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Volumn 22, Issue , 2014, Pages 92-99

Decoration of proteins with sugar chains: Recent advances in glycoprotein synthesis

Author keywords

[No Author keywords available]

Indexed keywords

ANTIFREEZE PROTEIN; ERYTHROPOIETIN; GLYCOPROTEIN; OLIGOSACCHARIDE; PROTEIN PRECURSOR;

EID: 84907809410     PISSN: 13675931     EISSN: 18790402     Source Type: Journal    
DOI: 10.1016/j.cbpa.2014.09.029     Document Type: Review
Times cited : (18)

References (46)
  • 1
    • 0001094662 scopus 로고    scopus 로고
    • Glycobiology: toward understanding the function of sugars
    • Dwek R.A. Glycobiology: toward understanding the function of sugars. Chem Rev 1996, 96:683-720.
    • (1996) Chem Rev , vol.96 , pp. 683-720
    • Dwek, R.A.1
  • 2
    • 33749860977 scopus 로고    scopus 로고
    • Post-translational modifications in the context of therapeutic proteins
    • Walsh G., Jefferis R. Post-translational modifications in the context of therapeutic proteins. Nat Biotechnol 2006, 24:1241-1252.
    • (2006) Nat Biotechnol , vol.24 , pp. 1241-1252
    • Walsh, G.1    Jefferis, R.2
  • 4
    • 84864238717 scopus 로고    scopus 로고
    • Chemoenzymatic glycoengineering of intact IgG antibodies for gain of functions
    • Huang W., Giddens J., Fan S.-Q., Toonstra C., Wang L.-X. Chemoenzymatic glycoengineering of intact IgG antibodies for gain of functions. J Am Chem Soc 2012, 134:12308-12318.
    • (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
  • 5
    • 84860802199 scopus 로고    scopus 로고
    • Chemical synthesis of intentionally misfolded homogeneous glycoprotein: a unique approach for the study of glycoprotein quality control
    • Izumi M., Makimura Y., Dedola S., Seko A., Kanamori A., Sakono M., Ito Y., Kajihara Y. Chemical synthesis of intentionally misfolded homogeneous glycoprotein: a unique approach for the study of glycoprotein quality control. J Am Chem Soc 2012, 134:7238-7241.
    • (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
  • 6
    • 84859524073 scopus 로고    scopus 로고
    • Chemical synthesis of an erythropoietin glycoform containing a complex-type disialyloligosaccharide
    • Murakami M., Okamoto R., Izumi M., Kajihara Y. Chemical synthesis of an erythropoietin glycoform containing a complex-type disialyloligosaccharide. Angew Chem Int Ed 2012, 51:3567-3572.
    • (2012) Angew Chem Int Ed , vol.51 , pp. 3567-3572
    • Murakami, M.1    Okamoto, R.2    Izumi, M.3    Kajihara, Y.4
  • 9
    • 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
    • Asahina Y., Kamitori S., Takao T., Nishi N., Hojo H. 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 2013, 52:9733-9737.
    • (2013) Angew Chem Int Ed , vol.52 , pp. 9733-9737
    • Asahina, Y.1    Kamitori, S.2    Takao, T.3    Nishi, N.4    Hojo, H.5
  • 10
    • 84880572002 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis and lectin recognition of a selectively fluorinated glycoprotein
    • Orwenyo J., Huang W., Wang L.-X. Chemoenzymatic synthesis and lectin recognition of a selectively fluorinated glycoprotein. Bioorg Med Chem 2013, 21:4768-4777.
    • (2013) Bioorg Med Chem , vol.21 , pp. 4768-4777
    • Orwenyo, J.1    Huang, W.2    Wang, L.-X.3
  • 11
    • 84880361310 scopus 로고    scopus 로고
    • Chemical synthesis of biologically active monoglycosylated GM2-activator protein analogue using N-sulfanylethylanilide peptide
    • Sato K., Shigenaga A., Kitakaze K., Sakamoto K., Tsuji D., Itoh K., Otaka A. Chemical synthesis of biologically active monoglycosylated GM2-activator protein analogue using N-sulfanylethylanilide peptide. Angew Chem Int Ed 2013, 52:7855-7859.
    • (2013) Angew Chem Int Ed , vol.52 , pp. 7855-7859
    • Sato, K.1    Shigenaga, A.2    Kitakaze, K.3    Sakamoto, K.4    Tsuji, D.5    Itoh, K.6    Otaka, A.7
  • 13
    • 84900020060 scopus 로고    scopus 로고
    • Total chemical synthesis and biological activities of glycosylated and non-glycosylated forms of the chemokines CCL1 and Ser-CCL1
    • Okamoto R., Mandal K., Ling M., Luster A.D., Kajihara Y., Kent S.B.H. Total chemical synthesis and biological activities of glycosylated and non-glycosylated forms of the chemokines CCL1 and Ser-CCL1. Angew Chem Int Ed 2014, 53:5188-5193.
    • (2014) Angew Chem Int Ed , vol.53 , pp. 5188-5193
    • Okamoto, R.1    Mandal, K.2    Ling, M.3    Luster, A.D.4    Kajihara, Y.5    Kent, S.B.H.6
  • 14
    • 84900033420 scopus 로고    scopus 로고
    • (Quasi-)racemic X-ray structures of glycosylated and non-glycosylated forms of the chemokine Ser-CCL1 prepared by total chemical synthesis
    • Okamoto R., Mandal K., Sawaya M.R., Kajihara Y., Yeates T.O., Kent S.B.H. (Quasi-)racemic X-ray structures of glycosylated and non-glycosylated forms of the chemokine Ser-CCL1 prepared by total chemical synthesis. Angew Chem Int Ed 2014, 53:5194-5198.
    • (2014) Angew Chem Int Ed , vol.53 , pp. 5194-5198
    • Okamoto, R.1    Mandal, K.2    Sawaya, M.R.3    Kajihara, Y.4    Yeates, T.O.5    Kent, S.B.H.6
  • 16
    • 84896823976 scopus 로고    scopus 로고
    • Synthesis of granulocyte-macrophage colony-stimulating factor as homogeneous glycoforms and early comparisons with yeast cell-derived material
    • Zhang Q., Johnston E.V., Shieh J.-H., Moore M.A.S., Danishefsky S.J. Synthesis of granulocyte-macrophage colony-stimulating factor as homogeneous glycoforms and early comparisons with yeast cell-derived material. Proc Natl Acad Sci U S A 2014, 111:2885-2890.
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 2885-2890
    • Zhang, Q.1    Johnston, E.V.2    Shieh, J.-H.3    Moore, M.A.S.4    Danishefsky, S.J.5
  • 18
    • 84857383999 scopus 로고    scopus 로고
    • Total synthesis of the α-subunit of human glycoprotein hormones: toward fully synthetic homogeneous human follicle-stimulating hormone
    • Aussedat B., Fasching B., Johnston E., Sane N., Nagorny P., Danishefsky S.J. Total synthesis of the α-subunit of human glycoprotein hormones: toward fully synthetic homogeneous human follicle-stimulating hormone. J Am Chem Soc 2012, 134:3532-3541.
    • (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
  • 19
  • 20
    • 84876920942 scopus 로고    scopus 로고
    • Chemical assembly of N-glycoproteins: a refined toolbox to address a ubiquitous posttranslational modification
    • Unverzagt C., Kajihara Y. Chemical assembly of N-glycoproteins: a refined toolbox to address a ubiquitous posttranslational modification. Chem Soc Rev 2013, 42:4408-4420.
    • (2013) Chem Soc Rev , vol.42 , pp. 4408-4420
    • Unverzagt, C.1    Kajihara, Y.2
  • 21
    • 84892662416 scopus 로고    scopus 로고
    • Chemical and chemoenzymatic synthesis of glycoproteins for deciphering functions
    • Wang L.-X., Amin M.N. Chemical and chemoenzymatic synthesis of glycoproteins for deciphering functions. Chem Biol 2014, 21:51-66.
    • (2014) Chem Biol , vol.21 , pp. 51-66
    • Wang, L.-X.1    Amin, M.N.2
  • 22
    • 0033397158 scopus 로고    scopus 로고
    • Polypeptide synthesis by the thioester method
    • Aimoto S. Polypeptide synthesis by the thioester method. Biopolymers 1999, 51:247-265.
    • (1999) Biopolymers , vol.51 , pp. 247-265
    • Aimoto, S.1
  • 23
    • 62449282062 scopus 로고    scopus 로고
    • Total chemical synthesis of proteins
    • Kent S.B.H. Total chemical synthesis of proteins. Chem Soc Rev 2009, 38:338-351.
    • (2009) Chem Soc Rev , vol.38 , pp. 338-351
    • Kent, S.B.H.1
  • 24
    • 0001270462 scopus 로고
    • A practical, convergent method for glycopeptide synthesis
    • Cohen-Anisfeld S.T., Lansbury P.T. A practical, convergent method for glycopeptide synthesis. J Am Chem Soc 1993, 115:10531-10537.
    • (1993) J Am Chem Soc , vol.115 , pp. 10531-10537
    • Cohen-Anisfeld, S.T.1    Lansbury, P.T.2
  • 25
    • 84868518416 scopus 로고    scopus 로고
    • Convergent solid-phase synthesis of N-glycopeptides facilitated by pseudoprolines at consensus-sequence Ser/Thr residues
    • Ullmann V., Rädisch M., Boos I., Freund J., Pöhner C., Schwarzinger S., Unverzagt C. Convergent solid-phase synthesis of N-glycopeptides facilitated by pseudoprolines at consensus-sequence Ser/Thr residues. Angew Chem Int Ed 2012, 51:11566-11570.
    • (2012) Angew Chem Int Ed , vol.51 , pp. 11566-11570
    • Ullmann, V.1    Rädisch, M.2    Boos, I.3    Freund, J.4    Pöhner, C.5    Schwarzinger, S.6    Unverzagt, C.7
  • 26
    • 84868568294 scopus 로고    scopus 로고
    • An advance in the chemical synthesis of homogeneous N-linked glycopolypeptides by convergent aspartylation
    • Wang P., Aussedat B., Vohra Y., Danishefsky S.J. An advance in the chemical synthesis of homogeneous N-linked glycopolypeptides by convergent aspartylation. Angew Chem Int Ed 2012, 51:11571-11575.
    • (2012) Angew Chem Int Ed , vol.51 , pp. 11571-11575
    • Wang, P.1    Aussedat, B.2    Vohra, Y.3    Danishefsky, S.J.4
  • 27
    • 77949402878 scopus 로고    scopus 로고
    • Study of on-resin convergent synthesis of N-linked glycopeptides containing a large high mannose N-linked oligosaccharide
    • Chen R., Tolbert T.J. Study of on-resin convergent synthesis of N-linked glycopeptides containing a large high mannose N-linked oligosaccharide. J Am Chem Soc 2010, 132:3211-3216.
    • (2010) J Am Chem Soc , vol.132 , pp. 3211-3216
    • Chen, R.1    Tolbert, T.J.2
  • 29
    • 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
    • Kajihara Y., Suzuki Y., Yamamoto N., Sasaki K., Sakakibara T., Juneja L.R. 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. Chem Eur J 2004, 10:971-985.
    • (2004) Chem Eur J , vol.10 , pp. 971-985
    • Kajihara, Y.1    Suzuki, Y.2    Yamamoto, N.3    Sasaki, K.4    Sakakibara, T.5    Juneja, L.R.6
  • 30
    • 0026702568 scopus 로고
    • Role of sugar chains in the expression of the biological activity of human erythropoietin
    • Higuchi M., Oh-eda M., Kuboniwa H., Tomonoh K., Shimonaka Y., Ochi N. Role of sugar chains in the expression of the biological activity of human erythropoietin. J Biol Chem 1992, 267:7703-7709.
    • (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
  • 31
    • 0016304768 scopus 로고
    • A biological antifreeze: a glycoprotein in the blood of polar fishes lowers the freezing temperature
    • Feeney R.E. A biological antifreeze: a glycoprotein in the blood of polar fishes lowers the freezing temperature. Am Sci 1974, 62:712-719.
    • (1974) Am Sci , vol.62 , pp. 712-719
    • Feeney, R.E.1
  • 32
    • 33646910318 scopus 로고    scopus 로고
    • Convenient synthesis of a sialylglycopeptide-thioester having an intact and homogeneous complex-type disialyl-oligosaccharide
    • Kajihara Y., Yoshihara A., Hirano K., Yamamoto N. Convenient synthesis of a sialylglycopeptide-thioester having an intact and homogeneous complex-type disialyl-oligosaccharide. Carbohydr Res 2006, 341:1333-1340.
    • (2006) Carbohydr Res , vol.341 , pp. 1333-1340
    • Kajihara, Y.1    Yoshihara, A.2    Hirano, K.3    Yamamoto, N.4
  • 33
    • 61649087668 scopus 로고    scopus 로고
    • Glycosylation as a strategy to improve antibody-based therapeutics
    • Jefferis R. Glycosylation as a strategy to improve antibody-based therapeutics. Nat Rev Drug Discov 2009, 8:226-234.
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 226-234
    • Jefferis, R.1
  • 34
  • 36
    • 0035801838 scopus 로고    scopus 로고
    • A novel disaccharide substrate having 1,2-oxazoline moiety for detection of transglycosylating activity of endoglycosidases
    • Fujita M., Shoda S.-I., Haneda K., Inazu T., Takegawa K., Yamamoto K. A novel disaccharide substrate having 1,2-oxazoline moiety for detection of transglycosylating activity of endoglycosidases. Biochim Biophys Acta 2001, 1528:9-14.
    • (2001) Biochim Biophys Acta , vol.1528 , pp. 9-14
    • Fujita, M.1    Shoda, S.-I.2    Haneda, K.3    Inazu, T.4    Takegawa, K.5    Yamamoto, K.6
  • 37
    • 22144450662 scopus 로고    scopus 로고
    • Highly efficient endoglycosidase-catalyzed synthesis of glycopeptides using oligosaccharide oxazolines as donor substrates
    • Li B., Zeng Y., Hauser S., Song H., Wang L.-X. Highly efficient endoglycosidase-catalyzed synthesis of glycopeptides using oligosaccharide oxazolines as donor substrates. J Am Chem Soc 2005, 127:9692-9693.
    • (2005) J Am Chem Soc , vol.127 , pp. 9692-9693
    • Li, B.1    Zeng, Y.2    Hauser, S.3    Song, H.4    Wang, L.-X.5
  • 38
    • 33747181055 scopus 로고    scopus 로고
    • Endohexosaminidase M: exploring and exploiting enzyme substrate specificity
    • Rising T.W.D.F., Claridge T.D.W., Moir J.W.B., Fairbanks A.J. Endohexosaminidase M: exploring and exploiting enzyme substrate specificity. ChemBioChem 2006, 7:1177-1180.
    • (2006) ChemBioChem , vol.7 , pp. 1177-1180
    • Rising, T.W.D.F.1    Claridge, T.D.W.2    Moir, J.W.B.3    Fairbanks, A.J.4
  • 39
    • 67749122310 scopus 로고    scopus 로고
    • Glycosynthases enable a highly efficient chemoenzymatic synthesis of N-glycoproteins carrying intact natural N-glycans
    • Huang W., Li C., Li B., Umekawa M., Yamamoto K., Zhang X., Wang L.-X. Glycosynthases enable a highly efficient chemoenzymatic synthesis of N-glycoproteins carrying intact natural N-glycans. J Am Chem Soc 2009, 131:2214-2223.
    • (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
  • 40
    • 84922686798 scopus 로고    scopus 로고
    • Misfolded glycoproteins as probes for analysis of folding sensor enzyme UDP-glucose: glycoprotein glucosyltransferase
    • Izumi M., Kiuchi T., Ito Y., Kajihara Y. Misfolded glycoproteins as probes for analysis of folding sensor enzyme UDP-glucose: glycoprotein glucosyltransferase. Trends Glycosci Glycotechnol 2013, 25:1-12.
    • (2013) Trends Glycosci Glycotechnol , vol.25 , pp. 1-12
    • Izumi, M.1    Kiuchi, T.2    Ito, Y.3    Kajihara, Y.4
  • 41
    • 0033782777 scopus 로고    scopus 로고
    • Protein glycosylation and its role in protein folding
    • Parodi A.J. Protein glycosylation and its role in protein folding. Annu Rev Biochem 2000, 69:69-93.
    • (2000) Annu Rev Biochem , vol.69 , pp. 69-93
    • Parodi, A.J.1
  • 42
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • Helenius A., Aebi M. Roles of N-linked glycans in the endoplasmic reticulum. Annu Rev Biochem 2004, 73:1019-1049.
    • (2004) Annu Rev Biochem , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 43
    • 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
    • Makimura Y., Kiuchi T., Izumi M., Dedola S., Ito Y., Kajihara Y. Efficient synthesis of glycopeptide-α-thioesters with a high-mannose type oligosaccharide by means of tert-Boc-solid phase peptide synthesis. Carbohydr Res 2012, 364:41-48.
    • (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
  • 44
  • 46
    • 84861378744 scopus 로고    scopus 로고
    • Racemic protein crystallography
    • Yeates T.O., Kent S.B.H. Racemic protein crystallography. Annu Rev Biophys 2012, 41:41-61.
    • (2012) Annu Rev Biophys , vol.41 , pp. 41-61
    • Yeates, T.O.1    Kent, S.B.H.2


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