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Volumn 275, Issue 6, 2008, Pages 1163-1173

C-mannosylation in the hypertrehalosaemic hormone from the stick insect Carausius morosus

Author keywords

mannosyltryptophan; Carausius morosus; Hypertrehalosaemic hormone; NMR; Protein C mannosylation

Indexed keywords

GLYCOGEN; HEXOSE; INSECT HORMONE; NEUROPEPTIDE; PROTEIN C; PYRAN DERIVATIVE; TREHALOSE; TRYPTOPHAN;

EID: 40349100562     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2008.06277.x     Document Type: Article
Times cited : (44)

References (39)
  • 1
    • 0030628549 scopus 로고    scopus 로고
    • The explosion of structural information on insect neuropeptides
    • In. Vol 71 (. Herz, W., Kirby, G.W., Moore, R.E., Steglich, W. Tamm, Ch, eds. pp. Springer Verlag Wien, New York, NY.
    • Gäde G (1997) The explosion of structural information on insect neuropeptides. In Progress in the Chemistry of Organic Natural Products, Vol 71 (Herz W, Kirby GW, Moore RE, Steglich W Tamm Ch, eds pp. 1 128. Springer Verlag Wien, New York, NY.
    • (1997) Progress in the Chemistry of Organic Natural Products , pp. 1-128
    • Gäde, G.1
  • 2
    • 0030239126 scopus 로고    scopus 로고
    • The revolution in insect neuropeptides illustrated by the adipokinetic hormone/ red pigment-concentrating hormone family of peptides
    • Gäde G (1996) The revolution in insect neuropeptides illustrated by the adipokinetic hormone/ red pigment-concentrating hormone family of peptides. Z Naturforsch 51c, 607 617.
    • (1996) Z Naturforsch , vol.51 , pp. 607-617
    • Gäde, G.1
  • 3
    • 1042302662 scopus 로고    scopus 로고
    • Regulation of intermediary metabolism and water balance of insects by neuropeptides
    • Gäde G (2004) Regulation of intermediary metabolism and water balance of insects by neuropeptides. Ann Rev Entomol 49, 93 113.
    • (2004) Ann Rev Entomol , vol.49 , pp. 93-113
    • Gäde, G.1
  • 4
    • 31544461506 scopus 로고    scopus 로고
    • Unique translational modification of an invertebrate neuropeptide: A phosphorylated member of the adipokinetic hormone peptide family
    • Gäde G, Simek P, Clark KD Auerswald L (2006) Unique translational modification of an invertebrate neuropeptide: a phosphorylated member of the adipokinetic hormone peptide family. Biochem J 393, 705 713.
    • (2006) Biochem J , vol.393 , pp. 705-713
    • Gäde, G.1    Simek, P.2    Clark, K.D.3    Auerswald, L.4
  • 5
    • 0027104746 scopus 로고
    • A tryptophan-substituted member of the AKH/RPCH family isolated from a stick insect corpus cardiacum
    • Gäde G, Kellner R, Rinehart KL Proefke ML (1992) A tryptophan-substituted member of the AKH/RPCH family isolated from a stick insect corpus cardiacum. Biochem Biophys Res Commun 189, 1303 1309.
    • (1992) Biochem Biophys Res Commun , vol.189 , pp. 1303-1309
    • Gäde, G.1    Kellner, R.2    Rinehart, K.L.3    Proefke, M.L.4
  • 6
    • 0028033725 scopus 로고
    • New-type of linkage between a carbohydrate and protein-C-glycosylation of a specific tryptophan residue in human RNase
    • Hofsteenge J, Müller DR, de Beer T, Löffler A, Richter WJ Vliegenthart JFG (1994) New-type of linkage between a carbohydrate and protein-C-glycosylation of a specific tryptophan residue in human RNase. Biochemistry 33, 13524 13530.
    • (1994) Biochemistry , vol.33 , pp. 13524-13530
    • Hofsteenge, J.1    Müller, D.R.2    De Beer, T.3    Löffler, A.4    Richter, W.J.5    Vliegenthart, J.F.G.6
  • 7
    • 0029088461 scopus 로고
    • The hexopyranosyl residue that is C-glycosidically linked to the side chain of tryptophan-7 in human RNase Us is α-mannopyranose
    • de Beer T, Vliegenthart JFG, Löffler A Hofsteenge J (1995) The hexopyranosyl residue that is C-glycosidically linked to the side chain of tryptophan-7 in human RNase Us is α-mannopyranose. Biochemistry 34, 11785 11789.
    • (1995) Biochemistry , vol.34 , pp. 11785-11789
    • De Beer, T.1    Vliegenthart, J.F.G.2    Löffler, A.3    Hofsteenge, J.4
  • 8
    • 0033041368 scopus 로고    scopus 로고
    • Recombinant human interleukin-12 is the second example of a C-mannosylated protein
    • Doucey M-A, Hess D, Blommers MJ Hofsteenge J (1999) Recombinant human interleukin-12 is the second example of a C-mannosylated protein. Glycobiology 9, 435 441.
    • (1999) Glycobiology , vol.9 , pp. 435-441
    • Doucey, M.-A.1    Hess, D.2    Blommers, M.J.3    Hofsteenge, J.4
  • 9
    • 0031881719 scopus 로고    scopus 로고
    • Protein C-mannosylation is enzyme-catalysed and uses dolichyl-phosphate- mannose as a precursor
    • Doucey M-A, Hess D, Cacan R Hofsteenge J (1998) Protein C-mannosylation is enzyme-catalysed and uses dolichyl-phosphate-mannose as a precursor. Mol Biol Cell 9, 291 300.
    • (1998) Mol Biol Cell , vol.9 , pp. 291-300
    • Doucey, M.-A.1    Hess, D.2    Cacan, R.3    Hofsteenge, J.4
  • 10
    • 0031882332 scopus 로고    scopus 로고
    • Recognition signal for C-mannosylation of Trp-7 in RNase 2 consists of sequence Trp-x-x-Trp
    • Krieg J, Hartmann S, Vicentini A, Gläsner W, Hess D Hofsteenge J (1998) Recognition signal for C-mannosylation of Trp-7 in RNase 2 consists of sequence Trp-x-x-Trp. Mol Biol Cell 9, 301 309.
    • (1998) Mol Biol Cell , vol.9 , pp. 301-309
    • Krieg, J.1    Hartmann, S.2    Vicentini, A.3    Gläsner, W.4    Hess, D.5    Hofsteenge, J.6
  • 11
    • 0032746280 scopus 로고    scopus 로고
    • The four terminal components of the complement system are C-mannosylated on multiple tryptophan residues
    • Hofsteenge J, Blommers M, Hess D, Furmanek A Miroshnichenko O (1999) The four terminal components of the complement system are C-mannosylated on multiple tryptophan residues. J Biol Chem 274, 32786 32794.
    • (1999) J Biol Chem , vol.274 , pp. 32786-32794
    • Hofsteenge, J.1    Blommers, M.2    Hess, D.3    Furmanek, A.4    Miroshnichenko, O.5
  • 12
    • 0034666159 scopus 로고    scopus 로고
    • Properdin, the positive regulator of complement, is highly C-mannosylated
    • Hartmann S Hofsteenge J (2000) Properdin, the positive regulator of complement, is highly C-mannosylated. J Biol Chem 275, 28569 28574.
    • (2000) J Biol Chem , vol.275 , pp. 28569-28574
    • Hartmann, S.1    Hofsteenge, J.2
  • 15
    • 0033794319 scopus 로고    scopus 로고
    • Random coil chemical shifts in acidic 8 m urea: Implementation of random coil shift data in NMRView
    • Schwarzinger S, Kroon GJA, Foss TR, Wright PE Dyson HJ (2000) Random coil chemical shifts in acidic 8 m urea: implementation of random coil shift data in NMRView. J Biomol NMR 18, 43 48.
    • (2000) J Biomol NMR , vol.18 , pp. 43-48
    • Schwarzinger, S.1    Kroon, G.J.A.2    Foss, T.R.3    Wright, P.E.4    Dyson, H.J.5
  • 17
    • 0030300101 scopus 로고    scopus 로고
    • 13C resonance assignments of a 21-amino acid glycopeptide prepared from human serum transferring
    • 13C resonance assignments of a 21-amino acid glycopeptide prepared from human serum transferring. Carb Res 296, 1 21.
    • (1996) Carb Res , vol.296 , pp. 1-21
    • Jianyun, L.1    Van, H.H.2
  • 18
    • 2442519149 scopus 로고    scopus 로고
    • C-Mannosylation of MUC5AC and MUC5B Cys subdomains
    • Perez-Vilar J, Randell SH Boucher RC (2004) C-Mannosylation of MUC5AC and MUC5B Cys subdomains. Glycobiology 14, 325 337.
    • (2004) Glycobiology , vol.14 , pp. 325-337
    • Perez-Vilar, J.1    Randell, S.H.2    Boucher, R.C.3
  • 20
    • 0033214732 scopus 로고    scopus 로고
    • Tryptophan glycoconjugates in food and human urine
    • Gutsche B, Grun C, Scheutzow D Herderich M (1999) Tryptophan glycoconjugates in food and human urine. Biochem J 343, 11 19.
    • (1999) Biochem J , vol.343 , pp. 11-19
    • Gutsche, B.1    Grun, C.2    Scheutzow, D.3    Herderich, M.4
  • 22
    • 0035108423 scopus 로고    scopus 로고
    • Conformational study of insect adipokinetic hormones using NMR constrained molecular dynamics
    • Nair MM, Jackson GE Gäde G (2001) Conformational study of insect adipokinetic hormones using NMR constrained molecular dynamics. J Comput Aided Mol Des 15, 259 270.
    • (2001) J Comput Aided Mol des , vol.15 , pp. 259-270
    • Nair, M.M.1    Jackson, G.E.2    Gäde, G.3
  • 25
    • 0033554852 scopus 로고    scopus 로고
    • Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques
    • Wilkins DH, Grimshaw SB, Receveur V, Dobson CM, Jones JA Smith LJ (1999) Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques. Biochem 38, 16424 16431.
    • (1999) Biochem , vol.38 , pp. 16424-16431
    • Wilkins, D.H.1    Grimshaw, S.B.2    Receveur, V.3    Dobson, C.M.4    Jones, J.A.5    Smith, L.J.6
  • 26
    • 0023079213 scopus 로고
    • Primary structure of the hypertrehalosaemic factor II from the corpus cardiacum of the Indian stick insect, Carausius morosus, determined by fast atom bombardment mass spectrometry
    • Gäde G Rinehart KL (1987) Primary structure of the hypertrehalosaemic factor II from the corpus cardiacum of the Indian stick insect, Carausius morosus, determined by fast atom bombardment mass spectrometry. Biol Chem Hoppe-Seyler 368, 67 75.
    • (1987) Biol Chem Hoppe-Seyler , vol.368 , pp. 67-75
    • Gäde, G.1    Rinehart, K.L.2
  • 28
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener J, Meier BH, Bachmann P Ernst RR (1979) Investigation of exchange processes by two-dimensional NMR spectroscopy. J Chem Phys 71, 4546 4553.
    • (1979) J Chem Phys , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 29
    • 5144229966 scopus 로고
    • 2D ROESY with cw spinlock for mixing phase sensitive using States-TPPI method
    • Bax A Davis DG (1985) 2D ROESY with cw spinlock for mixing phase sensitive using States-TPPI method. J Magn Reson 63, 207 213.
    • (1985) J Magn Reson , vol.63 , pp. 207-213
    • Bax, A.1    Davis, D.G.2
  • 30
    • 0344448273 scopus 로고
    • Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy
    • Braunschweiler L Ernst RR (1983) Coherence transfer by isotropic mixing: application to proton correlation spectroscopy. J Magn Reson 53, 521 528.
    • (1983) J Magn Reson , vol.53 , pp. 521-528
    • Braunschweiler, L.1    Ernst, R.R.2
  • 31
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax A Davis DG (1985) MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J Magn Reson 65, 355 360.
    • (1985) J Magn Reson , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 33
    • 0000195671 scopus 로고
    • Natural abundance Nitrogen-15 NMR by enhanced heteronuclear spectroscopy
    • Bodenhausen G Ruben DJ (1980) Natural abundance Nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem Phys Lett 69, 185 189.
    • (1980) Chem Phys Lett , vol.69 , pp. 185-189
    • Bodenhausen, G.1    Ruben, D.J.2
  • 34
    • 13444269041 scopus 로고
    • Computer-optimized decoupling scheme for wideband applications and low-level operation
    • Shaka AJ, Barker PB Freeman R (1985) Computer-optimized decoupling scheme for wideband applications and low-level operation. J Magn Reson 64, 547 552.
    • (1985) J Magn Reson , vol.64 , pp. 547-552
    • Shaka, A.J.1    Barker, P.B.2    Freeman, R.3
  • 35
    • 43949151247 scopus 로고
    • Self-compensating pulsed magnetic-field gradients for short recovery times
    • Wider G, Dötsch V Wüthrich K (1994) Self-compensating pulsed magnetic-field gradients for short recovery times. J Magn Reson 108, 255 258.
    • (1994) J Magn Reson , vol.108 , pp. 255-258
    • Wider, G.1    Dötsch, V.2    Wüthrich, K.3
  • 39
    • 0347359145 scopus 로고    scopus 로고
    • Diffusion ordered nuclear magnetic resonance spectroscopy: Principles and applications
    • Johnson CS Jr. (1999) Diffusion ordered nuclear magnetic resonance spectroscopy: principles and applications. Prog NMR Spectrosc 34, 203 256.
    • (1999) Prog NMR Spectrosc , vol.34 , pp. 203-256
    • Johnson Jr., C.S.1


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