메뉴 건너뛰기




Volumn 390, Issue 3, 2009, Pages 581-584

Crosslinking of N-acetyllactosamine-containing glycoproteins to galectin-1 with an introduced cysteine using a photoactivatable sulfhydryl reagent

Author keywords

Benzophenone; Crosslink; Galectin; Lectin; Ligand; Maleimide

Indexed keywords

4 MALEIMIDOBENZOPHENONE; ASIALOFETUIN; BENZOPHENONE DERIVATIVE; CYSTEINE; GALECTIN 1; GLYCOPROTEIN; LACTOSE; LAMININ; THIOL REAGENT; UNCLASSIFIED DRUG;

EID: 70449726453     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.10.009     Document Type: Article
Times cited : (7)

References (25)
  • 1
    • 0030064027 scopus 로고    scopus 로고
    • Galectins: a family of animal lectins that decipher glycocodes
    • Kasai K., and Hirabayashi J. Galectins: a family of animal lectins that decipher glycocodes. J. Biochem. (Tokyo) 119 (1996) 1-8
    • (1996) J. Biochem. (Tokyo) , vol.119 , pp. 1-8
    • Kasai, K.1    Hirabayashi, J.2
  • 3
    • 0032875554 scopus 로고    scopus 로고
    • God must love galectins; he made so many of them
    • Cooper D.N., and Barondes S.H. God must love galectins; he made so many of them. Glycobiology 9 (1999) 979-984
    • (1999) Glycobiology , vol.9 , pp. 979-984
    • Cooper, D.N.1    Barondes, S.H.2
  • 5
    • 11144241063 scopus 로고    scopus 로고
    • Galectins as modulators of tumor progression
    • Liu F.T., and Rabinovich G.A. Galectins as modulators of tumor progression. Nat. Rev. Cancer 5 (2005) 29-41
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 29-41
    • Liu, F.T.1    Rabinovich, G.A.2
  • 6
    • 0036798862 scopus 로고    scopus 로고
    • Ah, sweet mystery of death! Galectins and control of cell fate
    • Hernandez J.D., and Baum L.G. Ah, sweet mystery of death! Galectins and control of cell fate. Glycobiology 12 (2002) 127R-136R
    • (2002) Glycobiology , vol.12
    • Hernandez, J.D.1    Baum, L.G.2
  • 7
    • 0032904627 scopus 로고    scopus 로고
    • Mechanism that regulate the function of the selectins and their ligands
    • Vestweber D., and Blanks J.E. Mechanism that regulate the function of the selectins and their ligands. Physiol. Rev. 79 (1999) 181-213
    • (1999) Physiol. Rev. , vol.79 , pp. 181-213
    • Vestweber, D.1    Blanks, J.E.2
  • 8
    • 59149097542 scopus 로고    scopus 로고
    • Galectin-glycan lattices regulate cell-surface glycoprotein organization and signalling
    • Garner O.B., and Baum L.G. Galectin-glycan lattices regulate cell-surface glycoprotein organization and signalling. Biochem. Soc. Trans. 36 (2008) 1472-1477
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 1472-1477
    • Garner, O.B.1    Baum, L.G.2
  • 11
    • 33749044197 scopus 로고    scopus 로고
    • Crosslinking of low-affinity glycoprotein ligands to galectin LEC-1 using a photoactivatable sulfhydryl reagent
    • Arata Y., Tamura M., Nonaka T., and Kasai K. Crosslinking of low-affinity glycoprotein ligands to galectin LEC-1 using a photoactivatable sulfhydryl reagent. Biochem. Biophys. Res. Commun. 350 (2006) 185-190
    • (2006) Biochem. Biophys. Res. Commun. , vol.350 , pp. 185-190
    • Arata, Y.1    Tamura, M.2    Nonaka, T.3    Kasai, K.4
  • 12
    • 0026344814 scopus 로고
    • Effect of amino acid substitution by site-directed mutagenesis on the carbohydrate recognition and stability of human 14-kDa β-galactoside-binding lectin
    • Hirabayashi J., and Kasai K. Effect of amino acid substitution by site-directed mutagenesis on the carbohydrate recognition and stability of human 14-kDa β-galactoside-binding lectin. J. Biol. Chem. 266 (1991) 23648-23653
    • (1991) J. Biol. Chem. , vol.266 , pp. 23648-23653
    • Hirabayashi, J.1    Kasai, K.2
  • 13
    • 0030758114 scopus 로고    scopus 로고
    • The two lectin domains of the tandem-repeat 32-kDa galectin of the nematode Caenorhabditis elegans have different binding properties. Studies with recombinant protein
    • Arata Y., Hirabayashi J., and Kasai K. The two lectin domains of the tandem-repeat 32-kDa galectin of the nematode Caenorhabditis elegans have different binding properties. Studies with recombinant protein. J. Biochem. (Tokyo) 121 (1997) 1002-1009
    • (1997) J. Biochem. (Tokyo) , vol.121 , pp. 1002-1009
    • Arata, Y.1    Hirabayashi, J.2    Kasai, K.3
  • 14
    • 0023318256 scopus 로고
    • Further characterization and structural studies on human placenta lectin
    • Hirabayashi J., Kawasaki H., Suzuki K., and Kasai K. Further characterization and structural studies on human placenta lectin. J. Biochem. (Tokyo) 101 (1987) 987-995
    • (1987) J. Biochem. (Tokyo) , vol.101 , pp. 987-995
    • Hirabayashi, J.1    Kawasaki, H.2    Suzuki, K.3    Kasai, K.4
  • 15
    • 0028235205 scopus 로고
    • Benzophenone photophores in biochemistry
    • Dormán G., and Prestwich G.D. Benzophenone photophores in biochemistry. Biochemistry 33 (1994) 5661-5673
    • (1994) Biochemistry , vol.33 , pp. 5661-5673
    • Dormán, G.1    Prestwich, G.D.2
  • 16
    • 5144232009 scopus 로고    scopus 로고
    • Growth-regulatory human galectin-1: crystallographic characterization of the structural changes induced by single-site mutations and their impact on the thermodynamics of ligand binding
    • López-Lucendo M.F., Solís D., André S., Hirabayashi J., Kasai K., Kaltner K., Gabius H.J., and Romero A. Growth-regulatory human galectin-1: crystallographic characterization of the structural changes induced by single-site mutations and their impact on the thermodynamics of ligand binding. J. Mol. Biol. 343 (2004) 957-970
    • (2004) J. Mol. Biol. , vol.343 , pp. 957-970
    • López-Lucendo, M.F.1    Solís, D.2    André, S.3    Hirabayashi, J.4    Kasai, K.5    Kaltner, K.6    Gabius, H.J.7    Romero, A.8
  • 20
    • 0037125922 scopus 로고    scopus 로고
    • Localization of subunits D, E, and G in the yeast V-ATPase complex using cysteine-mediated crosslinking to subunit B
    • Arata Y., Baleja J.D., and Forgac M. Localization of subunits D, E, and G in the yeast V-ATPase complex using cysteine-mediated crosslinking to subunit B. Biochemistry 41 (2002) 11301-11307
    • (2002) Biochemistry , vol.41 , pp. 11301-11307
    • Arata, Y.1    Baleja, J.D.2    Forgac, M.3
  • 21
    • 0033462203 scopus 로고    scopus 로고
    • Smooth muscle α-tropomyosin crosslinks to caldesmon, to actin and to myosin subfragment 1 on the muscle thin filament
    • Golitsina N.L., and Lehrer S.S. Smooth muscle α-tropomyosin crosslinks to caldesmon, to actin and to myosin subfragment 1 on the muscle thin filament. FEBS Lett. 463 (1999) 146-150
    • (1999) FEBS Lett. , vol.463 , pp. 146-150
    • Golitsina, N.L.1    Lehrer, S.S.2
  • 23
    • 0042027823 scopus 로고    scopus 로고
    • Frontal affinity chromatography as a tool for elucidation of sugar recognition properties of lectins
    • Hirabayashi J., Arata Y., and Kasai K. Frontal affinity chromatography as a tool for elucidation of sugar recognition properties of lectins. Methods Enzymol. 362 (2003) 353-368
    • (2003) Methods Enzymol. , vol.362 , pp. 353-368
    • Hirabayashi, J.1    Arata, Y.2    Kasai, K.3
  • 24
    • 0035793553 scopus 로고    scopus 로고
    • Sugar binding properties of the two lectin domains of the tandem repeat-type galectin LEC-1 (N32) of Caenorhabditis elegans. Detailed analysis by an improved frontal affinity chromatography method
    • Arata Y., Hirabayashi J., and Kasai K. Sugar binding properties of the two lectin domains of the tandem repeat-type galectin LEC-1 (N32) of Caenorhabditis elegans. Detailed analysis by an improved frontal affinity chromatography method. J. Biol. Chem. 276 (2001) 3068-3077
    • (2001) J. Biol. Chem. , vol.276 , pp. 3068-3077
    • Arata, Y.1    Hirabayashi, J.2    Kasai, K.3
  • 25
    • 0028986609 scopus 로고
    • Galectin-1, a β-galactoside-binding lectin in Chinese hamster ovary cells. I. Physical and chemical characterization
    • Cho M., and Cummings R.D. Galectin-1, a β-galactoside-binding lectin in Chinese hamster ovary cells. I. Physical and chemical characterization. J. Biol. Chem. 270 (1995) 5189-5206
    • (1995) J. Biol. Chem. , vol.270 , pp. 5189-5206
    • Cho, M.1    Cummings, R.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.