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Volumn 9, Issue 2, 2014, Pages 390-397

Traceless labeling of glycoproteins and its application to the study of glycoprotein-protein interactions

Author keywords

[No Author keywords available]

Indexed keywords

BORONIC ACID DERIVATIVE; CARBOHYDRATE; CONCANAVALIN A; ETHER; FETUIN; GLYCAN; GLYCOPROTEIN; LECTIN; POLYOL; WHEAT GERM AGGLUTININ;

EID: 84896722046     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb400631w     Document Type: Article
Times cited : (17)

References (37)
  • 1
    • 45749151511 scopus 로고    scopus 로고
    • Chemoselective modification of proteins: Hitting the target
    • Carrico, I. S. (2008) Chemoselective modification of proteins: hitting the target Chem. Soc. Rev. 37, 1423-1431
    • (2008) Chem. Soc. Rev. , vol.37 , pp. 1423-1431
    • Carrico, I.S.1
  • 2
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien, R. Y. (1998) The green fluorescent protein Annu. Rev. Biochem. 67, 509-544
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 3
    • 77949546659 scopus 로고    scopus 로고
    • Protein chemical modification on endogenous amino acids
    • Baslé, E., Joubert, N., and Pucheault, M. (2010) Protein chemical modification on endogenous amino acids Chem. Biol. 17, 213-227
    • (2010) Chem. Biol. , vol.17 , pp. 213-227
    • Baslé, E.1    Joubert, N.2    Pucheault, M.3
  • 4
    • 78349313682 scopus 로고    scopus 로고
    • How to obtain labeled proteins and what to do with them
    • Hinner, M. J. and Johnsson, K. (2010) How to obtain labeled proteins and what to do with them Curr. Opin. Biotechnol. 21, 766-776
    • (2010) Curr. Opin. Biotechnol. , vol.21 , pp. 766-776
    • Hinner, M.J.1    Johnsson, K.2
  • 5
    • 13844306318 scopus 로고    scopus 로고
    • Enzymatic activity on a chip: The critical role of protein orientation
    • Cha, T., Guo, A., and Zhu, X. Y. (2005) Enzymatic activity on a chip: the critical role of protein orientation Proteomic 5, 416-419
    • (2005) Proteomic , vol.5 , pp. 416-419
    • Cha, T.1    Guo, A.2    Zhu, X.Y.3
  • 6
    • 33746294443 scopus 로고    scopus 로고
    • Site-specific protein modification through Cu(I)-catalyzed 1,2,3-triazole formation and its implementation in protein microarray fabrication
    • Lin, P. C., Ueng, S. H., Tseng, M. C., Ko, J. L., Huang, K. T., Yu, S. C., Adak, A. K., Chen, Y. J., and Lin, C. C. (2006) Site-specific protein modification through Cu(I)-catalyzed 1,2,3-triazole formation and its implementation in protein microarray fabrication Angew. Chem., Int. Ed. 45, 4286-4290
    • (2006) Angew. Chem., Int. Ed. , vol.45 , pp. 4286-4290
    • Lin, P.C.1    Ueng, S.H.2    Tseng, M.C.3    Ko, J.L.4    Huang, K.T.5    Yu, S.C.6    Adak, A.K.7    Chen, Y.J.8    Lin, C.C.9
  • 7
    • 70349917806 scopus 로고    scopus 로고
    • Bioorthogonal chemistry: Fishing for selectivity in a sea of functionality
    • Sletten, E. M. and Bertozzi, C. R. (2009) Bioorthogonal chemistry: fishing for selectivity in a sea of functionality Angew. Chem., Int. Ed. 48, 6974-6998
    • (2009) Angew. Chem., Int. Ed. , vol.48 , pp. 6974-6998
    • Sletten, E.M.1    Bertozzi, C.R.2
  • 8
    • 77249089970 scopus 로고    scopus 로고
    • Bioorthogonal chemistry: Recent progress and future directions
    • Lim, R. K. and Lin, Q. (2010) Bioorthogonal chemistry: recent progress and future directions Chem. Commun. (Cambridge) 46, 1589-1600
    • (2010) Chem. Commun. (Cambridge) , vol.46 , pp. 1589-1600
    • Lim, R.K.1    Lin, Q.2
  • 9
    • 0034677879 scopus 로고    scopus 로고
    • Cell surface engineering by a modified Staudinger reaction
    • Saxon, E. and Bertozzi, C. R. (2000) Cell surface engineering by a modified Staudinger reaction Science 287, 2007-2010
    • (2000) Science , vol.287 , pp. 2007-2010
    • Saxon, E.1    Bertozzi, C.R.2
  • 10
    • 0035917812 scopus 로고    scopus 로고
    • Expanding the genetic code of Escherichia coli
    • Wang, L., Brock, A., Herberich, B., and Schultz, P. G. (2001) Expanding the genetic code of Escherichia coli Science 292, 498-500
    • (2001) Science , vol.292 , pp. 498-500
    • Wang, L.1    Brock, A.2    Herberich, B.3    Schultz, P.G.4
  • 11
    • 0036022519 scopus 로고    scopus 로고
    • Proteomic profiling of mechanistically distinct enzyme classes using a common chemotype
    • Adam, G. C., Sorensen, E. J., and Cravatt, B. F. (2002) Proteomic profiling of mechanistically distinct enzyme classes using a common chemotype Nat. Biotechnol. 20, 805-809
    • (2002) Nat. Biotechnol. , vol.20 , pp. 805-809
    • Adam, G.C.1    Sorensen, E.J.2    Cravatt, B.F.3
  • 12
    • 35848965006 scopus 로고    scopus 로고
    • Activity-based protein profiling for the functional annotation of enzymes
    • Barglow, K. T. and Cravatt, B. F. (2007) Activity-based protein profiling for the functional annotation of enzymes Nat. Methods 4, 822-827
    • (2007) Nat. Methods , vol.4 , pp. 822-827
    • Barglow, K.T.1    Cravatt, B.F.2
  • 13
    • 0035113229 scopus 로고    scopus 로고
    • Profiling the specific reactivity of the proteome with non-directed activity-based probes
    • Adam, G. C., Cravatt, B. F., and Sorensen, E. J. (2001) Profiling the specific reactivity of the proteome with non-directed activity-based probes Chem. Biol. 8, 81-95
    • (2001) Chem. Biol. , vol.8 , pp. 81-95
    • Adam, G.C.1    Cravatt, B.F.2    Sorensen, E.J.3
  • 14
    • 0034614067 scopus 로고    scopus 로고
    • A general semisynthetic method for fluorescent saccharide-biosensors based on a lectin
    • Hamachi, I., Nagase, T., and Shinkai, S. (2000) A general semisynthetic method for fluorescent saccharide-biosensors based on a lectin J. Am. Chem. Soc. 122, 12065-12066
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 12065-12066
    • Hamachi, I.1    Nagase, T.2    Shinkai, S.3
  • 15
    • 84857850984 scopus 로고    scopus 로고
    • Ligand-directed acyl imidazole chemistry for labeling of membrane-bound proteins on live cells
    • Fujishima, S. H., Yasui, R., Miki, T., Ojida, A., and Hamachi, I. (2012) Ligand-directed acyl imidazole chemistry for labeling of membrane-bound proteins on live cells J. Am. Chem. Soc. 134, 3961-3964
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 3961-3964
    • Fujishima, S.H.1    Yasui, R.2    Miki, T.3    Ojida, A.4    Hamachi, I.5
  • 16
    • 38349008463 scopus 로고    scopus 로고
    • Target-specific chemical acylation of lectins by ligand-tethered DMAP catalysts
    • Koshi, Y., Nakata, E., Miyagawa, M., Tsukiji, S., Ogawa, T., and Hamachi, I. (2008) Target-specific chemical acylation of lectins by ligand-tethered DMAP catalysts J. Am. Chem. Soc. 130, 245-251
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 245-251
    • Koshi, Y.1    Nakata, E.2    Miyagawa, M.3    Tsukiji, S.4    Ogawa, T.5    Hamachi, I.6
  • 17
    • 33644946430 scopus 로고    scopus 로고
    • One-pot and sequential organic chemistry on an enzyme surface to tether a fluorescent probe at the proximity of the active site with restoring enzyme activity
    • Takaoka, Y., Tsutsumi, H., Kasagi, N., Nakata, E., and Hamachi, I. (2006) One-pot and sequential organic chemistry on an enzyme surface to tether a fluorescent probe at the proximity of the active site with restoring enzyme activity J. Am. Chem. Soc. 128, 3273-3280
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 3273-3280
    • Takaoka, Y.1    Tsutsumi, H.2    Kasagi, N.3    Nakata, E.4    Hamachi, I.5
  • 18
    • 84866384527 scopus 로고    scopus 로고
    • Traceless affinity labeling of endogenous proteins for functional analysis in living cells
    • Hayashi, T. and Hamachi, I. (2012) Traceless affinity labeling of endogenous proteins for functional analysis in living cells Acc. Chem. Res. 45, 1460-1469
    • (2012) Acc. Chem. Res. , vol.45 , pp. 1460-1469
    • Hayashi, T.1    Hamachi, I.2
  • 20
    • 67649628228 scopus 로고    scopus 로고
    • Quenched ligand-directed tosylate reagents for one-step construction of turn-on fluorescent biosensors
    • Tsukiji, S., Wang, H., Miyagawa, M., Tamura, T., Takaoka, Y., and Hamachi, I. (2009) Quenched ligand-directed tosylate reagents for one-step construction of turn-on fluorescent biosensors J. Am. Chem. Soc. 131, 9046-9054
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 9046-9054
    • Tsukiji, S.1    Wang, H.2    Miyagawa, M.3    Tamura, T.4    Takaoka, Y.5    Hamachi, I.6
  • 21
    • 84856433232 scopus 로고    scopus 로고
    • Native FKBP12 engineering by ligand-directed tosyl chemistry: Labeling properties and application to photo-cross-linking of protein complexes in vitro and in living cells
    • Tamura, T., Tsukiji, S., and Hamachi, I. (2012) Native FKBP12 engineering by ligand-directed tosyl chemistry: labeling properties and application to photo-cross-linking of protein complexes in vitro and in living cells J. Am. Chem. Soc. 134, 2216-2226
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 2216-2226
    • Tamura, T.1    Tsukiji, S.2    Hamachi, I.3
  • 22
    • 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
  • 23
    • 33846818820 scopus 로고    scopus 로고
    • Chemical methods for glycoprotein discovery
    • Bond, M. R. and Kohler, J. J. (2007) Chemical methods for glycoprotein discovery Curr. Opin. Chem. Biol. 11, 52-58
    • (2007) Curr. Opin. Chem. Biol. , vol.11 , pp. 52-58
    • Bond, M.R.1    Kohler, J.J.2
  • 25
    • 84866506114 scopus 로고    scopus 로고
    • Design of a "turn-off/turn-on" biosensor: Understanding carbohydrate-lectin interactions for use in noncovalent drug delivery
    • Gorityala, B. K., Lu, Z., and Leow, X. W. (2012) Design of a "turn-off/turn-on" biosensor: understanding carbohydrate-lectin interactions for use in noncovalent drug delivery J. Am. Chem. Soc. 134, 15229-15232
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 15229-15232
    • Gorityala, B.K.1    Lu, Z.2    Leow, X.W.3
  • 26
    • 84862062666 scopus 로고    scopus 로고
    • Molecular logic with a saccharide probe on the few-molecules level
    • Elstner, M., Weisshart, K., Mullen, K., and Schiller, A. (2012) Molecular logic with a saccharide probe on the few-molecules level J. Am. Chem. Soc. 134, 8098-8100
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 8098-8100
    • Elstner, M.1    Weisshart, K.2    Mullen, K.3    Schiller, A.4
  • 27
    • 84866483987 scopus 로고    scopus 로고
    • Self-propelled carbohydrate-sensitive microtransporters with built-in boronic acid recognition for isolating sugars and cells
    • Kuralay, F., Sattayasamitsathit, S., Gao, W., Uygun, A., Katzenberg, A., and Wang, J. (2012) Self-propelled carbohydrate-sensitive microtransporters with built-in boronic acid recognition for isolating sugars and cells J. Am. Chem. Soc. 134, 15217-15220
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 15217-15220
    • Kuralay, F.1    Sattayasamitsathit, S.2    Gao, W.3    Uygun, A.4    Katzenberg, A.5    Wang, J.6
  • 29
    • 45749142499 scopus 로고    scopus 로고
    • Carbohydrate arrays as tools for research and diagnostics
    • Horlacher, T. and Seeberger, P. H. (2008) Carbohydrate arrays as tools for research and diagnostics Chem. Soc. Rev. 37, 1414-1422
    • (2008) Chem. Soc. Rev. , vol.37 , pp. 1414-1422
    • Horlacher, T.1    Seeberger, P.H.2
  • 30
    • 70349286075 scopus 로고    scopus 로고
    • Glycomic analysis: An array of technologies
    • Krishnamoorthy, L. and Mahal, L. K. (2009) Glycomic analysis: an array of technologies ACS Chem. Biol. 4, 715-732
    • (2009) ACS Chem. Biol. , vol.4 , pp. 715-732
    • Krishnamoorthy, L.1    Mahal, L.K.2
  • 31
    • 53049085180 scopus 로고    scopus 로고
    • Glycoconjugate microarray based on an evanescent-field fluorescence-assisted detection principle for investigation of glycan-binding proteins
    • Tateno, H., Mori, A., Uchiyama, N., Yabe, R., Iwaki, J., Shikanai, T., Angata, T., Narimatsu, H., and Hirabayashi, J. (2008) Glycoconjugate microarray based on an evanescent-field fluorescence-assisted detection principle for investigation of glycan-binding proteins Glycobiology 18, 789-798
    • (2008) Glycobiology , vol.18 , pp. 789-798
    • Tateno, H.1    Mori, A.2    Uchiyama, N.3    Yabe, R.4    Iwaki, J.5    Shikanai, T.6    Angata, T.7    Narimatsu, H.8    Hirabayashi, J.9
  • 32
    • 34249341648 scopus 로고    scopus 로고
    • Glycoprotein microarrays with multi-lectin detection: Unique lectin binding patterns as a tool for classifying normal, chronic pancreatitis and pancreatic cancer sera
    • Zhao, J., Patwa, T. H., Qiu, W., Shedden, K., Hinderer, R., Misek, D. E., Anderson, M. A., Simeone, D. M., and Lubman, D. M. (2007) Glycoprotein microarrays with multi-lectin detection: unique lectin binding patterns as a tool for classifying normal, chronic pancreatitis and pancreatic cancer sera J. Proteome Res. 6, 1864-1874
    • (2007) J. Proteome Res. , vol.6 , pp. 1864-1874
    • Zhao, J.1    Patwa, T.H.2    Qiu, W.3    Shedden, K.4    Hinderer, R.5    Misek, D.E.6    Anderson, M.A.7    Simeone, D.M.8    Lubman, D.M.9
  • 33
    • 3042646556 scopus 로고    scopus 로고
    • Oligosaccharide and glycoprotein microarrays as tools in HIV glycobiology: Glycan-dependent gp120/protein interactions
    • Adams, E. W., Ratner, D. M., Bokesch, H. R., McMahon, J. B., O'Keefe, B. R., and Seeberger, P. H. (2004) Oligosaccharide and glycoprotein microarrays as tools in HIV glycobiology: glycan-dependent gp120/protein interactions Chem. Biol. 11, 875-881
    • (2004) Chem. Biol. , vol.11 , pp. 875-881
    • Adams, E.W.1    Ratner, D.M.2    Bokesch, H.R.3    McMahon, J.B.4    O'Keefe, B.R.5    Seeberger, P.H.6
  • 34
    • 0016245734 scopus 로고
    • Structure of the O-glycosidically linked carbohydrate units of fetuin
    • Spiro, R. G. and Bhoyroo, V. D. (1974) Structure of the O-glycosidically linked carbohydrate units of fetuin J. Biol. Chem. 249, 5704-5717
    • (1974) J. Biol. Chem. , vol.249 , pp. 5704-5717
    • Spiro, R.G.1    Bhoyroo, V.D.2
  • 35
    • 0023055757 scopus 로고
    • Asparagine-linked sugar chains of fetuin: Occurrence of tetrasialyl triantennary sugar chains containing the Galβ1→3GlcNAc sequence
    • Takasaki, S. and Kobata, A. (1986) Asparagine-linked sugar chains of fetuin: occurrence of tetrasialyl triantennary sugar chains containing the Galβ1→3GlcNAc sequence Biochemistry 25, 5709-5715
    • (1986) Biochemistry , vol.25 , pp. 5709-5715
    • Takasaki, S.1    Kobata, A.2
  • 36
    • 0034166581 scopus 로고    scopus 로고
    • Presence of a glycan at a potential N-glycosylation site, Asn-281, of bovine lactoferrin
    • Wei, Z., Nishimura, T., and Yoshida, S. (2000) Presence of a glycan at a potential N-glycosylation site, Asn-281, of bovine lactoferrin J. Dairy Sci. 83, 683-689
    • (2000) J. Dairy Sci. , vol.83 , pp. 683-689
    • Wei, Z.1    Nishimura, T.2    Yoshida, S.3


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