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Volumn 275, Issue 9, 2008, Pages 1949-1959

Chemical approaches to mapping the function of post-translational modifications

Author keywords

Chemoselective ligation; Post translational modification; Protein glycosylation; Protein modification; Synthetic proteins

Indexed keywords

BINDING PROTEIN; GLYCOPROTEIN; P SELECTIN GLYCOPROTEIN LIGAND 1; PADGEM PROTEIN; PROTEOME;

EID: 42449141921     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2008.06347.x     Document Type: Review
Times cited : (39)

References (77)
  • 2
    • 28044433451 scopus 로고    scopus 로고
    • Protein posttranslational modifications: The chemistry of proteome diversifications
    • Walsh CT, Garneau-Tsodikova S Gatto GJ Jr. (2005) Protein posttranslational modifications: the chemistry of proteome diversifications. Angew Chemie Int Edn 44, 7342 7372.
    • (2005) Angew Chemie Int Edn , vol.44 , pp. 7342-7372
    • Walsh, C.T.1    Garneau-Tsodikova, S.2    Gatto Jr., G.J.3
  • 3
    • 0019376492 scopus 로고
    • In vivo chemical modification of proteins (post-translational modification)
    • Wold F (1981) In vivo chemical modification of proteins (post-translational modification). Annu Rev Biochem 50, 783 814.
    • (1981) Annu Rev Biochem , vol.50 , pp. 783-814
    • Wold, F.1
  • 4
    • 1642434197 scopus 로고    scopus 로고
    • Mimicking posttranslational modifications of proteins
    • Davis BG (2004) Mimicking posttranslational modifications of proteins. Science 303, 480 482.
    • (2004) Science , vol.303 , pp. 480-482
    • Davis, B.G.1
  • 5
    • 76549240988 scopus 로고
    • The desoxyribonucleic acid content of animal cells and its evolutionary significance
    • Mirsky AE Ris H (1951) The desoxyribonucleic acid content of animal cells and its evolutionary significance. J Gen Physiol 34, 451 462.
    • (1951) J Gen Physiol , vol.34 , pp. 451-462
    • Mirsky, A.E.1    Ris, H.2
  • 6
    • 0000822856 scopus 로고
    • Genetic organization of chromosomes
    • Thomas CA (1971) Genetic organization of chromosomes. Annu Rev Genet 5, 237.
    • (1971) Annu Rev Genet , vol.5237
    • Thomas, C.A.1
  • 8
    • 0036462604 scopus 로고    scopus 로고
    • Synthesis of glycoproteins
    • Davis BG (2002) Synthesis of glycoproteins. Chem Rev 102, 579 601.
    • (2002) Chem Rev , vol.102 , pp. 579-601
    • Davis, B.G.1
  • 11
    • 0001094662 scopus 로고    scopus 로고
    • Glycobiology: Toward understanding the function of sugars
    • Dwek RA (1996) Glycobiology: toward understanding the function of sugars. Chem Rev 96, 683 720.
    • (1996) Chem Rev , vol.96 , pp. 683-720
    • Dwek, R.A.1
  • 12
    • 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
  • 13
    • 0033782777 scopus 로고    scopus 로고
    • Protein glucosylation and its role in protein folding
    • Parodi AJ (2000) Protein glucosylation and its role in protein folding. Annu Rev Biochem 69, 69 93.
    • (2000) Annu Rev Biochem , vol.69 , pp. 69-93
    • Parodi, A.J.1
  • 15
    • 33947724303 scopus 로고    scopus 로고
    • Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation
    • Lau KS, Partridge EA, Grigorian A, Silvescu CI, Reinhold VN, Demetriou M Dennis JW (2007) Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation. Cell 129, 123 134.
    • (2007) Cell , vol.129 , pp. 123-134
    • Lau, K.S.1    Partridge, E.A.2    Grigorian, A.3    Silvescu, C.I.4    Reinhold, V.N.5    Demetriou, M.6    Dennis, J.W.7
  • 16
    • 33748155285 scopus 로고    scopus 로고
    • Bacterial glycans: Key mediators of diverse host immune responses
    • Comstock LE Kasper DL (2006) Bacterial glycans: key mediators of diverse host immune responses. Cell 126, 847 850.
    • (2006) Cell , vol.126 , pp. 847-850
    • Comstock, L.E.1    Kasper, D.L.2
  • 17
    • 0029001510 scopus 로고
    • Selectin-carbohydrate interactions and the initiation of the inflammatory response
    • Lasky LA (1995) Selectin-carbohydrate interactions and the initiation of the inflammatory response. Annu Rev Biochem 64, 113 139.
    • (1995) Annu Rev Biochem , vol.64 , pp. 113-139
    • Lasky, L.A.1
  • 19
    • 4444231014 scopus 로고    scopus 로고
    • Engineering of an artificial glycosylation pathway blocked in core oligosaccharide assembly in the yeast Pichia pastoris: Production of complex humanized glycoproteins with terminal galactose
    • Bobrowicz P, Davidson RC, Li H, Potgieter TI, Nett JH, Hamilton SR, Stadheim TA, Miele RG, Bobrowicz B, Mitchell T et al. (2004) Engineering of an artificial glycosylation pathway blocked in core oligosaccharide assembly in the yeast Pichia pastoris: production of complex humanized glycoproteins with terminal galactose. Glycobiology 14, 757 766.
    • (2004) Glycobiology , vol.14 , pp. 757-766
    • Bobrowicz, P.1    Davidson, R.C.2    Li, H.3    Potgieter, T.I.4    Nett, J.H.5    Hamilton, S.R.6    Stadheim, T.A.7    Miele, R.G.8    Bobrowicz, B.9    Mitchell, T.10
  • 24
    • 33749019097 scopus 로고    scopus 로고
    • A chemical toolkit for proteins - An expanded genetic code
    • Xie J Schultz PG (2006) A chemical toolkit for proteins - an expanded genetic code. Nat Rev Mol Cell Biol 7, 775 782.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 775-782
    • Xie, J.1    Schultz, P.G.2
  • 26
    • 10044288227 scopus 로고    scopus 로고
    • Site-specific incorporation of the mucin-type N-acetylgalactosamine-a-O- threonine into protein in Escherichia coli
    • Xu R, Hanson SR, Zhang Z, Yang Y-Y, Schultz PG Wong C-H (2004) Site-specific incorporation of the mucin-type N-acetylgalactosamine-a-O- threonine into protein in Escherichia coli. J Am Chem Soc 126, 15654 15655.
    • (2004) J Am Chem Soc , vol.126 , pp. 15654-15655
    • Xu, R.1    Hanson, S.R.2    Zhang, Z.3    Yang, Y.-Y.4    Schultz, P.G.5    Wong, C.-H.6
  • 27
    • 33746608497 scopus 로고    scopus 로고
    • A Highly efficient chemoenzymatic approach toward glycoprotein synthesis
    • Li B, Song H, Hauser S Wang L-X (2006) A Highly efficient chemoenzymatic approach toward glycoprotein synthesis. Organic Lett 8, 3081 3084.
    • (2006) Organic Lett , vol.8 , pp. 3081-3084
    • Li, B.1    Song, H.2    Hauser, S.3    Wang, L.-X.4
  • 28
    • 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 (2005) Highly efficient endoglycosidase-catalyzed synthesis of glycopeptides using oligosaccharide oxazolines as donor substrates. J Am Chem Soc 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
  • 29
    • 33646040968 scopus 로고    scopus 로고
    • Glycopeptide synthesis through endo-glycosidase-catalyzed oligosaccharide transfer of sugar oxazolines: Probing substrate structural requirement
    • Zeng Y, Wang J, Li B, Hauser S, Li H Wang L-X (2006) Glycopeptide synthesis through endo-glycosidase-catalyzed oligosaccharide transfer of sugar oxazolines: probing substrate structural requirement. Chem Eur J 12, 3355 3364.
    • (2006) Chem Eur J , vol.12 , pp. 3355-3364
    • Zeng, Y.1    Wang, J.2    Li, B.3    Hauser, S.4    Li, H.5    Wang, L.-X.6
  • 31
    • 0035977638 scopus 로고    scopus 로고
    • Synthesis of peptides and proteins without cysteine residues by native chemical ligation combined with desulfurization
    • Yan LZ Dawson PE (2001) Synthesis of peptides and proteins without cysteine residues by native chemical ligation combined with desulfurization. J Am Chem Soc 123, 526 533.
    • (2001) J Am Chem Soc , vol.123 , pp. 526-533
    • Yan, L.Z.1    Dawson, P.E.2
  • 33
    • 3543108674 scopus 로고    scopus 로고
    • Modular assembly of glycoproteins: Towards the synthesis of GlyCAM-1 by using expressed protein ligation
    • Macmillan D Bertozzi CR (2004) Modular assembly of glycoproteins: towards the synthesis of GlyCAM-1 by using expressed protein ligation. Angew Chem Int Edn 43, 1355 1359.
    • (2004) Angew Chem Int Edn , vol.43 , pp. 1355-1359
    • MacMillan, D.1    Bertozzi, C.R.2
  • 34
    • 33644888786 scopus 로고    scopus 로고
    • Convergent glycopeptide synthesis by traceless Staudinger ligation and enzymatic coupling
    • Liu L, Hong Z-Y Wong C-H (2006) Convergent glycopeptide synthesis by traceless Staudinger ligation and enzymatic coupling. ChemBioChem 7, 429 432.
    • (2006) ChemBioChem , vol.7 , pp. 429-432
    • Liu, L.1    Hong, Z.-Y.2    Wong, C.-H.3
  • 35
    • 0030936614 scopus 로고    scopus 로고
    • Enzymic glycoprotein synthesis: Preparation of ribonuclease glycoforms via enzymic glycopeptide condensation and glycosylation
    • Witte K, Sears P Wong C-H (1997) Enzymic glycoprotein synthesis: preparation of ribonuclease glycoforms via enzymic glycopeptide condensation and glycosylation. J Am Chem Soc 119, 2114 2118.
    • (1997) J Am Chem Soc , vol.119 , pp. 2114-2118
    • Witte, K.1    Sears, P.2    Wong, C.-H.3
  • 36
    • 12744268422 scopus 로고    scopus 로고
    • 'Polar patch' proteases as glycopeptiligases
    • Doores KJ Davis BG (2005) 'Polar patch' proteases as glycopeptiligases. Chem Commun, 168 170.
    • (2005) Chem Commun , pp. 168-170
    • Doores, K.J.1    Davis, B.G.2
  • 37
    • 0025998876 scopus 로고
    • A novel method for the specific glycosylation of proteins
    • Davis NJ Flitsch SL (1991) A novel method for the specific glycosylation of proteins. Tetrahedron Lett 32, 6793 6796.
    • (1991) Tetrahedron Lett , vol.32 , pp. 6793-6796
    • Davis, N.J.1    Flitsch, S.L.2
  • 38
    • 25844454688 scopus 로고    scopus 로고
    • Structural approaches to the study of oligosaccharides in glycoprotein quality control
    • Ito Y, Hagihara S, Matsuo I Totani K (2005) Structural approaches to the study of oligosaccharides in glycoprotein quality control. Current Opin Struct Biol 15, 481 489.
    • (2005) Current Opin Struct Biol , vol.15 , pp. 481-489
    • Ito, Y.1    Hagihara, S.2    Matsuo, I.3    Totani, K.4
  • 39
    • 0028336647 scopus 로고
    • Synthetic glycosylation of proteins using N-(beta-saccharide) iodoacetamides: Applications in site-specific glycosylation and solid-phase enzymic oligosaccharide synthesis
    • Wong SY, Guile GR, Dwek RA Arsequell G (1994) Synthetic glycosylation of proteins using N-(beta-saccharide) iodoacetamides: applications in site-specific glycosylation and solid-phase enzymic oligosaccharide synthesis. Biochem J 300 (Pt 3 843 850.
    • (1994) Biochem J , vol.300 , Issue.3 , pp. 843-850
    • Wong, S.Y.1    Guile, G.R.2    Dwek, R.A.3    Arsequell, G.4
  • 40
    • 0005985212 scopus 로고    scopus 로고
    • A unique and highly facile method for synthesizing disulfide linked neoglycoconjugates: A new approach for remodeling of peptides and proteins
    • Macindoe WM, van Oijen AH Boons G-J (1998) A unique and highly facile method for synthesizing disulfide linked neoglycoconjugates: a new approach for remodeling of peptides and proteins. Chem Commun, 847 848.
    • (1998) Chem Commun , pp. 847-848
    • MacIndoe, W.M.1    Van Oijen, A.H.2    Boons, G.-J.3
  • 41
    • 0032567423 scopus 로고    scopus 로고
    • Controlled site-selective glycosylation of proteins by a combined site-directed mutagenesis and chemical modification approach
    • Davis BG, Lloyd RC Jones JB (1998) Controlled site-selective glycosylation of proteins by a combined site-directed mutagenesis and chemical modification approach. J Organic Chem 63, 9614 9615.
    • (1998) J Organic Chem , vol.63 , pp. 9614-9615
    • Davis, B.G.1    Lloyd, R.C.2    Jones, J.B.3
  • 42
    • 0141565183 scopus 로고    scopus 로고
    • Site-specific glycosylation of an aglycosylated human IgG1-Fc antibody protein generates neoglycoproteins with enhanced function
    • Watt GM, Lund J, Levens M, Kolli VSK, Jefferis R Boons G-J (2003) Site-specific glycosylation of an aglycosylated human IgG1-Fc antibody protein generates neoglycoproteins with enhanced function. Chem Biol 10, 807 814.
    • (2003) Chem Biol , vol.10 , 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
  • 45
    • 0033491434 scopus 로고    scopus 로고
    • Altering the specificity of subtilisin Bacillus lentus through the introduction of positive charge at single amino acid sites
    • Davis BG, Khumtaveeporn K, Bott RR Jones JB (1999) Altering the specificity of subtilisin Bacillus lentus through the introduction of positive charge at single amino acid sites. Bioorganic Med Chem 7, 2303 2311.
    • (1999) Bioorganic Med Chem , vol.7 , pp. 2303-2311
    • Davis, B.G.1    Khumtaveeporn, K.2    Bott, R.R.3    Jones, J.B.4
  • 46
    • 0033491620 scopus 로고    scopus 로고
    • The controlled introduction of multiple negative charge at single amino acid sites in subtilisin Bacillus lentus
    • Davis BG, Shang X, DeSantis G, Bott RR Jones JB (1999) The controlled introduction of multiple negative charge at single amino acid sites in subtilisin Bacillus lentus. Bioorganic Med Chem 7, 2293 2301.
    • (1999) Bioorganic Med Chem , vol.7 , pp. 2293-2301
    • Davis, B.G.1    Shang, X.2    Desantis, G.3    Bott, R.R.4    Jones, J.B.5
  • 47
    • 0037120187 scopus 로고    scopus 로고
    • Chemically modified 'polar patch' mutants of subtilisin in peptide synthesis with remarkably broad substrate acceptance: Designing combinatorial biocatalysts
    • Matsumoto K, Davis BG Jones JB (2002) Chemically modified 'polar patch' mutants of subtilisin in peptide synthesis with remarkably broad substrate acceptance: designing combinatorial biocatalysts. Chem Eur J 8, 4129 4137.
    • (2002) Chem Eur J , vol.8 , pp. 4129-4137
    • Matsumoto, K.1    Davis, B.G.2    Jones, J.B.3
  • 50
    • 0035925211 scopus 로고    scopus 로고
    • The controlled glycosylation of a protein with a bivalent glycan: Towards a new class of glycoconjugates, glycodendriproteins
    • Davis BG (2001) The controlled glycosylation of a protein with a bivalent glycan: towards a new class of glycoconjugates, glycodendriproteins. Chem Commun, 351 352.
    • (2001) Chem Commun , pp. 351-352
    • Davis, B.G.1
  • 51
    • 1842863050 scopus 로고    scopus 로고
    • Glycodendriproteins: A synthetic glycoprotein mimic enzyme with branched sugar-display potently inhibits bacterial aggregation
    • Rendle PM, Seger A, Rodrigues J, Oldham NJ, Bott RR, Jones JB, Cowan MM Davis BG (2004) Glycodendriproteins: a synthetic glycoprotein mimic enzyme with branched sugar-display potently inhibits bacterial aggregation. J Am Chem Soc 126, 4750 4751.
    • (2004) J Am Chem Soc , vol.126 , pp. 4750-4751
    • Rendle, P.M.1    Seger, A.2    Rodrigues, J.3    Oldham, N.J.4    Bott, R.R.5    Jones, J.B.6    Cowan, M.M.7    Davis, B.G.8
  • 52
    • 0035057706 scopus 로고    scopus 로고
    • Selective in vitro glycosylation of recombinant proteins: Semi-synthesis of novel homogeneous glycoforms of human erythropoietin
    • Macmillan D, Bill RM, Sage KA, Fern D Flitsch SL (2001) Selective in vitro glycosylation of recombinant proteins: semi-synthesis of novel homogeneous glycoforms of human erythropoietin. Chem Biol 8, 133 145.
    • (2001) Chem Biol , vol.8 , pp. 133-145
    • MacMillan, D.1    Bill, R.M.2    Sage, K.A.3    Fern, D.4    Flitsch, S.L.5
  • 53
    • 33746300332 scopus 로고    scopus 로고
    • Glycosylation of a neoglycoprotein by using glycosynthase and thioglycoligase approaches: The generation of a thioglycoprotein
    • Mullegger J, Chen HM, Warren RAJ Withers SG (2006) Glycosylation of a neoglycoprotein by using glycosynthase and thioglycoligase approaches: the generation of a thioglycoprotein. Angew Chem Int Edn 45, 2585 2588.
    • (2006) Angew Chem Int Edn , vol.45 , pp. 2585-2588
    • Mullegger, J.1    Chen, H.M.2    Warren, R.A.J.3    Withers, S.G.4
  • 54
    • 0347415742 scopus 로고    scopus 로고
    • A convergent strategy for the preparation of N-glycan core di-, tri-, and pentasaccharide thioaldoses for the site-specific glycosylation of peptides and proteins bearing free cysteines
    • Watt GM Boons G-J (2004) A convergent strategy for the preparation of N-glycan core di-, tri-, and pentasaccharide thioaldoses for the site-specific glycosylation of peptides and proteins bearing free cysteines. Carbohydr Res 339, 181 193.
    • (2004) Carbohydr Res , vol.339 , pp. 181-193
    • Watt, G.M.1    Boons, G.-J.2
  • 55
    • 4544387352 scopus 로고    scopus 로고
    • Glyco-SeS: Selenenylsulfide-mediated protein glycoconjugation - A new strategy in post-translational modification
    • Gamblin DP, Garnier P, van Kasteren S, Oldham NJ, Fairbanks AJ Davis BG (2004) Glyco-SeS: selenenylsulfide-mediated protein glycoconjugation - a new strategy in post-translational modification. Angew Chem Int Edn 43, 828 833.
    • (2004) Angew Chem Int Edn , vol.43 , pp. 828-833
    • Gamblin, D.P.1    Garnier, P.2    Van Kasteren, S.3    Oldham, N.J.4    Fairbanks, A.J.5    Davis, B.G.6
  • 57
    • 33746294817 scopus 로고    scopus 로고
    • The direct formation of glycosyl thiols from reducing sugars allows one-pot protein glycoconjugation
    • Bernardes GJL, Gamblin DP Davis BG (2006) The direct formation of glycosyl thiols from reducing sugars allows one-pot protein glycoconjugation. Angew Chem Int Edn 45, 4007 4011.
    • (2006) Angew Chem Int Edn , vol.45 , pp. 4007-4011
    • Bernardes, G.J.L.1    Gamblin, D.P.2    Davis, B.G.3
  • 58
    • 0027026591 scopus 로고
    • Protein prenylation: More than just glue?
    • Cox AD Der CJ (1992) Protein prenylation: more than just glue? Curr Opin Cell Biol 4, 1008 1016.
    • (1992) Curr Opin Cell Biol , vol.4 , pp. 1008-1016
    • Cox, A.D.1    Der, C.J.2
  • 59
    • 0642306909 scopus 로고    scopus 로고
    • Are prenyl groups on proteins sticky fingers or greasy handles?
    • Magee AI Seabra MC (2003) Are prenyl groups on proteins sticky fingers or greasy handles? Biochem J 376, e3 e4.
    • (2003) Biochem J , vol.376
    • Magee, A.I.1    Seabra, M.C.2
  • 60
    • 0242331665 scopus 로고    scopus 로고
    • AIPL1, a protein implicated in Leber's congenital amaurosis, interacts with and aids in processing of farnesylated proteins
    • Ramamurthy V, Roberts M, van den Akker F, Niemi G, Reh TA Hurley JB (2003) AIPL1, a protein implicated in Leber's congenital amaurosis, interacts with and aids in processing of farnesylated proteins. Proc Natl Acad Sci USA 100, 12630 12635.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 12630-12635
    • Ramamurthy, V.1    Roberts, M.2    Van Den Akker, F.3    Niemi, G.4    Reh, T.A.5    Hurley, J.B.6
  • 61
    • 0034672686 scopus 로고    scopus 로고
    • Functional aspects of polyisoprenoid protein substituents: Roles in protein-protein interaction and trafficking
    • Sinensky M (2000) Functional aspects of polyisoprenoid protein substituents: roles in protein-protein interaction and trafficking. Biochim Biophys Acta 1529, 203 209.
    • (2000) Biochim Biophys Acta , vol.1529 , pp. 203-209
    • Sinensky, M.1
  • 63
    • 4344619948 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitors disrupt EGF receptor traffic through modulation of the RhoB GTPase
    • Wherlock M, Gampel A, Futter C Mellor H (2004) Farnesyltransferase inhibitors disrupt EGF receptor traffic through modulation of the RhoB GTPase. J Cell Sci 117, 3221 3231.
    • (2004) J Cell Sci , vol.117 , pp. 3221-3231
    • Wherlock, M.1    Gampel, A.2    Futter, C.3    Mellor, H.4
  • 64
    • 0029091683 scopus 로고
    • In vivo requirement of protein prenylation for maintenance of retinal cytoarchitecture and photoreceptor structure
    • Pittler SJ, Fliesler SJ, Fisher PL, Keller PK Rapp LM (1995) In vivo requirement of protein prenylation for maintenance of retinal cytoarchitecture and photoreceptor structure. J Cell Biol 130, 431 439.
    • (1995) J Cell Biol , vol.130 , pp. 431-439
    • Pittler, S.J.1    Fliesler, S.J.2    Fisher, P.L.3    Keller, P.K.4    Rapp, L.M.5
  • 65
    • 30744478198 scopus 로고    scopus 로고
    • Role of protein phosphorylation on serine/threonine and tyrosine in the virulence of bacterial pathogens
    • Cozzone AJ (2005) Role of protein phosphorylation on serine/threonine and tyrosine in the virulence of bacterial pathogens. J Mol Microbiol Biotechnol 9, 198 213.
    • (2005) J Mol Microbiol Biotechnol , vol.9 , pp. 198-213
    • Cozzone, A.J.1
  • 67
    • 20544472348 scopus 로고    scopus 로고
    • Regulation of protein function by glutathionylation
    • Ghezzi P (2005) Regulation of protein function by glutathionylation. Free Rad Res 39, 573 580.
    • (2005) Free Rad Res , vol.39 , pp. 573-580
    • Ghezzi, P.1
  • 68
    • 19044381583 scopus 로고    scopus 로고
    • Post-translational disulfide modifications in cell signaling-role of inter-protein, intra-protein, S-glutathionyl, and S-cysteaminyl disulfide modifications in signal transmission
    • O'Brian CA Chu F (2005) Post-translational disulfide modifications in cell signaling-role of inter-protein, intra-protein, S-glutathionyl, and S-cysteaminyl disulfide modifications in signal transmission. Free Rad Res 39, 471 480.
    • (2005) Free Rad Res , vol.39 , pp. 471-480
    • O'Brian, C.A.1    Chu, F.2
  • 69
    • 0037099395 scopus 로고    scopus 로고
    • A stepwise Huisgen cycloaddition process: Copper(I)-catalyzed regioselective 'ligation' of azides and terminal alkynes
    • Rostovtsev VV, Green LG, Fokin VV Sharpless KB (2002) A stepwise Huisgen cycloaddition process: copper(I)-catalyzed regioselective 'ligation' of azides and terminal alkynes. Angew Chem Int Edn 41, 2596 2599.
    • (2002) Angew Chem Int Edn , vol.41 , pp. 2596-2599
    • Rostovtsev, V.V.1    Green, L.G.2    Fokin, V.V.3    Sharpless, K.B.4
  • 70
    • 0037012920 scopus 로고    scopus 로고
    • Peptidotriazoles on solid phase: [1,2,3]-triazoles by regiospecific copper(I)-catalyzed 1,3-dipolar cycloadditions of terminal alkynes to azides
    • Tornøe CW, Christensen C Meldal M (2002) Peptidotriazoles on solid phase: [1,2,3]-triazoles by regiospecific copper(I)-catalyzed 1,3-dipolar cycloadditions of terminal alkynes to azides. J Org Chem 67, 3057 3064.
    • (2002) J Org Chem , vol.67 , pp. 3057-3064
    • Tornøe, C.W.1    Christensen, C.2    Meldal, M.3
  • 71
    • 0037039298 scopus 로고    scopus 로고
    • Incorporation of azides into recombinant proteins for chemoselective modification by the Staudinger ligation
    • Kiick KL, Saxon E, Tirrell DA Bertozzi CR (2002) Incorporation of azides into recombinant proteins for chemoselective modification by the Staudinger ligation. Proc Natl Acad Sci USA 99, 19 24.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 19-24
    • Kiick, K.L.1    Saxon, E.2    Tirrell, D.A.3    Bertozzi, C.R.4
  • 72
    • 0034003659 scopus 로고    scopus 로고
    • Efficient incorporation of unsaturated methionine analogues into proteins in vivo
    • Van Hest JCM, Kiick KL Tirrell DA (2000) Efficient incorporation of unsaturated methionine analogues into proteins in vivo. J Am Chem Soc 122, 1282 1288.
    • (2000) J Am Chem Soc , vol.122 , pp. 1282-1288
    • Van Hest, J.C.M.1    Kiick, K.L.2    Tirrell, D.A.3
  • 73
    • 0029858031 scopus 로고    scopus 로고
    • Selectins and their ligands: Current concepts and controversies
    • Kansas GS (1996) Selectins and their ligands: current concepts and controversies. Blood 88, 3259 3287.
    • (1996) Blood , vol.88 , pp. 3259-3287
    • Kansas, G.S.1
  • 74
    • 0034721650 scopus 로고    scopus 로고
    • Insights into the molecular basis of leukocyte tethering and rolling revealed by structures of P- and E-selectin bound to SLe(X) and PSGL-1
    • Somers WS, Tang J, Shaw GD Camphausen RT (2000) Insights into the molecular basis of leukocyte tethering and rolling revealed by structures of P- and E-selectin bound to SLe(X) and PSGL-1. Cell 103, 467 479.
    • (2000) Cell , vol.103 , pp. 467-479
    • Somers, W.S.1    Tang, J.2    Shaw, G.D.3    Camphausen, R.T.4
  • 75
    • 0036898933 scopus 로고    scopus 로고
    • Diverse regulation of protein function by O-GlcNAc: A nuclear and cytoplasmic carbohydrate post-translational modification
    • Vosseller K, Sakabe K, Wells L Hart Gerald W (2002) Diverse regulation of protein function by O-GlcNAc: a nuclear and cytoplasmic carbohydrate post-translational modification. Curr Opin Chem Biol 6, 851 857.
    • (2002) Curr Opin Chem Biol , vol.6 , pp. 851-857
    • Vosseller, K.1    Sakabe, K.2    Wells, L.3    Hart Gerald, W.4
  • 77
    • 0027299484 scopus 로고
    • An 83 kDa O-GlcNAc-glycoprotein is found in the axoplasm and nucleus of Aplysia neurons
    • Elliot SP, Schmied R, Gabel CA Ambron RT (1993) An 83 kDa O-GlcNAc-glycoprotein is found in the axoplasm and nucleus of Aplysia neurons. J Neurosci 13, 2424 2429.
    • (1993) J Neurosci , vol.13 , pp. 2424-2429
    • Elliot, S.P.1    Schmied, R.2    Gabel, C.A.3    Ambron, R.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.