로고    scopus 로고
    • Efficient synthesis of glycopeptide-α-thioesters with a high-mannose type oligosaccharide by means of tert-Boc-solid phase peptide synthesis
    • Y. Makimura, T. Kiuchi, M. Izumi, S. Dedola, Y. Ito, and Y. Kajihara Efficient synthesis of glycopeptide-α-thioesters with a high-mannose type oligosaccharide by means of tert-Boc-solid phase peptide synthesis Carbohydr. Res. 364 2012 41 48
    • (2012) Carbohydr. Res. , vol.364 , pp. 41-48
    • Makimura, Y.1    Kiuchi, T.2    Izumi, M.3    Dedola, S.4    Ito, Y.5    Kajihara, Y.6
  • 80
    • 17044390429 scopus 로고    scopus 로고
    • An orthogonal double-linker resin facilitates the efficient solid-phase synthesis of complex-type N-glycopeptide thioesters suitable for native chemical ligation
    • S. Mezzato, M. Schaffrath, and C. Unverzagt An orthogonal double-linker resin facilitates the efficient solid-phase synthesis of complex-type N-glycopeptide thioesters suitable for native chemical ligation Angew. Chem. Int. Ed. Engl. 44 2005 1650 1654
    • (2005) Angew. Chem. Int. Ed. Engl. , vol.44 , pp. 1650-1654
    • Mezzato, S.1    Schaffrath, M.2    Unverzagt, C.3
  • 81
    • 0037548053 scopus 로고    scopus 로고
    • Semisynthesis of proteins by expressed protein ligation
    • DOI 10.1146/annurev.biochem.72.121801.161900
    • T.W. Muir Semisynthesis of proteins by expressed protein ligation Annu. Rev. Biochem. 72 2003 249 289 (Pubitemid 36930447)
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 249-289
    • Muir, T.W.1
  • 83
    • 84859524073 scopus 로고    scopus 로고
    • Chemical synthesis of an erythropoietin glycoform containing a complex-type disialyloligosaccharide
    • M. Murakami, R. Okamoto, M. Izumi, and Y. Kajihara Chemical synthesis of an erythropoietin glycoform containing a complex-type disialyloligosaccharide Angew. Chem. Int. Ed. Engl. 51 2012 3567 3572
    • (2012) Angew. Chem. Int. Ed. Engl. , vol.51 , pp. 3567-3572
    • Murakami, M.1    Okamoto, R.2    Izumi, M.3    Kajihara, Y.4
  • 84
    • 70549088023 scopus 로고    scopus 로고
    • Recent progress in chemical and chemoenzymatic synthesis of carbohydrates
    • S. Muthana, H. Cao, and X. Chen Recent progress in chemical and chemoenzymatic synthesis of carbohydrates Curr. Opin. Chem. Biol. 13 2009 573 581
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 573-581
    • Muthana, S.1    Cao, H.2    Chen, X.3
  • 85
    • 84855984822 scopus 로고    scopus 로고
    • Probing the frontiers of glycoprotein synthesis: The fully elaborated β-subunit of the human follicle-stimulating hormone
    • P. Nagorny, N. Sane, B. Fasching, B. Aussedat, and S.J. Danishefsky Probing the frontiers of glycoprotein synthesis: the fully elaborated β-subunit of the human follicle-stimulating hormone Angew. Chem. Int. Ed. Engl. 51 2012 975 979
    • (2012) Angew. Chem. Int. Ed. Engl. , vol.51 , pp. 975-979
    • Nagorny, P.1    Sane, N.2    Fasching, B.3    Aussedat, B.4    Danishefsky, S.J.5
  • 86
    • 42649089750 scopus 로고    scopus 로고
    • Anti-inflammatory actions of intravenous immunoglobulin
    • DOI 10.1146/annurev.immunol.26.021607.090232
    • F. Nimmerjahn, and J.V. Ravetch Anti-inflammatory actions of intravenous immunoglobulin Annu. Rev. Immunol. 26 2008 513 533 (Pubitemid 351600384)
    • (2008) Annual Review of Immunology , vol.26 , pp. 513-533
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 87
    • 37549036732 scopus 로고    scopus 로고
    • Fcgamma receptors as regulators of immune responses
    • F. Nimmerjahn, and J.V. Ravetch Fcgamma receptors as regulators of immune responses Nat. Rev. Immunol. 8 2008 34 47
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 34-47
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 88
    • 53849101862 scopus 로고    scopus 로고
    • Expeditious chemoenzymatic synthesis of homogeneous N-glycoproteins carrying defined oligosaccharide ligands
    • H. Ochiai, W. Huang, and L.X. Wang Expeditious chemoenzymatic synthesis of homogeneous N-glycoproteins carrying defined oligosaccharide ligands J. Am. Chem. Soc. 130 2008 13790 13803
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 13790-13803
    • Ochiai, H.1    Huang, W.2    Wang, L.X.3
  • 89
    • 84880572002 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis and lectin recognition of a selectively fluorinated glycoprotein
    • J. Orwenyo, W. Huang, and L.X. Wang Chemoenzymatic synthesis and lectin recognition of a selectively fluorinated glycoprotein Bioorg. Med. Chem. 21 2013 4768 4777
    • (2013) Bioorg. Med. Chem. , vol.21 , pp. 4768-4777
    • Orwenyo, J.1    Huang, W.2    Wang, L.X.3
  • 90
    • 72149096309 scopus 로고    scopus 로고
    • Advances in chemical ligation strategies for the synthesis of glycopeptides and glycoproteins
    • R.J. Payne, and C.H. Wong Advances in chemical ligation strategies for the synthesis of glycopeptides and glycoproteins Chem. Commun. (Camb.) 46 2010 21 43
    • (2010) Chem. Commun. (Camb.) , vol.46 , pp. 21-43
    • Payne, R.J.1    Wong, C.H.2
  • 91
    • 33749071408 scopus 로고    scopus 로고
    • Structural aspects of glycomes with a focus on N-glycosylation and glycoprotein folding
    • DOI 10.1016/j.sbi.2006.08.007, PII S0959440X06001424, Carbohydrates and Glycoconjugates / Biophysical Methods
    • A.J. Petrescu, M.R. Wormald, and R.A. Dwek Structural aspects of glycomes with a focus on N-glycosylation and glycoprotein folding Curr. Opin. Struct. Biol. 16 2006 600 607 (Pubitemid 44466408)
    • (2006) Current Opinion in Structural Biology , vol.16 , Issue.5 , pp. 600-607
    • Petrescu, A.-J.1    Wormald, M.R.2    Dwek, R.A.3
  • 94
    • 14544269999 scopus 로고    scopus 로고
    • Synthetic glycopeptides and glycoproteins as tools for biology
    • DOI 10.1039/b400593g
    • M.R. Pratt, and C.R. Bertozzi Synthetic glycopeptides and glycoproteins as tools for biology Chem. Soc. Rev. 34 2005 58 68 (Pubitemid 40311183)
    • (2005) Chemical Society Reviews , vol.34 , Issue.1 , pp. 58-68
    • Pratt, M.R.1    Bertozzi, C.R.2
  • 96
    • 62649171202 scopus 로고    scopus 로고
    • Emerging methods for the production of homogeneous human glycoproteins
    • J.R. Rich, and S.G. Withers Emerging methods for the production of homogeneous human glycoproteins Nat. Chem. Biol. 5 2009 206 215
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 206-215
    • Rich, J.R.1    Withers, S.G.2
  • 97
    • 33747181055 scopus 로고    scopus 로고
    • Endohexosaminidase M: Exploring and exploiting enzyme substrate specificity
    • DOI 10.1002/cbic.200600183
    • T.W. Rising, T.D. Claridge, J.W. Moir, and A.J. Fairbanks Endohexosaminidase M: exploring and exploiting enzyme substrate specificity ChemBioChem 7 2006 1177 1180 (Pubitemid 44230840)
    • (2006) ChemBioChem , vol.7 , Issue.8 , pp. 1177-1180
    • Rising, T.W.D.F.1    Claridge, T.D.W.2    Moir, J.W.B.3    Fairbanks, A.J.4
  • 99
    • 79960566715 scopus 로고    scopus 로고
    • Enzymes in the synthesis of glycoconjugates
    • R.M. Schmaltz, S.R. Hanson, and C.H. Wong Enzymes in the synthesis of glycoconjugates Chem. Rev. 111 2011 4259 4307
    • (2011) Chem. Rev. , vol.111 , pp. 4259-4307
    • Schmaltz, R.M.1    Hanson, S.R.2    Wong, C.H.3
  • 101
    • 80053392394 scopus 로고    scopus 로고
    • Cytoplasmic N-glycosyltransferase of Actinobacillus pleuropneumoniae is an inverting enzyme and recognizes the NX(S/T) consensus sequence
    • F. Schwarz, Y.Y. Fan, M. Schubert, and M. Aebi Cytoplasmic N-glycosyltransferase of Actinobacillus pleuropneumoniae is an inverting enzyme and recognizes the NX(S/T) consensus sequence J. Biol. Chem. 286 2011 35267 35274
    • (2011) J. Biol. Chem. , vol.286 , pp. 35267-35274
    • Schwarz, F.1    Fan, Y.Y.2    Schubert, M.3    Aebi, M.4
  • 102
    • 27744495195 scopus 로고    scopus 로고
    • Protein semisynthesis and expressed protein ligation: Chasing a protein's tail
    • DOI 10.1016/j.cbpa.2005.09.018, PII S1367593105001353, Biopolymers / Model Systems
    • D. Schwarzer, and P.A. Cole Protein semisynthesis and expressed protein ligation: chasing a protein's tail Curr. Opin. Chem. Biol. 9 2005 561 569 (Pubitemid 41612183)
    • (2005) Current Opinion in Chemical Biology , vol.9 , Issue.6 , pp. 561-569
    • Schwarzer, D.1    Cole, P.A.2
  • 103
    • 0039174268 scopus 로고    scopus 로고
    • Glycopeptide synthesis and the effects of glycosylation on protein structure and activity
    • O. Seitz Glycopeptide synthesis and the effects of glycosylation on protein structure and activity ChemBioChem 1 2000 214 246
    • (2000) ChemBioChem , vol.1 , pp. 214-246
    • Seitz, O.1
  • 105
    • 0037178791 scopus 로고    scopus 로고
    • Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human FcγRIII and antibody-dependent cellular toxicity
    • DOI 10.1074/jbc.M202069200
    • R.L. Shields, J. Lai, R. Keck, L.Y. O'Connell, K. Hong, Y.G. Meng, S.H. Weikert, and L.G. Presta Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity J. Biol. Chem. 277 2002 26733 26740 (Pubitemid 34951677)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.30 , pp. 26733-26740
    • Shields, R.L.1    Lai, J.2    Keck, R.3    O'Connell, L.Y.4    Hong, K.5    Gloria Meng, Y.6    Weikert, S.H.A.7    Presta, L.G.8
  • 106
    • 0033596308 scopus 로고    scopus 로고
    • Fmoc-Based Synthesis of Peptide-αThioesters:c Application to the Total Chemical Synthesis of a Glycoprotein by Native Chemical Ligation
    • Y. Shin, K.A. Winans, B.J. Backes, S.B.H. Kent, J.A. Ellman, and C.B. Bertozzi Fmoc-Based Synthesis of Peptide-αThioesters:c Application to the Total Chemical Synthesis of a Glycoprotein by Native Chemical Ligation J. Am. Chem. Soc. 121 1999 11684 11689
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 11684-11689
    • Shin, Y.1    Winans, K.A.2    Backes, B.J.3    Kent, S.B.H.4    Ellman, J.A.5    Bertozzi, C.B.6
  • 109
    • 0034680911 scopus 로고    scopus 로고
    • Glucose residues as key determinants in the biosynthesis and quality control of glycoproteins with N-linked oligosaccharides
    • R.G. Spiro Glucose residues as key determinants in the biosynthesis and quality control of glycoproteins with N-linked oligosaccharides J. Biol. Chem. 275 2000 35657 35660
    • (2000) J. Biol. Chem. , vol.275 , pp. 35657-35660
    • Spiro, R.G.1
  • 110
    • 0036019907 scopus 로고    scopus 로고
    • Protein glycosylation: Nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds
    • R.G. Spiro Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds Glycobiology 12 2002 43R 56R (Pubitemid 34760066)
    • (2002) Glycobiology , vol.12 , Issue.4
    • Spiro, R.G.1
  • 111
    • 0026516422 scopus 로고
    • Glycosylation engineering
    • P. Stanley Glycosylation engineering Glycobiology 2 1992 99 107
    • (1992) Glycobiology , vol.2 , pp. 99-107
    • Stanley, P.1
  • 112
    • 53849145029 scopus 로고    scopus 로고
    • Pre-activation-based one-pot synthesis of an alpha-(2,3)-sialylated core-fucosylated complex type bi-antennary N-glycan dodecasaccharide
    • B. Sun, B. Srinivasan, and X. Huang Pre-activation-based one-pot synthesis of an alpha-(2,3)-sialylated core-fucosylated complex type bi-antennary N-glycan dodecasaccharide Chemistry 14 2008 7072 7081
    • (2008) Chemistry , vol.14 , pp. 7072-7081
    • Sun, B.1    Srinivasan, B.2    Huang, X.3
  • 113
    • 70549101180 scopus 로고    scopus 로고
    • Chemical approaches toward understanding glycan-mediated protein quality control
    • Y. Takeda, K. Totani, I. Matsuo, and Y. Ito Chemical approaches toward understanding glycan-mediated protein quality control Curr. Opin. Chem. Biol. 13 2009 582 591
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 582-591
    • Takeda, Y.1    Totani, K.2    Matsuo, I.3    Ito, Y.4
  • 114
    • 84862659885 scopus 로고    scopus 로고
    • Recent developments in bacterial protein glycan coupling technology and glycoconjugate vaccine design
    • V.S. Terra, D.C. Mills, L.E. Yates, S. Abouelhadid, J. Cuccui, and B.W. Wren Recent developments in bacterial protein glycan coupling technology and glycoconjugate vaccine design J. Med. Microbiol. 61 2012 919 926
    • (2012) J. Med. Microbiol. , vol.61 , pp. 919-926
    • Terra, V.S.1    Mills, D.C.2    Yates, L.E.3    Abouelhadid, S.4    Cuccui, J.5    Wren, B.W.6
  • 115
    • 41949130819 scopus 로고    scopus 로고
    • Mutants of Mucor hiemalis endo-beta-N-acetylglucosaminidase show enhanced transglycosylation and glycosynthase-like activities
    • M. Umekawa, W. Huang, B. Li, K. Fujita, H. Ashida, L.X. Wang, and K. Yamamoto Mutants of Mucor hiemalis endo-beta-N-acetylglucosaminidase show enhanced transglycosylation and glycosynthase-like activities J. Biol. Chem. 283 2008 4469 4479
    • (2008) J. Biol. Chem. , vol.283 , pp. 4469-4479
    • Umekawa, M.1    Huang, W.2    Li, B.3    Fujita, K.4    Ashida, H.5    Wang, L.X.6    Yamamoto, K.7
  • 116
    • 73649089287 scopus 로고    scopus 로고
    • Efficient glycosynthase mutant derived from Mucor hiemalis endo-beta-N-acetylglucosaminidase capable of transferring oligosaccharide from both sugar oxazoline and natural N-glycan
    • M. Umekawa, C. Li, T. Higashiyama, W. Huang, H. Ashida, K. Yamamoto, and L.X. Wang Efficient glycosynthase mutant derived from Mucor hiemalis endo-beta-N-acetylglucosaminidase capable of transferring oligosaccharide from both sugar oxazoline and natural N-glycan J. Biol. Chem. 285 2010 511 521
    • (2010) J. Biol. Chem. , vol.285 , pp. 511-521
    • Umekawa, M.1    Li, C.2    Higashiyama, T.3    Huang, W.4    Ashida, H.5    Yamamoto, K.6    Wang, L.X.7
  • 117
    • 84876920942 scopus 로고    scopus 로고
    • Chemical assembly of N-glycoproteins: A refined toolbox to address a ubiquitous posttranslational modification
    • C. Unverzagt, and Y. Kajihara Chemical assembly of N-glycoproteins: a refined toolbox to address a ubiquitous posttranslational modification Chem. Soc. Rev. 42 2013 4408 4420
    • (2013) Chem. Soc. Rev. , vol.42 , pp. 4408-4420
    • Unverzagt, C.1    Kajihara, Y.2
  • 119
    • 34247622775 scopus 로고    scopus 로고
    • Expanding the diversity of chemical protein modification allows post-translational mimicry
    • DOI 10.1038/nature05757, PII NATURE05757
    • S.I. van Kasteren, H.B. Kramer, H.H. Jensen, S.J. Campbell, J. Kirkpatrick, N.J. Oldham, D.C. Anthony, and B.G. Davis Expanding the diversity of chemical protein modification allows post-translational mimicry Nature 446 2007 1105 1109 (Pubitemid 46676061)
    • (2007) Nature , vol.446 , Issue.7139 , pp. 1105-1109
    • Van Kasteren, S.I.1    Kramer, H.B.2    Jensen, H.H.3    Campbell, S.J.4    Kirkpatrick, J.5    Oldham, N.J.6    Anthony, D.C.7    Davis, B.G.8
  • 120
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • A. Varki Biological roles of oligosaccharides: all of the theories are correct Glycobiology 3 1993 97 130 (Pubitemid 23132602)
    • (1993) Glycobiology , vol.3 , Issue.2 , pp. 97-130
    • Varki, A.1
  • 121
    • 84867080246 scopus 로고    scopus 로고
    • Solving the convergence problem in the synthesis of triantennary N-glycan relevant to prostate-specific membrane antigen (PSMA)
    • M.A. Walczak, and S.J. Danishefsky Solving the convergence problem in the synthesis of triantennary N-glycan relevant to prostate-specific membrane antigen (PSMA) J. Am. Chem. Soc. 134 2012 16430 16433
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 16430-16433
    • Walczak, M.A.1    Danishefsky, S.J.2
  • 122
  • 123
    • 77958115264 scopus 로고    scopus 로고
    • A limited number of antibody specificities mediate broad and potent serum neutralization in selected HIV-1 infected individuals
    • L.M. Walker, M.D. Simek, F. Priddy, J.S. Gach, D. Wagner, M.B. Zwick, S.K. Phogat, P. Poignard, and D.R. Burton A limited number of antibody specificities mediate broad and potent serum neutralization in selected HIV-1 infected individuals PLoS Pathog. 6 2010 e1001028
    • (2010) PLoS Pathog. , vol.6 , pp. 1001028
    • 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
  • 125
    • 46549088526 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of glycopeptides and glycoproteins through endoglycosidase-catalyzed transglycosylation
    • L.X. Wang Chemoenzymatic synthesis of glycopeptides and glycoproteins through endoglycosidase-catalyzed transglycosylation Carbohydr. Res. 343 2008 1509 1522
    • (2008) Carbohydr. Res. , vol.343 , pp. 1509-1522
    • Wang, L.X.1
  • 126
    • 85015328820 scopus 로고    scopus 로고
    • The amazing transglycosylation activity of endo-beta-N- acetylglucosaminidases
    • L.X. Wang The amazing transglycosylation activity of endo-beta-N- acetylglucosaminidases Trends Glycosci. Glycotechnol. 23 2011 33 52
    • (2011) Trends Glycosci. Glycotechnol. , vol.23 , pp. 33-52
    • Wang, L.X.1
  • 127
    • 84890196169 scopus 로고    scopus 로고
    • Synthetic carbohydrate antigens for HIV vaccine design
    • L.X. Wang Synthetic carbohydrate antigens for HIV vaccine design Curr. Opin. Chem. Biol. 17 2013 997 1005
    • (2013) Curr. Opin. Chem. Biol. , vol.17 , pp. 997-1005
    • Wang, L.X.1
  • 128
    • 84862908666 scopus 로고    scopus 로고
    • Emerging technologies for making glycan-defined glycoproteins
    • L.X. Wang, and J.V. Lomino Emerging technologies for making glycan-defined glycoproteins ACS Chem. Biol. 7 2012 110 122
    • (2012) ACS Chem. Biol. , vol.7 , pp. 110-122
    • Wang, L.X.1    Lomino, J.V.2
  • 129
    • 84886867848 scopus 로고    scopus 로고
    • Realizing the Promise of Chemical Glycobiology
    • L.X. Wang, and B.G. Davis Realizing the Promise of Chemical Glycobiology Chem. Sci. 4 2013 3381 3394
    • (2013) Chem. Sci. , vol.4 , pp. 3381-3394
    • Wang, L.X.1    Davis, B.G.2
  • 130
    • 1142306158 scopus 로고    scopus 로고
    • Binding of High-Mannose-Type Oligosaccharides and Synthetic Oligomannose Clusters to Human Antibody 2G12: Implications for HIV-1 Vaccine Design
    • DOI 10.1016/S1074-5521(03)00299-0
    • L.X. Wang, J. Ni, S. Singh, and H. Li Binding of high-mannose-type oligosaccharides and synthetic oligomannose clusters to human antibody 2G12: implications for HIV-1 vaccine design Chem. Biol. 11 2004 127 134 (Pubitemid 38203997)
    • (2004) Chemistry and Biology , vol.11 , Issue.1 , pp. 127-134
    • Wang, L.-X.1    Ni, J.2    Singh, S.3    Li, H.4
  • 131
    • 38849132058 scopus 로고    scopus 로고
    • Processing of N-terminal unnatural amino acids in recombinant human interferon-β in Escherichia coli
    • DOI 10.1002/cbic.200700379
    • A. Wang, N. Winblade Nairn, R.S. Johnson, D.A. Tirrell, and K. Grabstein Processing of N-terminal unnatural amino acids in recombinant human interferon-beta in Escherichia coli ChemBioChem 9 2008 324 330 (Pubitemid 351196801)
    • (2008) ChemBioChem , vol.9 , Issue.2 , pp. 324-330
    • Wang, A.1    Nairn, N.W.2    Johnson, R.S.3    Tirrell, D.A.4    Grabstein, K.5
  • 135
    • 0141565183 scopus 로고    scopus 로고
    • Site-specific glycosylation of an aglycosylated human IgG1-Fc antibody protein generates neoglycoproteins with enhanced function
    • DOI 10.1016/j.chembiol.2003.08.006
    • G.M. Watt, J. Lund, M. Levens, V.S. Kolli, R. Jefferis, and G.J. Boons Site-specific glycosylation of an aglycosylated human IgG1-Fc antibody protein generates neoglycoproteins with enhanced function Chem. Biol. 10 2003 807 814 (Pubitemid 37171899)
    • (2003) Chemistry and Biology , vol.10 , Issue.9 , pp. 807-814
    • Watt, G.M.1    Lund, J.2    Levens, M.3    Kolli, V.S.K.4    Jefferis, R.5    Boons, G.-J.6
  • 136
    • 33646892873 scopus 로고    scopus 로고
    • Asparagine-linked protein glycosylation: From eukaryotic to prokaryotic systems
    • DOI 10.1093/glycob/cwj099
    • E. Weerapana, and B. Imperiali Asparagine-linked protein glycosylation: from eukaryotic to prokaryotic systems Glycobiology 16 2006 91R 101R (Pubitemid 43779042)
    • (2006) Glycobiology , vol.16 , Issue.6
    • Weerapana, E.1    Imperiali, B.2
  • 137
    • 52949115690 scopus 로고    scopus 로고
    • Glycoengineering of human IgG1-Fc through combined yeast expression and in vitro chemoenzymatic glycosylation
    • Y. Wei, C. Li, W. Huang, B. Li, S. Strome, and L.X. Wang Glycoengineering of human IgG1-Fc through combined yeast expression and in vitro chemoenzymatic glycosylation Biochemistry 47 2008 10294 10304
    • (2008) Biochemistry , vol.47 , pp. 10294-10304
    • Wei, Y.1    Li, C.2    Huang, W.3    Li, B.4    Strome, S.5    Wang, L.X.6
  • 138
    • 13444262282 scopus 로고    scopus 로고
    • The humanization of N-glycosylation pathways in yeast
    • DOI 10.1038/nrmicro1087
    • S. Wildt, and T.U. Gerngross The humanization of N-glycosylation pathways in yeast Nat. Rev. Microbiol. 3 2005 119 128 (Pubitemid 40207593)
    • (2005) Nature Reviews Microbiology , vol.3 , Issue.2 , pp. 119-128
    • Wildt, S.1    Gerngross, T.U.2
  • 139
    • 84885105341 scopus 로고    scopus 로고
    • A vision for vaccines built from fully synthetic tumor-associated antigens: From the laboratory to the clinic
    • R.M. Wilson, and S.J. Danishefsky A vision for vaccines built from fully synthetic tumor-associated antigens: from the laboratory to the clinic J. Am. Chem. Soc. 135 2013 14462 14472
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 14462-14472
    • Wilson, R.M.1    Danishefsky, S.J.2
  • 140
    • 84880392333 scopus 로고    scopus 로고
    • The winding pathway to erythropoietin along the chemistry-biology frontier: A success at last
    • R.M. Wilson, S. Dong, P. Wang, and S.J. Danishefsky The winding pathway to erythropoietin along the chemistry-biology frontier: a success at last Angew. Chem. Int. Ed. Engl. 52 2013 7646 7665
    • (2013) Angew. Chem. Int. Ed. Engl. , vol.52 , pp. 7646-7665
    • Wilson, R.M.1    Dong, S.2    Wang, P.3    Danishefsky, S.J.4
  • 141
    • 58149328976 scopus 로고    scopus 로고
    • Expanding the genetic code of Saccharomyces cerevisiae with methionine analogues
    • B. Wiltschi, W. Wenger, S. Nehring, and N. Budisa Expanding the genetic code of Saccharomyces cerevisiae with methionine analogues Yeast 25 2008 775 786
    • (2008) Yeast , vol.25 , pp. 775-786
    • Wiltschi, B.1    Wenger, W.2    Nehring, S.3    Budisa, N.4
  • 142
    • 0030936614 scopus 로고    scopus 로고
    • Enzymatic glycoprotein synthesis: Preparation of ribonuclease glycoforms via enzymatic glycopeptide condensation and glycosylation
    • DOI 10.1021/ja961846z, PII S000278639601846X
    • K. Witte, P. Sears, R. Martin, and C.H. Wong Enzymatic glycoprotein synthesis: Preparation of ribonuclease glycoforms via enzymatic glycopeptide condensation and glycosylation J. Am. Chem. Soc. 119 1997 2114 2118 (Pubitemid 27159977)
    • (1997) Journal of the American Chemical Society , vol.119 , Issue.9 , pp. 2114-2118
    • Witte, K.1    Sears, P.2    Martin, R.3    Wong, C.-H.4
  • 143
    • 62549121136 scopus 로고    scopus 로고
    • Site-specific chemical modification of recombinant proteins produced in mammalian cells by using the genetically encoded aldehyde tag
    • P. Wu, W. Shui, B.L. Carlson, N. Hu, D. Rabuka, J. Lee, and C.R. Bertozzi Site-specific chemical modification of recombinant proteins produced in mammalian cells by using the genetically encoded aldehyde tag Proc. Natl. Acad. Sci. USA 106 2009 3000 3005
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 3000-3005
    • Wu, P.1    Shui, W.2    Carlson, B.L.3    Hu, N.4    Rabuka, D.5    Lee, J.6    Bertozzi, C.R.7
  • 144
    • 0030608827 scopus 로고    scopus 로고
    • 15N-labeled peptide substrates as mechanistic probes of oligosaccharyltransferase
    • DOI 10.1021/bi9719511
    • T. Xu, and J.K. Coward 13C- and 15N-labeled peptide substrates as mechanistic probes of oligosaccharyltransferase Biochemistry 36 1997 14683 14689 (Pubitemid 27524388)
    • (1997) Biochemistry , vol.36 , Issue.48 , pp. 14683-14689
    • Xu, T.1    Coward, J.K.2
  • 145
    • 40149092211 scopus 로고    scopus 로고
    • Chemical synthesis of a glycoprotein having an intact human complex-type sialyloligosaccharide under the Boc and Fmoc synthetic strategies
    • DOI 10.1021/ja072543f
    • N. Yamamoto, Y. Tanabe, R. Okamoto, P.E. Dawson, and Y. Kajihara Chemical synthesis of a glycoprotein having an intact human complex-type sialyloligosaccharide under the Boc and Fmoc synthetic strategies J. Am. Chem. Soc. 130 2008 501 510 (Pubitemid 351455564)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.2 , pp. 501-510
    • Yamamoto, N.1    Tanabe, Y.2    Okamoto, R.3    Dawson, P.E.4    Kajihara, Y.5
  • 146
    • 77956037173 scopus 로고    scopus 로고
    • Toward fully synthetic, homogeneous glycoproteins: Advances in chemical ligation
    • Y. Yuan, J. Chen, Q. Wan, R.M. Wilson, and S.J. Danishefsky Toward fully synthetic, homogeneous glycoproteins: advances in chemical ligation Biopolymers 94 2010 373 384
    • (2010) Biopolymers , vol.94 , pp. 373-384
    • Yuan, Y.1    Chen, J.2    Wan, Q.3    Wilson, R.M.4    Danishefsky, S.J.5
  • 147
    • 0036462599 scopus 로고    scopus 로고
    • The emerging significance of O-GlcNAc in cellular regulation
    • DOI 10.1021/cr000406u
    • N.E. Zachara, and G.W. Hart The emerging significance of O-GlcNAc in cellular regulation Chem. Rev. 102 2002 431 438 (Pubitemid 35377621)
    • (2002) Chemical Reviews , vol.102 , Issue.2 , pp. 431-438
    • Zachara, N.E.1    Hart, G.W.2
  • 148
    • 0030933129 scopus 로고    scopus 로고
    • Conformation-independent binding of monoglucosylated ribonuclease B to calnexin
    • A. Zapun, S.M. Petrescu, P.M. Rudd, R.A. Dwek, D.Y. Thomas, and J.J. Bergeron Conformation-independent binding of monoglucosylated ribonuclease B to calnexin Cell 88 1997 29 38 (Pubitemid 27180328)
    • (1997) Cell , vol.88 , Issue.1 , pp. 29-38
    • Zapun, A.1    Petrescu, S.M.2    Rudd, P.M.3    Dwek, R.A.4    Thomas, D.Y.5    Bergeron, J.J.M.6
  • 149
    • 83055166012 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis and Fcγ receptor binding of homogeneous glycoforms of antibody Fc domain. Presence of a bisecting sugar moiety enhances the affinity of Fc to FcγIIIa receptor
    • G. Zou, H. Ochiai, W. Huang, Q. Yang, C. Li, and L.X. Wang Chemoenzymatic synthesis and Fcγ receptor binding of homogeneous glycoforms of antibody Fc domain. Presence of a bisecting sugar moiety enhances the affinity of Fc to FcγIIIa receptor J. Am. Chem. Soc. 133 2011 18975 18991
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 18975-18991
    • Zou, G.1    Ochiai, H.2    Huang, W.3    Yang, Q.4    Li, C.5    Wang, L.X.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.