메뉴 건너뛰기




Volumn 343, Issue 4, 2004, Pages 957-970

Growth-regulatory human galectin-1: Crystallographic characterisation of the structural changes induced by single-site mutations and their impact on the thermodynamics of ligand binding

Author keywords

apoptosis; galectin; glycoprotein; lectin; neuroblastoma

Indexed keywords

ASPARTIC ACID; CARBOHYDRATE; DISULFIDE; GALECTIN; GALECTIN 1; LECTIN; LIGAND; REDUCING AGENT; SUGAR;

EID: 5144232009     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.08.078     Document Type: Article
Times cited : (275)

References (74)
  • 1
    • 0001810168 scopus 로고    scopus 로고
    • The information-storing potential of the sugar code
    • H.-J. Gabius S. Gabius Chapman & Hall Weinheim-London
    • R.A. Laine The information-storing potential of the sugar code H.-J. Gabius S. Gabius Glycosciences: Status and Perspectives 1997 Chapman & Hall Weinheim-London 1 14
    • (1997) Glycosciences: Status and Perspectives , pp. 1-14
    • Laine, R.A.1
  • 2
    • 0034079042 scopus 로고    scopus 로고
    • Biological information transfer beyond the genetic code: The sugar code
    • H.-J. Gabius Biological information transfer beyond the genetic code: the sugar code Naturwissenschaften 87 2000 108 121
    • (2000) Naturwissenschaften , vol.87 , pp. 108-121
    • Gabius, H.-J.1
  • 3
    • 0035834665 scopus 로고    scopus 로고
    • Reflections on glycobiology
    • S. Roseman Reflections on glycobiology J. Biol. Chem. 276 2001 41527 41542
    • (2001) J. Biol. Chem. , vol.276 , pp. 41527-41542
    • Roseman, S.1
  • 4
    • 0035208055 scopus 로고    scopus 로고
    • Towards defining the role of glycans as hardware in information storage and transfer: Basic principles, experimental approaches and recent progress
    • D. Solís, J. Jiménez-Barbero, H. Kaltner, A. Romero, H.-C. Siebert, C.-W. von der Lieth, and H.-J. Gabius Towards defining the role of glycans as hardware in information storage and transfer: basic principles, experimental approaches and recent progress Cells Tissues Organs 168 2001 5 23
    • (2001) Cells Tissues Organs , vol.168 , pp. 5-23
    • Solís, D.1    Jiménez-Barbero, J.2    Kaltner, H.3    Romero, A.4    Siebert, H.-C.5    Von Der Lieth, C.-W.6    Gabius, H.-J.7
  • 5
    • 0001811291 scopus 로고    scopus 로고
    • Glycosyltransferases involved in N- and O-glycan synthesis
    • H.-J. Gabius S. Gabius Chapman & Hall Weinheim-London
    • I. Brockhausen, and H. Schachter Glycosyltransferases involved in N- and O-glycan synthesis H.-J. Gabius S. Gabius Glycosciences: Status and Perspectives 1997 Chapman & Hall Weinheim-London 79 113
    • (1997) Glycosciences: Status and Perspectives , pp. 79-113
    • Brockhausen, I.1    Schachter, H.2
  • 6
    • 0032953692 scopus 로고    scopus 로고
    • Eukaryotic glycosylation - Whim of nature or multipurpose tool?
    • G. Reuter, and H.-J. Gabius Eukaryotic glycosylation - whim of nature or multipurpose tool? Cell. Mol. Life Sci. 55 1999 368 422
    • (1999) Cell. Mol. Life Sci. , vol.55 , pp. 368-422
    • Reuter, G.1    Gabius, H.-J.2
  • 8
    • 2042442428 scopus 로고    scopus 로고
    • On the origin of glycome and saccharide recognition
    • J. Hirabayashi On the origin of glycome and saccharide recognition Trends Glycosci. Glycotechnol. 16 2004 63 85
    • (2004) Trends Glycosci. Glycotechnol. , vol.16 , pp. 63-85
    • Hirabayashi, J.1
  • 9
    • 0030064027 scopus 로고    scopus 로고
    • Galectins: A family of animal lectins that decipher glycocodes
    • K.-I. Kasai, and J. Hirabayashi Galectins: a family of animal lectins that decipher glycocodes J. Biochem. 119 1996 1 8
    • (1996) J. Biochem. , vol.119 , pp. 1-8
    • Kasai, K.-I.1    Hirabayashi, J.2
  • 10
  • 11
    • 0031784245 scopus 로고    scopus 로고
    • Animal lectins as cell adhesion molecules
    • H. Kaltner, and B. Stierstorfer Animal lectins as cell adhesion molecules Acta Anat. 161 1998 162 179
    • (1998) Acta Anat. , vol.161 , pp. 162-179
    • Kaltner, H.1    Stierstorfer, B.2
  • 12
    • 0037136416 scopus 로고    scopus 로고
    • Galectinomics: Finding themes in complexity
    • D.N.W. Cooper Galectinomics: finding themes in complexity Biochim. Biophys. Acta 1572 2002 209 231
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 209-231
    • Cooper, D.N.W.1
  • 13
    • 4143099262 scopus 로고    scopus 로고
    • Tumor galectinology: Insights into the complex network of a family of endogenous lectins
    • H. Lahm, S. André, A. Hoeflich, H. Kaltner, H.-C. Siebert, and B. Sordat Tumor galectinology: insights into the complex network of a family of endogenous lectins Glycoconjugate J. 20 2004 227 238
    • (2004) Glycoconjugate J. , vol.20 , pp. 227-238
    • Lahm, H.1    André, S.2    Hoeflich, A.3    Kaltner, H.4    Siebert, H.-C.5    Sordat, B.6
  • 15
    • 0035929631 scopus 로고    scopus 로고
    • Negative regulation of neuroblastoma cell growth by carbohydrate- dependent surface binding of galectin-1 and functional divergence from galectin-3
    • J. Kopitz, C. von Reitzenstein, S. André, H. Kaltner, J. Uhl, and V. Ehemann Negative regulation of neuroblastoma cell growth by carbohydrate-dependent surface binding of galectin-1 and functional divergence from galectin-3 J. Biol. Chem. 276 2001 35917 35923
    • (2001) J. Biol. Chem. , vol.276 , pp. 35917-35923
    • Kopitz, J.1    Von Reitzenstein, C.2    André, S.3    Kaltner, H.4    Uhl, J.5    Ehemann, V.6
  • 16
    • 0035107949 scopus 로고    scopus 로고
    • Galectin-1 is highly expressed in human gliomas with relevance for modulation of invasion of tumor astrocytes into the brain parenchyma
    • S. Rorive, N. Belot, C. Decaestecker, F. Lefranc, L. Gordower, and S. Micik Galectin-1 is highly expressed in human gliomas with relevance for modulation of invasion of tumor astrocytes into the brain parenchyma Glia 33 2001 241 255
    • (2001) Glia , vol.33 , pp. 241-255
    • Rorive, S.1    Belot, N.2    Decaestecker, C.3    Lefranc, F.4    Gordower, L.5    Micik, S.6
  • 17
    • 0036289096 scopus 로고    scopus 로고
    • Galectin-1 modulates human glioblastoma cell migration into the brain through modifications to the actin cytoskeleton and levels of expression of small GTPases
    • I. Camby, N. Belot, F. Lefranc, N. Sadeghi, Y. de Launoit, and H. Kaltner Galectin-1 modulates human glioblastoma cell migration into the brain through modifications to the actin cytoskeleton and levels of expression of small GTPases J. Neuropathol. Exp. Neurol. 61 2002 585 596
    • (2002) J. Neuropathol. Exp. Neurol. , vol.61 , pp. 585-596
    • Camby, I.1    Belot, N.2    Lefranc, F.3    Sadeghi, N.4    De Launoit, Y.5    Kaltner, H.6
  • 18
    • 0037136408 scopus 로고    scopus 로고
    • Role of galectins in inflammatory and immunomodulatory processes
    • G.A. Rabinovich, N. Rubinstein, and M.A. Toscano Role of galectins in inflammatory and immunomodulatory processes Biochim. Biophys. Acta 1572 2002 274 284
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 274-284
    • Rabinovich, G.A.1    Rubinstein, N.2    Toscano, M.A.3
  • 19
    • 18444408692 scopus 로고    scopus 로고
    • - leukemic T cells from patients with Sézary syndrome are protected from galectin-1-triggered T cell death
    • - leukemic T cells from patients with Sézary syndrome are protected from galectin-1-triggered T cell death Leukemia 16 2002 840 845
    • (2002) Leukemia , vol.16 , pp. 840-845
    • Rappl, G.1    Abken, H.2    Muche, J.M.3    Sterry, W.4    Tilgen, W.5    André, S.6
  • 20
    • 0037454758 scopus 로고    scopus 로고
    • Upregulation of galectins-1 and -3 in human colon cancer and their role in regulating cell migration
    • A. Hittelet, H. Legendre, N. Nagy, Y. Bronckart, J.-C. Pector, and I. Salmon Upregulation of galectins-1 and -3 in human colon cancer and their role in regulating cell migration Int. J. Cancer 103 2003 370 379
    • (2003) Int. J. Cancer , vol.103 , pp. 370-379
    • Hittelet, A.1    Legendre, H.2    Nagy, N.3    Bronckart, Y.4    Pector, J.-C.5    Salmon, I.6
  • 21
    • 0344559105 scopus 로고    scopus 로고
    • Refined prognostic evaluation in colon carcinoma using immunohistochemical galectin fingerprinting
    • N. Nagy, H. Legendre, O. Engels, S. André, H. Kaltner, and K. Wasano Refined prognostic evaluation in colon carcinoma using immunohistochemical galectin fingerprinting Cancer 97 2003 1849 1858
    • (2003) Cancer , vol.97 , pp. 1849-1858
    • Nagy, N.1    Legendre, H.2    Engels, O.3    André, S.4    Kaltner, H.5    Wasano, K.6
  • 22
    • 0842328412 scopus 로고    scopus 로고
    • Persubstituted cyclodextrin-based glycoclusters as inhibitors of protein-carbohydrate recognition using purified plant and mammalian lectins and wild-type and lectin-gene-transfected tumor cells as targets
    • S. André, H. Kaltner, T. Furuike, S.-I. Nishimura, and H.-J. Gabius Persubstituted cyclodextrin-based glycoclusters as inhibitors of protein-carbohydrate recognition using purified plant and mammalian lectins and wild-type and lectin-gene-transfected tumor cells as targets Bioconjugate Chem. 15 2004 87 98
    • (2004) Bioconjugate Chem. , vol.15 , pp. 87-98
    • André, S.1    Kaltner, H.2    Furuike, T.3    Nishimura, S.-I.4    Gabius, H.-J.5
  • 23
    • 0032080122 scopus 로고    scopus 로고
    • 1, a product of the growth-controlling activity of a cell surface ganglioside sialidase, on human neuroblastoma cells in culture
    • 1, a product of the growth-controlling activity of a cell surface ganglioside sialidase, on human neuroblastoma cells in culture J. Biol. Chem. 273 1998 11205 11211
    • (1998) J. Biol. Chem. , vol.273 , pp. 11205-11211
    • Kopitz, J.1    Von Reitzenstein, C.2    Burchert, M.3    Cantz, M.4    Gabius, H.-J.5
  • 26
    • 0035915498 scopus 로고    scopus 로고
    • NMR investigation of protein-carbohydrate interactions: Insights into the topology of the bound conformation of a lactose isomer and β-galactosyl xyloses to mistletoe lectin and galectin-1
    • J.M. Alonso-Plaza, M.A. Canales, M. Jimenez, J.L. Roldan, A. Garcia-Herrero, and L. Itturrino NMR investigation of protein-carbohydrate interactions: insights into the topology of the bound conformation of a lactose isomer and β-galactosyl xyloses to mistletoe lectin and galectin-1 Biochim. Biophys. Acta 1568 2001 225 236
    • (2001) Biochim. Biophys. Acta , vol.1568 , pp. 225-236
    • Alonso-Plaza, J.M.1    Canales, M.A.2    Jimenez, M.3    Roldan, J.L.4    Garcia-Herrero, A.5    Itturrino, L.6
  • 29
    • 2342508517 scopus 로고    scopus 로고
    • Galectin-1(L11A) predicted from a computed galectin-1 farnesyl-binding pocket selectively inhibits Ras-GTP
    • B. Rotblat, H. Niv, S. André, H. Kaltner, H.-J. Gabius, and Y. Kloog Galectin-1(L11A) predicted from a computed galectin-1 farnesyl-binding pocket selectively inhibits Ras-GTP Cancer Res. 64 2004 3112 3118
    • (2004) Cancer Res. , vol.64 , pp. 3112-3118
    • Rotblat, B.1    Niv, H.2    André, S.3    Kaltner, H.4    Gabius, H.-J.5    Kloog, Y.6
  • 30
    • 0037136412 scopus 로고    scopus 로고
    • Binding and cross-linking properties of galectins
    • C.F. Brewer Binding and cross-linking properties of galectins Biochim. Biophys. Acta 1572 2002 265 272
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 265-272
    • Brewer, C.F.1
  • 31
    • 0037635976 scopus 로고    scopus 로고
    • Detection of ligand- and solvent-induced shape alterations of cell-growth-regulatory human lectin galectin-1 in solution by small angle neutron and x-ray scattering
    • L. He, S. André, H.-C. Siebert, H. Helmholz, B. Niemeyer, and H.-J. Gabius Detection of ligand- and solvent-induced shape alterations of cell-growth-regulatory human lectin galectin-1 in solution by small angle neutron and x-ray scattering Biophys. J. 85 2003 511 524
    • (2003) Biophys. J. , vol.85 , pp. 511-524
    • He, L.1    André, S.2    Siebert, H.-C.3    Helmholz, H.4    Niemeyer, B.5    Gabius, H.-J.6
  • 32
    • 0029035874 scopus 로고
    • Energetics of carbohydrate binding by a 14 kDa S-type mammalian lectin
    • R. Ramkumar, A. Surolia, and S.K. Podder Energetics of carbohydrate binding by a 14 kDa S-type mammalian lectin Biochem. J. 308 1995 237 241
    • (1995) Biochem. J. , vol.308 , pp. 237-241
    • Ramkumar, R.1    Surolia, A.2    Podder, S.K.3
  • 33
    • 0029908797 scopus 로고    scopus 로고
    • Thermodynamics of carbohydrate binding to galectin-1 from Chinese hamster ovary cells and two mutants. a comparison with four galactose-specific plant lectins
    • D. Gupta, M. Cho, R.D. Cummings, and C.F. Brewer Thermodynamics of carbohydrate binding to galectin-1 from Chinese hamster ovary cells and two mutants. A comparison with four galactose-specific plant lectins Biochemistry 35 1996 15236 15243
    • (1996) Biochemistry , vol.35 , pp. 15236-15243
    • Gupta, D.1    Cho, M.2    Cummings, R.D.3    Brewer, C.F.4
  • 34
    • 0032574694 scopus 로고    scopus 로고
    • Thermodynamics of bovine spleen galectin-1 binding to disaccharides: Correlation with structure and its effect on oligomerization at the denaturation temperature
    • F.P. Schwarz, H. Ahmed, M.A. Bianchet, L.M. Amzel, and G.R. Vasta Thermodynamics of bovine spleen galectin-1 binding to disaccharides: correlation with structure and its effect on oligomerization at the denaturation temperature Biochemistry 37 1998 5867 5877
    • (1998) Biochemistry , vol.37 , pp. 5867-5877
    • Schwarz, F.P.1    Ahmed, H.2    Bianchet, M.A.3    Amzel, L.M.4    Vasta, G.R.5
  • 35
    • 0032852724 scopus 로고    scopus 로고
    • Microcalorimetric indications for ligand binding as a function of the protein for galactoside-specific plant and avian lectins
    • S. Bharadwaj, H. Kaltner, E.Y. Korchagina, N.V. Bovin, H.-J. Gabius, and A. Surolia Microcalorimetric indications for ligand binding as a function of the protein for galactoside-specific plant and avian lectins Biochim. Biophys. Acta 1472 1999 191 196
    • (1999) Biochim. Biophys. Acta , vol.1472 , pp. 191-196
    • Bharadwaj, S.1    Kaltner, H.2    Korchagina, E.Y.3    Bovin, N.V.4    Gabius, H.-J.5    Surolia, A.6
  • 36
    • 0036436051 scopus 로고    scopus 로고
    • Thermodynamic binding studies of cell surface carbohydrate epitopes to galectins-1, -3, and -7: Evidence for differential binding specificities
    • N. Ahmad, H.-J. Gabius, H. Kaltner, S. André, I. Kuwabara, and F.-T. Liu Thermodynamic binding studies of cell surface carbohydrate epitopes to galectins-1, -3, and -7: evidence for differential binding specificities Can. J. Chem. 80 2002 1096 1104
    • (2002) Can. J. Chem. , vol.80 , pp. 1096-1104
    • Ahmad, N.1    Gabius, H.-J.2    Kaltner, H.3    André, S.4    Kuwabara, I.5    Liu, F.-T.6
  • 38
    • 0027958144 scopus 로고
    • Structure of S-lectin, a developmentally regulated vertebrate β-galactoside-binding protein
    • D. Liao, G. Kapadia, H. Ahmed, G.R. Vasta, and O. Herzberg Structure of S-lectin, a developmentally regulated vertebrate β-galactoside-binding protein Proc. Natl Acad. Sci. USA 91 1994 1428 1432
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 1428-1432
    • Liao, D.1    Kapadia, G.2    Ahmed, H.3    Vasta, G.R.4    Herzberg, O.5
  • 39
    • 0033607322 scopus 로고    scopus 로고
    • The 2.15 Å crystal structure of CG-16, the developmentally regulated homodimeric chicken galectin
    • P.F. Varela, D. Solís, T. Díaz-Mauriño, H. Kaltner, H.-J. Gabius, and A. Romero The 2.15 Å crystal structure of CG-16, the developmentally regulated homodimeric chicken galectin J. Mol. Biol. 294 1999 537 549
    • (1999) J. Mol. Biol. , vol.294 , pp. 537-549
    • Varela, P.F.1    Solís, D.2    Díaz-Mauriño, T.3    Kaltner, H.4    Gabius, H.-J.5    Romero, A.6
  • 40
    • 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
    • J. Hirabayashi, and K.-I. Kasai 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.-I.2
  • 41
    • 0027942208 scopus 로고
    • Further evidence by site-directed mutagenesis that conserved hydrophilic residues form a carbohydrate-binding site of human galectin-1
    • J. Hirabayashi, and K.-I. Kasai Further evidence by site-directed mutagenesis that conserved hydrophilic residues form a carbohydrate-binding site of human galectin-1 Glycoconjugate J. 11 1994 437 442
    • (1994) Glycoconjugate J. , vol.11 , pp. 437-442
    • Hirabayashi, J.1    Kasai, K.-I.2
  • 42
    • 0027754166 scopus 로고
    • X-ray crystal structure of the human dimeric S-lac lectin, L-14-II, in complex with lactose at 2.9 Å resolution
    • Y.D. Lobsanov, M.A. Gitt, H. Leffler, S.H. Barondes, and J.M. Rini X-ray crystal structure of the human dimeric S-lac lectin, L-14-II, in complex with lactose at 2.9 Å resolution J. Biol. Chem. 268 1993 27034 27038
    • (1993) J. Biol. Chem. , vol.268 , pp. 27034-27038
    • Lobsanov, Y.D.1    Gitt, M.A.2    Leffler, H.3    Barondes, S.H.4    Rini, J.M.5
  • 43
    • 0032557645 scopus 로고    scopus 로고
    • X-ray crystal structure of the human galectin-3 carbohydrate recognition domain at 2.1 Å resolution
    • J. Seetharam, A. Kanigsberg, R. Slaaby, H. Leffler, S.H. Barondes, and J.M. Rini X-ray crystal structure of the human galectin-3 carbohydrate recognition domain at 2.1 Å resolution J. Biol. Chem. 273 1998 13047 13052
    • (1998) J. Biol. Chem. , vol.273 , pp. 13047-13052
    • Seetharam, J.1    Kanigsberg, A.2    Slaaby, R.3    Leffler, H.4    Barondes, S.H.5    Rini, J.M.6
  • 45
    • 0029646108 scopus 로고
    • Crystal structure of human Charcot-Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins
    • D.D. Leonidas, B.L. Elbert, Z. Zhou, H. Leffler, S.J. Ackerman, and K.R. Acharya Crystal structure of human Charcot-Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins Structure 3 1995 1379 1393
    • (1995) Structure , vol.3 , pp. 1379-1393
    • Leonidas, D.D.1    Elbert, B.L.2    Zhou, Z.3    Leffler, H.4    Ackerman, S.J.5    Acharya, K.R.6
  • 46
    • 0034663733 scopus 로고    scopus 로고
    • Soluble β-galactosyl-binding lectin (galectin) from toad ovary: Crystallographic studies of two protein-sugar complexes
    • M.A. Bianchet, H. Ahmed, G.R. Vasta, and L.M. Amzel Soluble β-galactosyl-binding lectin (galectin) from toad ovary: crystallographic studies of two protein-sugar complexes Proteins: Struct. Funct. Genet. 40 2000 378 388
    • (2000) Proteins: Struct. Funct. Genet. , vol.40 , pp. 378-388
    • Bianchet, M.A.1    Ahmed, H.2    Vasta, G.R.3    Amzel, L.M.4
  • 47
    • 0037136417 scopus 로고    scopus 로고
    • Principles of structures of animal and plant lectins
    • R. Loris Principles of structures of animal and plant lectins Biochim. Biophys. Acta 1572 2002 198 208
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 198-208
    • Loris, R.1
  • 49
    • 0035814138 scopus 로고    scopus 로고
    • Wedgelike glycodendrimers as inhibitors of binding of mammalian galectins to various glycoproteins, lactose maxiclusters and cell surface glycoconjugates
    • S. André, R.J. Pieters, I. Vrasidas, H. Kaltner, I. Kuwabara, and F.-T. Liu Wedgelike glycodendrimers as inhibitors of binding of mammalian galectins to various glycoproteins, lactose maxiclusters and cell surface glycoconjugates ChemBioChem 2 2001 822 830
    • (2001) ChemBioChem , vol.2 , pp. 822-830
    • André, S.1    Pieters, R.J.2    Vrasidas, I.3    Kaltner, H.4    Kuwabara, I.5    Liu, F.-T.6
  • 50
    • 1642499128 scopus 로고    scopus 로고
    • Determination of modulation of ligand properties of synthetic complex-type biantennary N-glycans by introduction of bisecting GlcNAc in silico, in vitro and in vivo
    • S. André, C. Unverzagt, S. Kojima, M. Frank, J. Seifert, and C. Fink Determination of modulation of ligand properties of synthetic complex-type biantennary N-glycans by introduction of bisecting GlcNAc in silico, in vitro and in vivo Eur. J. Biochem. 271 2004 118 134
    • (2004) Eur. J. Biochem. , vol.271 , pp. 118-134
    • André, S.1    Unverzagt, C.2    Kojima, S.3    Frank, M.4    Seifert, J.5    Fink, C.6
  • 51
    • 0036384139 scopus 로고    scopus 로고
    • Crystal structure of a conger eel galectin (congerin II) at 1.45 Å resolution: Implication for the accelerated evolution of a new ligand-binding site following gene duplication
    • T. Shirai, Y. Matsui, C. Shionyu-Mitsuyama, T. Yamane, H. Kamiya, and C. Ishii Crystal structure of a conger eel galectin (congerin II) at 1.45 Å resolution: implication for the accelerated evolution of a new ligand-binding site following gene duplication J. Mol. Biol. 321 2002 879 889
    • (2002) J. Mol. Biol. , vol.321 , pp. 879-889
    • Shirai, T.1    Matsui, Y.2    Shionyu-Mitsuyama, C.3    Yamane, T.4    Kamiya, H.5    Ishii, C.6
  • 52
    • 9844267959 scopus 로고    scopus 로고
    • Involvement of laser photo-CIDNP (chemically induced dynamic nuclear polarization)-reactive amino acid side chains in ligand binding by galactoside-specific lectins in solution
    • H.-C. Siebert, R. Adar, R. Arango, M. Burchert, H. Kaltner, and G. Kayser Involvement of laser photo-CIDNP (chemically induced dynamic nuclear polarization)-reactive amino acid side chains in ligand binding by galactoside-specific lectins in solution Eur. J. Biochem. 249 1997 27 38
    • (1997) Eur. J. Biochem. , vol.249 , pp. 27-38
    • Siebert, H.-C.1    Adar, R.2    Arango, R.3    Burchert, M.4    Kaltner, H.5    Kayser, G.6
  • 53
    • 0028275197 scopus 로고
    • Probing hydrogen-bonding interactions of bovine heart galectin-1 and methyl-β-lactoside by use of engineered ligands
    • D. Solís, J. Jiménez-Barbero, M. Martín-Lomas, and T. Díaz-Mauriño Probing hydrogen-bonding interactions of bovine heart galectin-1 and methyl-β-lactoside by use of engineered ligands Eur. J. Biochem. 223 1994 107 114
    • (1994) Eur. J. Biochem. , vol.223 , pp. 107-114
    • Solís, D.1    Jiménez-Barbero, J.2    Martín-Lomas, M.3    Díaz-Mauriño, T.4
  • 54
    • 17544377102 scopus 로고    scopus 로고
    • Different architechture of the combining sites of two chicken galectins revealed by chemical-mapping studies with synthetic ligand derivatives
    • D. Solís, A. Romero, H. Kaltner, H.-J. Gabius, and T. Díaz-Mauriño Different architechture of the combining sites of two chicken galectins revealed by chemical-mapping studies with synthetic ligand derivatives J. Biol. Chem. 271 1996 12744 12748
    • (1996) J. Biol. Chem. , vol.271 , pp. 12744-12748
    • Solís, D.1    Romero, A.2    Kaltner, H.3    Gabius, H.-J.4    Díaz- Mauriño, T.5
  • 56
    • 0026739782 scopus 로고
    • Subunit molecular mass assignment of 14,654 Da to the soluble β-galactoside-binding lectin from bovine heart muscle and demonstration of intramolecular disulfide bonding associated with oxidative inactivation
    • B.M. Tracey, T. Feizi, W.M. Abbott, R.A. Carruthers, B.N. Green, and A.M. Lawson Subunit molecular mass assignment of 14,654 Da to the soluble β-galactoside-binding lectin from bovine heart muscle and demonstration of intramolecular disulfide bonding associated with oxidative inactivation J. Biol. Chem. 267 1992 10342 10347
    • (1992) J. Biol. Chem. , vol.267 , pp. 10342-10347
    • Tracey, B.M.1    Feizi, T.2    Abbott, W.M.3    Carruthers, R.A.4    Green, B.N.5    Lawson, A.M.6
  • 57
    • 0029954457 scopus 로고    scopus 로고
    • Structural and functional characterization of a novel tumor-derived rat galectin-1 having transforming growth factor activity: The relationship between intramolecular disulfide bridges and TGF activity
    • K. Yamaoka, A. Ingendoh, S. Tsubuki, Y. Nagai, and Y. Sanai Structural and functional characterization of a novel tumor-derived rat galectin-1 having transforming growth factor activity: the relationship between intramolecular disulfide bridges and TGF activity J. Biochem. 119 1996 878 886
    • (1996) J. Biochem. , vol.119 , pp. 878-886
    • Yamaoka, K.1    Ingendoh, A.2    Tsubuki, S.3    Nagai, Y.4    Sanai, Y.5
  • 58
    • 0034074288 scopus 로고    scopus 로고
    • Oxidized galectin-1 promotes axonal regeneration in peripheral nerves but does not possess lectin properties
    • Y. Inagaki, Y. Sohma, H. Horie, R. Nozawa, and T. Kadoya Oxidized galectin-1 promotes axonal regeneration in peripheral nerves but does not possess lectin properties Eur. J. Biochem. 267 2000 2955 2964
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2955-2964
    • Inagaki, Y.1    Sohma, Y.2    Horie, H.3    Nozawa, R.4    Kadoya, T.5
  • 59
    • 0001528720 scopus 로고    scopus 로고
    • Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules
    • R. Fraczkiewicz, and W. Braun Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules J. Comp. Chem. 19 1998 319 333
    • (1998) J. Comp. Chem. , vol.19 , pp. 319-333
    • Fraczkiewicz, R.1    Braun, W.2
  • 60
    • 0024356783 scopus 로고
    • Production and purification of a recombinant human 14 kDa beta-galactoside-binding lectin
    • J. Hirabayashi, H. Ayaki, G. Soma, and K.-I. Kasai Production and purification of a recombinant human 14 kDa beta-galactoside-binding lectin FEBS Letters 250 1989 161 165
    • (1989) FEBS Letters , vol.250 , pp. 161-165
    • Hirabayashi, J.1    Ayaki, H.2    Soma, G.3    Kasai, K.-I.4
  • 61
    • 0024382081 scopus 로고
    • Cloning and nucleotide sequence of a full-length cDNA for human 14 kDa beta-galactoside-binding lectin
    • J. Hirabayashi, H. Ayaki, G. Soma, and K.-I. Kasai Cloning and nucleotide sequence of a full-length cDNA for human 14 kDa beta-galactoside-binding lectin Biochim. Biophys. Acta 1008 1989 85 91
    • (1989) Biochim. Biophys. Acta , vol.1008 , pp. 85-91
    • Hirabayashi, J.1    Ayaki, H.2    Soma, G.3    Kasai, K.-I.4
  • 62
    • 0033212815 scopus 로고    scopus 로고
    • Integration of macromolecular diffraction data
    • A.G. Leslie Integration of macromolecular diffraction data Acta Crystallog. sect. A 55 1999 1696 1702
    • (1999) Acta Crystallog. Sect. a , vol.55 , pp. 1696-1702
    • Leslie, A.G.1
  • 63
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project Number 4 The CCP4 suite: programs for protein crystallography Acta Crystallog. sect. D 50 1994 760 763
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 64
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • J. Navaza AMoRe: an automated package for molecular replacement Acta Crystallog. sect. A 50 1994 157 163
    • (1994) Acta Crystallog. Sect. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 67
  • 68
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • T. Wiseman, S. Williston, J.F. Brandts, and L.N. Lin Rapid measurement of binding constants and heats of binding using a new titration calorimeter Anal. Biochem. 179 1989 131 137
    • (1989) Anal. Biochem. , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.N.4
  • 69
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • A. Nicholls, K.A. Sharp, and B. Honig Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons Proteins: Struct. Funct. Genet. 11 1991 281 296
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 70
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • P.J. Kraulis MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallog. 24 1991 946 950
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 71
    • 0027412196 scopus 로고
    • ALSCRIPT, a tool to format multiple sequence alignments
    • G.J. Barton ALSCRIPT, a tool to format multiple sequence alignments Protein Eng. 6 1993 37 40
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 72
    • 0030017889 scopus 로고    scopus 로고
    • Analysis of topological and nontopological structural similarities in the PDB: New examples with old structures
    • N.N. Alexandrov, and D. Fischer Analysis of topological and nontopological structural similarities in the PDB: new examples with old structures Proteins: Struct. Funct. Genet. 25 1996 354 365
    • (1996) Proteins: Struct. Funct. Genet. , vol.25 , pp. 354-365
    • Alexandrov, N.N.1    Fischer, D.2
  • 73
    • 0033119938 scopus 로고    scopus 로고
    • Further additions to MolScript version 1.4, including reading and contouring of electron-density maps
    • R.M. Esnouf Further additions to MolScript version 1.4, including reading and contouring of electron-density maps Acta Crystallog. sect. D 55 1999 938 940
    • (1999) Acta Crystallog. Sect. D , vol.55 , pp. 938-940
    • Esnouf, R.M.1
  • 74
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • B.W. Matthews Solvent content of protein crystals J. Mol. Biol. 33 1968 491 497
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.