메뉴 건너뛰기




Volumn 118, Issue 8, 2014, Pages 2050-2057

Effects of branched O-glycosylation on a semiflexible peptide linker

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CONFORMATIONS; GLYCOSYLATION; PEPTIDES; POLYSACCHARIDES;

EID: 84897604287     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp410788r     Document Type: Article
Times cited : (13)

References (46)
  • 2
    • 0036261826 scopus 로고    scopus 로고
    • The Diversity of Acetylated Proteins
    • Polevoda, B.; Sherman, F. The Diversity of Acetylated Proteins Genome Biol. 2002, 3, 1-6
    • (2002) Genome Biol. , vol.3 , pp. 1-6
    • Polevoda, B.1    Sherman, F.2
  • 4
    • 44449128912 scopus 로고    scopus 로고
    • Structural Glycobiology: A Game of Snakes and Ladders
    • DeMarco, M. L.; Woods, R. J. Structural Glycobiology: A Game of Snakes and Ladders Glycobiology 2008, 18, 426-440
    • (2008) Glycobiology , vol.18 , pp. 426-440
    • Demarco, M.L.1    Woods, R.J.2
  • 6
    • 46149089907 scopus 로고    scopus 로고
    • Effect of Glycosylation on Protein Folding: A Close Look at Thermodynamic Stabilization
    • Shental-Bechor, D.; Levy, Y. Effect of Glycosylation on Protein Folding: A Close Look at Thermodynamic Stabilization Proc. Natl. Acad. Sci. U.S.A. 2008, 105, 8256-8261
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 8256-8261
    • Shental-Bechor, D.1    Levy, Y.2
  • 7
    • 70349886556 scopus 로고    scopus 로고
    • Folding of Glycoproteins: Toward Understanding the Biophysics of the Glycosylation Code
    • Shental-Bechor, D.; Levy, Y. Folding of Glycoproteins: Toward Understanding the Biophysics of the Glycosylation Code Curr. Opin. Struct. Biol. 2009, 19, 524-533
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 524-533
    • Shental-Bechor, D.1    Levy, Y.2
  • 8
    • 0032488983 scopus 로고    scopus 로고
    • Influence of N-Glycosylation and N-Glycan Trimming on the Activity and Intracellular Traffic of GD3 Synthase
    • Martina, J.; Daniotti, J.; Maccioni, H. Influence of N-Glycosylation and N-Glycan Trimming on the Activity and Intracellular Traffic of GD3 Synthase Biol. Chem. 1998, 273, 3725-3731
    • (1998) Biol. Chem. , vol.273 , pp. 3725-3731
    • Martina, J.1    Daniotti, J.2    Maccioni, H.3
  • 9
    • 33645966218 scopus 로고    scopus 로고
    • Trypanosoma Cruzi Surface Mucins: Host-Dependent Coat Diversity
    • Buscaglia, C.; Campo, V.; Di Noia, J. Trypanosoma Cruzi Surface Mucins: Host-Dependent Coat Diversity Nat. Rev. Microbiol. 2006, 4, 229-236
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 229-236
    • Buscaglia, C.1    Campo, V.2    Di Noia, J.3
  • 10
    • 74849131820 scopus 로고    scopus 로고
    • O-Mannosyl Phosphorylation of Alpha-Dystroglycan Is Required for Laminin Binding
    • Yoshida-Moriguchi, T.; Stalnaker, S.; Campbell, K. O-Mannosyl Phosphorylation of Alpha-Dystroglycan Is Required for Laminin Binding Science 2010, 327, 88-92
    • (2010) Science , vol.327 , pp. 88-92
    • Yoshida-Moriguchi, T.1    Stalnaker, S.2    Campbell, K.3
  • 11
    • 11944272604 scopus 로고
    • Environmental Effects on Protein Glycosylation
    • Goochee, C.; Monica, T. Environmental Effects on Protein Glycosylation Nat. Biotechnol. 1990, 8, 421-427
    • (1990) Nat. Biotechnol. , vol.8 , pp. 421-427
    • Goochee, C.1    Monica, T.2
  • 12
    • 2342580146 scopus 로고    scopus 로고
    • Aberrant Glycosylation in IgA Nephropathy (IgAN)
    • Coppo, R.; Amore, A. Aberrant Glycosylation in IgA Nephropathy (IgAN) Kidney Int. 2004, 65, 1544-1547
    • (2004) Kidney Int. , vol.65 , pp. 1544-1547
    • Coppo, R.1    Amore, A.2
  • 13
    • 13344291142 scopus 로고
    • Effects of Glycosylation on Peptide Backbone Conformation
    • Andreotti, A.; Kahne, D. Effects of Glycosylation on Peptide Backbone Conformation J. Am. Chem. Soc. 1993, 115, 3352-3359
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 3352-3359
    • Andreotti, A.1    Kahne, D.2
  • 14
    • 0345530978 scopus 로고    scopus 로고
    • Conformational Studies on the MUC1 Tandem Repeat Glycopeptides: Implication for the Enzymatic O-Glycosylation of the Mucin Protein Core
    • Kinarsky, L.; Suryanarayanan, G.; Paulsen, O. P. H.; Clausen, H.; Hanisch, F.-G.; Hollingsworth, M.; Sherman, S. Conformational Studies on the MUC1 Tandem Repeat Glycopeptides: Implication for the Enzymatic O-Glycosylation of the Mucin Protein Core Glycobiology 2003, 13, 929-939
    • (2003) Glycobiology , vol.13 , pp. 929-939
    • Kinarsky, L.1    Suryanarayanan, G.2    Paulsen, O.P.H.3    Clausen, H.4    Hanisch, F.-G.5    Hollingsworth, M.6    Sherman, S.7
  • 15
    • 0029803424 scopus 로고    scopus 로고
    • Conformational Influences of Glycosylation of a Peptide: A Possible Model for the Effect of Glycosylation on the Rate of Protein Folding
    • Live, D. H.; Kumar, R. A.; Beebe, X.; Danishefsky, S. J. Conformational Influences of Glycosylation of a Peptide: A Possible Model for the Effect of Glycosylation on the Rate of Protein Folding Proc. Natl. Acad. Sci. U.S.A. 1996, 93, 12759-12761
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 12759-12761
    • Live, D.H.1    Kumar, R.A.2    Beebe, X.3    Danishefsky, S.J.4
  • 16
    • 62549107841 scopus 로고    scopus 로고
    • The Core Trisaccharide of an N-Linked Glycoprotein Intrinsically Accelerates Folding and Enhances Stability
    • Hansona, S. R.; Culybaa, E. K.; Hsua, T.-L.; Wong, C.-H.; Kelly, J. W.; Powers, E. T. The Core Trisaccharide of an N-Linked Glycoprotein Intrinsically Accelerates Folding and Enhances Stability Proc. Natl. Acad. Sci. U.S.A. 2009, 106, 3131-3136
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 3131-3136
    • Hansona, S.R.1    Culybaa, E.K.2    Hsua, T.-L.3    Wong, C.-H.4    Kelly, J.W.5    Powers, E.T.6
  • 19
    • 0001346959 scopus 로고
    • Sensitivity of Glycopeptide Conformation to Carbohydrate Chain Length
    • Liang, R.; Andreotti, A. Sensitivity of Glycopeptide Conformation to Carbohydrate Chain Length J. Am. Chem. Soc. 1995, 117, 10395-10403
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 10395-10403
    • Liang, R.1    Andreotti, A.2
  • 20
    • 0030590534 scopus 로고    scopus 로고
    • Structural Comparison of a 15 Residue Peptide from the V3 Loop of HIV-1IIIb and an O-Glycosylated Analogue
    • Huang, X.; Berzofsky, J.; Barchi, J. Structural Comparison of a 15 Residue Peptide from the V3 Loop of HIV-1IIIb and an O-Glycosylated Analogue FEBS Lett. 1996, 16, 280-286
    • (1996) FEBS Lett. , vol.16 , pp. 280-286
    • Huang, X.1    Berzofsky, J.2    Barchi, J.3
  • 21
    • 0027951227 scopus 로고
    • Solid-Phase Chemical-Enzymic Synthesis of Glycopeptides and Oligosaccharides
    • Schuster, M.; Wang, P.; Paulson, J.; Wong, C. Solid-Phase Chemical-Enzymic Synthesis of Glycopeptides and Oligosaccharides J. Am. Chem. Soc. 1994, 116, 1135-1136
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 1135-1136
    • Schuster, M.1    Wang, P.2    Paulson, J.3    Wong, C.4
  • 22
    • 70349275888 scopus 로고    scopus 로고
    • Mass Spectrometry in the Analysis of N-Linked and O-Linked Glycans
    • North, S.; Hitchen, P.; Haslam, S.; Dell, A. Mass Spectrometry in the Analysis of N-Linked and O-Linked Glycans Curr. Opin. Struct. Biol. 2009, 19, 498-506
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 498-506
    • North, S.1    Hitchen, P.2    Haslam, S.3    Dell, A.4
  • 23
    • 3142695658 scopus 로고    scopus 로고
    • Effects of Glycosylation on Peptide Conformation: A Synergistic Experimental and Computational Study
    • Bosques, C. J.; Tschampel, S. M.; Woods, R. J.; Imperiali, B. Effects of Glycosylation on Peptide Conformation: A Synergistic Experimental and Computational Study J. Am. Chem. Soc. 2004, 126, 8421-8425
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 8421-8425
    • Bosques, C.J.1    Tschampel, S.M.2    Woods, R.J.3    Imperiali, B.4
  • 24
    • 80053112125 scopus 로고    scopus 로고
    • Influence of Solvent and Intramolecular Hydrogen Bonding on the Conformational Properties of O-Linked Glycopeptides
    • Mallajosyula, S. S.; MacKerell, A. D., Jr. Influence of Solvent and Intramolecular Hydrogen Bonding on the Conformational Properties of O-Linked Glycopeptides J. Phys. Chem. B 2011, 115, 11215-11229
    • (2011) J. Phys. Chem. B , vol.115 , pp. 11215-11229
    • Mallajosyula, S.S.1    MacKerell Jr., A.D.2
  • 25
    • 0035913754 scopus 로고    scopus 로고
    • Atomistic Brownian Dynamics Simulation of Peptide Phosphorylation
    • Shen, T.; Wong, C. F.; McCammon, J. A. Atomistic Brownian Dynamics Simulation of Peptide Phosphorylation J. Am. Chem. Soc. 2001, 123, 9107-9111
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 9107-9111
    • Shen, T.1    Wong, C.F.2    McCammon, J.A.3
  • 26
    • 0033548612 scopus 로고    scopus 로고
    • The Fab and Fc Fragments of IgA1 Exhibit a Different Arrangement from that in IgG: A Study by X-Ray and Neutron Solution Scattering and Homology Modelling
    • Boehm, M.; Woof, J.; Kerr, M.; Perkins, S. The Fab and Fc Fragments of IgA1 Exhibit a Different Arrangement from that in IgG: a Study by X-Ray and Neutron Solution Scattering and Homology Modelling J. Mol. Biol. 1999, 286, 1421-1447
    • (1999) J. Mol. Biol. , vol.286 , pp. 1421-1447
    • Boehm, M.1    Woof, J.2    Kerr, M.3    Perkins, S.4
  • 28
    • 0030836018 scopus 로고    scopus 로고
    • Galactose-Deficient IgA1 in Sera of IgA Nephropathy Patients is Present in Complexes with IgG
    • Tomana, M.; Matousovic, K.; Mestecky, J. Galactose-Deficient IgA1 in Sera of IgA Nephropathy Patients is Present in Complexes with IgG Kidney Int. 1997, 52, 509-516
    • (1997) Kidney Int. , vol.52 , pp. 509-516
    • Tomana, M.1    Matousovic, K.2    Mestecky, J.3
  • 29
    • 0031787449 scopus 로고    scopus 로고
    • Protective Role of IgA 1 Glycans Against IgA 1 Self-Aggregation and Adhesion to Extracellular Matrix Proteins
    • Kokubo, T.; Hiki, Y.; Iwase, H.; Tanaka, A.; Toma, K.; Hotta, K.; Kobayashi, Y. Protective Role of IgA 1 Glycans Against IgA 1 Self-Aggregation and Adhesion to Extracellular Matrix Proteins J. Am. Soc. Nephrol. 1998, 9, 2048-2054
    • (1998) J. Am. Soc. Nephrol. , vol.9 , pp. 2048-2054
    • Kokubo, T.1    Hiki, Y.2    Iwase, H.3    Tanaka, A.4    Toma, K.5    Hotta, K.6    Kobayashi, Y.7
  • 30
    • 33144464467 scopus 로고    scopus 로고
    • Control of Protein Functional Dynamics by Peptide Linkers
    • Wriggers, W.; Chakravarty, S.; Jennings, P. Control of Protein Functional Dynamics by Peptide Linkers Biopolymers 2005, 80, 736-746
    • (2005) Biopolymers , vol.80 , pp. 736-746
    • Wriggers, W.1    Chakravarty, S.2    Jennings, P.3
  • 31
    • 0018775747 scopus 로고
    • Primary Structure of a Human IgA1 Immunoglobulin. IV. Streptococcal IgA1 Protease, Digestion, Fab and Fc Fragments, and the Complete Amino Acid Sequence of the Alpha 1 Heavy Chain
    • Putnam, F. W.; Liu, Y. S.; Low, T. L. Primary Structure of a Human IgA1 Immunoglobulin. IV. Streptococcal IgA1 Protease, Digestion, Fab and Fc Fragments, and the Complete Amino Acid Sequence of the Alpha 1 Heavy Chain J. Biol. Chem. 1979, 25, 2865-2874
    • (1979) J. Biol. Chem. , vol.25 , pp. 2865-2874
    • Putnam, F.W.1    Liu, Y.S.2    Low, T.L.3
  • 32
    • 0016765526 scopus 로고
    • The Primary Structure of a Monoclonal IgA-Immunoglobulin (IgA Tro.), II. The Amino Acid Sequence of the H-Chain, Alpha-Type, Subgroup III; Structure of the Complete IgA-Molecule (Author's Transl)
    • Kratzin, H.; Altevogt, P.; Ruban, E.; Kortt, A.; Staroscik, K.; Hilchmann, N. The Primary Structure of a Monoclonal IgA-Immunoglobulin (IgA Tro.), II. The Amino Acid Sequence of the H-Chain, Alpha-Type, Subgroup III; Structure of the Complete IgA-Molecule (Author's Transl) J. Biol. Chem. 1975, 356, 1337-1342
    • (1975) J. Biol. Chem. , vol.356 , pp. 1337-1342
    • Kratzin, H.1    Altevogt, P.2    Ruban, E.3    Kortt, A.4    Staroscik, K.5    Hilchmann, N.6
  • 34
    • 4444307298 scopus 로고    scopus 로고
    • Human Serum IgA1 is Substituted with up to Six O-Glycans as Shown by Matrix Assisted Laser Desorption Ionisation Time-of-Flight Mass Spectrometry
    • Tarelli, E.; Smith, A. C.; Hendry, B. M.; Challacombe, S. J.; Pouria, S. Human Serum IgA1 is Substituted with up to Six O-Glycans as Shown by Matrix Assisted Laser Desorption Ionisation Time-of-Flight Mass Spectrometry Carbohydr. Res. 2004, 339, 2329-2335
    • (2004) Carbohydr. Res. , vol.339 , pp. 2329-2335
    • Tarelli, E.1    Smith, A.C.2    Hendry, B.M.3    Challacombe, S.J.4    Pouria, S.5
  • 35
    • 34547683219 scopus 로고    scopus 로고
    • Serine Versus Threonine Glycosylation: The Methyl Group Causes a Drastic Alteration on the Carbohydrate Orientation and on the Surrounding Water Shell
    • Corzana, F.; Busto, J. H.; Jimenez-Oses, G.; de Luis, M. G.; Asensio, J. L.; Barbero, J. J.; Peregrina, J. M.; Avenoza, A. Serine Versus Threonine Glycosylation: The Methyl Group Causes a Drastic Alteration on the Carbohydrate Orientation and on the Surrounding Water Shell J. Am. Chem. Soc. 2007, 129, 9458-9467
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 9458-9467
    • Corzana, F.1    Busto, J.H.2    Jimenez-Oses, G.3    De Luis, M.G.4    Asensio, J.L.5    Barbero, J.J.6    Peregrina, J.M.7    Avenoza, A.8
  • 37
    • 84897654606 scopus 로고    scopus 로고
    • The University of Georgia Carbohydrate Research Center. (accessed Oct, 17)
    • The University of Georgia Carbohydrate Research Center. http://glycam.ccrc.uga.edu/ccrc/ (accessed Oct, 17 2012).
    • (2012)
  • 39
    • 0035845496 scopus 로고    scopus 로고
    • Solvent Interactions Determine Carbohydrate Conformation
    • Kirschner, K.; Woods, R. Solvent Interactions Determine Carbohydrate Conformation Proc. Natl. Acad. Sci. U.S.A. 2001, 98, 10541-10545
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 10541-10545
    • Kirschner, K.1    Woods, R.2
  • 41
    • 33846823909 scopus 로고
    • Particle Mesh Ewald: An N.log(N) Method for Ewald sums in Large Systems
    • Darden, T.; York, D.; Pedersen, L. Particle Mesh Ewald: An N.log(N) Method for Ewald sums in Large Systems J. Chem. Phys. 1993, 98, 10089-10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 42
    • 33646940952 scopus 로고
    • Numerical Integration of the Cartesian Equations of Motion of a System with Constraints: Molecular Dynamics of n-Alkanes
    • Ryckaert, J. P.; Ciccotti, G.; Berendsen, H. J. C. Numerical Integration of the Cartesian Equations of Motion of a System with Constraints: Molecular Dynamics of n-Alkanes J. Comput. Phys. 1977, 23, 327-341
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 44
    • 70350044640 scopus 로고    scopus 로고
    • Conformational Flexibility of Soluble Cellulose Oligomers: Chain Length and Temperature Dependence
    • Shen, T.; Langan, P.; French, A.; Johnson, G. P.; Gnanakaran, S. Conformational Flexibility of Soluble Cellulose Oligomers: Chain Length and Temperature Dependence J. Am. Chem. Soc. 2009, 131, 14786-14794
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 14786-14794
    • Shen, T.1    Langan, P.2    French, A.3    Johnson, G.P.4    Gnanakaran, S.5
  • 45
    • 0025299887 scopus 로고
    • Occurrence and Role of Cis Peptide-Bonds in Protein Structures
    • Stewart, D. E.; Sarkar, A.; Wampler, J. E. Occurrence and Role of Cis Peptide-Bonds in Protein Structures J. Mol. Biol. 1990, 214, 253-260
    • (1990) J. Mol. Biol. , vol.214 , pp. 253-260
    • Stewart, D.E.1    Sarkar, A.2    Wampler, J.E.3
  • 46
    • 13644250683 scopus 로고    scopus 로고
    • Phosphorylation Effects on Cis/trans Isomerization and the Backbone Conformation of Serine-Proline Motifs: Accelerated Molecular Dynamics analysis
    • Hamelberg, D.; Shen, T.; McCammon, J. A. Phosphorylation Effects on Cis/trans Isomerization and the Backbone Conformation of Serine-Proline Motifs: Accelerated Molecular Dynamics analysis J. Am. Chem. Soc. 2005, 127, 1969-1974
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 1969-1974
    • Hamelberg, D.1    Shen, T.2    McCammon, J.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.