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Volumn 415, Issue , 2006, Pages 103-113

Determination of Glycosylation Sites and Disulfide Bond Structures Using LC/ESI-MS/MS Analysis

(2)  Yen, Ten Yang a   Macher, Bruce A a  

a NONE

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CHYMOTRYPSIN; CYSTEINE; GLYCOPROTEIN; MEMBRANE PROTEIN; TRYPSIN;

EID: 33751003222     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(06)15007-7     Document Type: Review
Times cited : (11)

References (10)
  • 1
    • 0035805605 scopus 로고    scopus 로고
    • Unique disulfide bond structures found in ST8Sia IV polysialyltransferase are required for its activity
    • Angata K., Yen T.-Y., El-Battari A., Macher B.A., and Fukuda M. Unique disulfide bond structures found in ST8Sia IV polysialyltransferase are required for its activity. J. Biol. Chem. 276 (2001) 15369-15377
    • (2001) J. Biol. Chem. , vol.276 , pp. 15369-15377
    • Angata, K.1    Yen, T.-Y.2    El-Battari, A.3    Macher, B.A.4    Fukuda, M.5
  • 2
    • 0034917531 scopus 로고    scopus 로고
    • Neighboring cysteine residues in human Fucosyltransferase VII are engaged in disulfide bridges, forming small loop structures: A proposed 3D model based on location of cysteines, and threading and homology modeling
    • de Vries T., Yen T.-Y., Joshi R.K., Storm J., van den Eijnden D.H., Knegtel R.M.A., Bunschoten H., Joziasse D.H., and Macher B.A. Neighboring cysteine residues in human Fucosyltransferase VII are engaged in disulfide bridges, forming small loop structures: A proposed 3D model based on location of cysteines, and threading and homology modeling. Glycobiology 11 (2001) 423-432
    • (2001) Glycobiology , vol.11 , pp. 423-432
    • de Vries, T.1    Yen, T.-Y.2    Joshi, R.K.3    Storm, J.4    van den Eijnden, D.H.5    Knegtel, R.M.A.6    Bunschoten, H.7    Joziasse, D.H.8    Macher, B.A.9
  • 3
    • 0027467841 scopus 로고
    • A conserved disulphide bond in sialyltransferases
    • Drickamer K. A conserved disulphide bond in sialyltransferases. Glycobiology 3 (1993) 2-3
    • (1993) Glycobiology , vol.3 , pp. 2-3
    • Drickamer, K.1
  • 6
    • 0030851778 scopus 로고    scopus 로고
    • Lewis X biosynthesis in Helicobacter pylori: Molecular cloning of an α (1,3)-fucosyltransferase gene
    • Martin S.L., Edbrooke M.R., Hodgman T.C., van den Eijnden D.H., and Bird M.I. Lewis X biosynthesis in Helicobacter pylori: Molecular cloning of an α (1,3)-fucosyltransferase gene. J. Biol. Chem. 272 (1997) 21349-21356
    • (1997) J. Biol. Chem. , vol.272 , pp. 21349-21356
    • Martin, S.L.1    Edbrooke, M.R.2    Hodgman, T.C.3    van den Eijnden, D.H.4    Bird, M.I.5
  • 7
    • 0032906430 scopus 로고    scopus 로고
    • Divergent evolution of fucosyltransferase genes from vertebrates, invertebrates, and bacteria
    • Oriol R., Mollicone R., Cailleay A., Balanzino L., and Breton C. Divergent evolution of fucosyltransferase genes from vertebrates, invertebrates, and bacteria. Glycobiology 9 (1999) 323-334
    • (1999) Glycobiology , vol.9 , pp. 323-334
    • Oriol, R.1    Mollicone, R.2    Cailleay, A.3    Balanzino, L.4    Breton, C.5
  • 8
    • 0034866109 scopus 로고    scopus 로고
    • α1,3 galactosyltransferase: New sequences and characterization of conserved cysteine residues
    • Shetterly S., Tom I., Yen T.-Y., Joshi R., Lee L., Wang P.G., and Macher B.A. α1,3 galactosyltransferase: New sequences and characterization of conserved cysteine residues. Glycobiology 11 (2001) 645-653
    • (2001) Glycobiology , vol.11 , pp. 645-653
    • Shetterly, S.1    Tom, I.2    Yen, T.-Y.3    Joshi, R.4    Lee, L.5    Wang, P.G.6    Macher, B.A.7
  • 9
    • 0033863181 scopus 로고    scopus 로고
    • Characterization of cysteine residues and disulfide bonds in proteins by liquid chromatography/electrospray ionization tandem mass spectrometry
    • Yen T.-Y., Joshi R.K., Yan H., Seto N.O.L., Palcic M.M., and Macher B.A. Characterization of cysteine residues and disulfide bonds in proteins by liquid chromatography/electrospray ionization tandem mass spectrometry. J. Mass Spectrom. 35 (2000) 990-1002
    • (2000) J. Mass Spectrom. , vol.35 , pp. 990-1002
    • Yen, T.-Y.1    Joshi, R.K.2    Yan, H.3    Seto, N.O.L.4    Palcic, M.M.5    Macher, B.A.6
  • 10
    • 0242496203 scopus 로고    scopus 로고
    • Highly Conserved Cysteines of Mouse Core 2 β1,6 N-Acetylglucosaminyltransferase-I Form a Network of Disulfide Bonds and Include a Thiol That Affects Enzyme Activity
    • Yen T.-Y., Macher B.A., Bryson S., Chang X., Tvaroška I., Tse R., Takeshita S., Lew A.M., and Datti A. Highly Conserved Cysteines of Mouse Core 2 β1,6 N-Acetylglucosaminyltransferase-I Form a Network of Disulfide Bonds and Include a Thiol That Affects Enzyme Activity. J. Biol. Chem. 278 (2003) 45864-45881
    • (2003) J. Biol. Chem. , vol.278 , pp. 45864-45881
    • Yen, T.-Y.1    Macher, B.A.2    Bryson, S.3    Chang, X.4    Tvaroška, I.5    Tse, R.6    Takeshita, S.7    Lew, A.M.8    Datti, A.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.