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1
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27844470091
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What should be called a lectin?
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Goldstein IJ, Hughes RC, Monsigny M, Osawa T, Sharon N. What should be called a lectin? Nature. 285:1980;66.
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(1980)
Nature
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Goldstein, I.J.1
Hughes, R.C.2
Monsigny, M.3
Osawa, T.4
Sharon, N.5
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2
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0024414280
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Lectins as cell recognition molecules
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Sharon N, Lis H. Lectins as cell recognition molecules. Science. 246:1989;227-234.
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Science
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Sharon, N.1
Lis, H.2
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Lectins, lectin genes, and their role in plant defense
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Chrispeels MJ, Raikhel NV. Lectins, lectin genes, and their role in plant defense. Plant Cell. 3:1991;1-9.
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Chrispeels, M.J.1
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The biochemistry of plant lectins
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Lis H, Sharon N. The biochemistry of plant lectins. Annu Rev Biochem. 42:1973;541-574.
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Annu Rev Biochem
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7
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Use of lectins for the study of membranes
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Sharon N, Lis H. Use of lectins for the study of membranes. Methods Membr Biol. 3:1975;147-200.
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Methods Membr Biol
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Lis, H.2
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8
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Lectins as molecules and as tools
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Lis H, Sharon N. Lectins as molecules and as tools. Annu Rev Biochem. 53:1986;35-67.
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Annu Rev Biochem
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Lis, H.1
Sharon, N.2
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0002199711
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Isolation, physiochemical characterization and carbohydrate-binding specificity of lectins
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E.E. Liener, N. Sharon, Goldstein I.J. London/Orlando: Academic Press
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Goldstein IJ, Poretz RD. Isolation, physiochemical characterization and carbohydrate-binding specificity of lectins. Liener EE, Sharon N, Goldstein IJ. The Lectins, Properties, Function, and Application in Biology and Medicine. 1986;35-247 Academic Press, London/Orlando.
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The Lectins, Properties, Function, and Application in Biology and Medicine
, pp. 35-247
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Goldstein, I.J.1
Poretz, R.D.2
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10
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0027078720
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Analysis of sequence variation among legume lectins. A ring of hypervariable residues forms the perimeter of the carbohydrate binding site
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Young NM, Oomen RP. Analysis of sequence variation among legume lectins. A ring of hypervariable residues forms the perimeter of the carbohydrate binding site. J Mol Biol. 228:1992;924-934.
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J Mol Biol
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Young, N.M.1
Oomen, R.P.2
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11
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0025222989
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Legume lectins - A large family of homologous proteins
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Sharon N, Lis H. Legume lectins - a large family of homologous proteins. FASEB J. 4:1990;3198-3208.
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(1990)
FASEB J
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, pp. 3198-3208
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Sharon, N.1
Lis, H.2
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14
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0028588086
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Structural analysis of two crystal forms of lentil lectin at 1.8 Å resolution
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Loris R, Van Overberge D, Dao-Thi M-H, Poortmans F, Maene N, Wyns L. Structural analysis of two crystal forms of lentil lectin at 1.8 Å resolution. Proteins. 20:1994;330-346.
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(1994)
Proteins
, vol.20
, pp. 330-346
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Loris, R.1
Van Overberge, D.2
Dao-Thi, M.-H.3
Poortmans, F.4
Maene, N.5
Wyns, L.6
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15
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0028921961
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X-ray crystal structure of soybean agglutinin cross-linked with a biantennary analog of the blood group I carbohydrate antigen
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Dessen A, Gupta D, Sabesan S, Brewer CF, Sacchettini JC. X-ray crystal structure of soybean agglutinin cross-linked with a biantennary analog of the blood group I carbohydrate antigen. Biochemistry. 34:1995;4933-4942.
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Biochemistry
, vol.34
, pp. 4933-4942
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Dessen, A.1
Gupta, D.2
Sabesan, S.3
Brewer, C.F.4
Sacchettini, J.C.5
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16
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0027979382
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Crystal structure of peanut lectin, a protein with an unusual quaternary structure
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Banerjee R, Mande SC, Ganesh V, Das K, Dhanaraj V, Mahanta SK, Suguna L, Surolia A, Vijayan M. Crystal structure of peanut lectin, a protein with an unusual quaternary structure. Proc Natl Acad Sci USA. 91:1994;227-231.
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(1994)
Proc Natl Acad Sci USA
, vol.91
, pp. 227-231
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Banerjee, R.1
Mande, S.C.2
Ganesh, V.3
Das, K.4
Dhanaraj, V.5
Mahanta, S.K.6
Suguna, L.7
Surolia, A.8
Vijayan, M.9
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17
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0029997826
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Conformation, protein - carbohydrate interactions and a novel subunit association in the refined structure of peanut lectin - lactose complex
-
A detailed analysis is presented of the secondary and quaternary structural properties of peanut lectin in comparison with other legume lectins. The peanut agglutinin tetramer does not obey 222 symmetry. Each dimer has its own pseudotwofold axis. The dimer interfaces are a back-to-back sandwich of the six-stranded β sheets. Sugar-binding contacts are similar to those found in other legume lectins and explain the specificity for galactose. of special interest
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Banerjee R, Das K, Ravishankar R, Suguna K, Surolia A, Vijayan M. Conformation, protein - carbohydrate interactions and a novel subunit association in the refined structure of peanut lectin - lactose complex. J Mol Biol. 259:1996;281-296 A detailed analysis is presented of the secondary and quaternary structural properties of peanut lectin in comparison with other legume lectins. The peanut agglutinin tetramer does not obey 222 symmetry. Each dimer has its own pseudotwofold axis. The dimer interfaces are a back-to-back sandwich of the six-stranded β sheets. Sugar-binding contacts are similar to those found in other legume lectins and explain the specificity for galactose. of special interest.
-
(1996)
J Mol Biol
, vol.259
, pp. 281-296
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-
Banerjee, R.1
Das, K.2
Ravishankar, R.3
Suguna, K.4
Surolia, A.5
Vijayan, M.6
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18
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0029786409
-
The crystallographic structure of phytohemagglutinin-L
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The crystal structure is determined at 2.8 Å resolution using lentil lectin as molecular replacement model. Phytohemagglutinin-L is a glycoprotein with two glycosylation sites. The 222 tetramer, contained within the C2 asymmetric unit, consists of two canonical concanavalin A-type dimers. These dimers associate forming a tetrameric structure different from that of concanavalin A. This lectin binds adenine in addition to oligosaccharides (most specific for Galβ1-4GlcNAcβ1-2[Galβ1-4GlcNAcβ1-6]Man). Comparisons are made with the protein transthyretin (prealbumin). of special interest
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Hamelryck TW, Dao-Thi M-H, Poortmans F, Chrispeels MJ, Wyns L, Loris R. The crystallographic structure of phytohemagglutinin-L. J Biol Chem. 271:1996;20479-20485 The crystal structure is determined at 2.8 Å resolution using lentil lectin as molecular replacement model. Phytohemagglutinin-L is a glycoprotein with two glycosylation sites. The 222 tetramer, contained within the C2 asymmetric unit, consists of two canonical concanavalin A-type dimers. These dimers associate forming a tetrameric structure different from that of concanavalin A. This lectin binds adenine in addition to oligosaccharides (most specific for Galβ1-4GlcNAcβ1-2[Galβ1-4GlcNAcβ1-6]Man). Comparisons are made with the protein transthyretin (prealbumin). of special interest.
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(1996)
J Biol Chem
, vol.271
, pp. 20479-20485
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-
Hamelryck, T.W.1
Dao-Thi, M.-H.2
Poortmans, F.3
Chrispeels, M.J.4
Wyns, L.5
Loris, R.6
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19
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0031588904
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Analyses of carbohydrate recognition by legume lectins: Size of the combining site loops and their primary specificity
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The sugar-binding sites of five mannose/glucose-specific legume lectins (concanavalin A, pea lectin, favin, lentil lectin and Lol I) and four galactose-specific legume lectins (ECorL, soybean lectin, peanut lectina and GSA IV) are analyzed to explain their specificities. Differences are found mainly in the length and orientation of loop regions that provide the framework of the binding site. of special interest
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Sharma V, Surolia A. Analyses of carbohydrate recognition by legume lectins: size of the combining site loops and their primary specificity. J Mol Biol. 267:1997;433-445 The sugar-binding sites of five mannose/glucose-specific legume lectins (concanavalin A, pea lectin, favin, lentil lectin and Lol I) and four galactose-specific legume lectins (ECorL, soybean lectin, peanut lectina and GSA IV) are analyzed to explain their specificities. Differences are found mainly in the length and orientation of loop regions that provide the framework of the binding site. of special interest.
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(1997)
J Mol Biol
, vol.267
, pp. 433-445
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Sharma, V.1
Surolia, A.2
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20
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0025721792
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Evolution of a family of N-acetylglucosamine binding proteins containing the disulfide-rich domain of wheat germ agglutinin
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Wright HT, Sandrasegaram G, Wright CS. Evolution of a family of N-acetylglucosamine binding proteins containing the disulfide-rich domain of wheat germ agglutinin. J Mol Evol. 33:1991;283-294.
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(1991)
J Mol Evol
, vol.33
, pp. 283-294
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Wright, H.T.1
Sandrasegaram, G.2
Wright, C.S.3
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21
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0003116043
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The mannose-binding monocot lectins and their genes
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A. Pusztai, Bardocz S. London: Taylor and Francis
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Van Damme EJM, Smeets K, Peumans WJ. The mannose-binding monocot lectins and their genes. Pusztai A, Bardocz S. Lectins, Biomedical Perspective. 1995;59-80 Taylor and Francis, London.
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(1995)
Lectins, Biomedical Perspective
, pp. 59-80
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Van Damme, E.J.M.1
Smeets, K.2
Peumans, W.J.3
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22
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44949278767
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A comparative study of mannose-binding lectins from the Amaryllidaceae and Alliaceae
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Van Damme EJM, Goldstein IJ, Peumans WJ. A comparative study of mannose-binding lectins from the Amaryllidaceae and Alliaceae. Phytochemistry. 30:1991;509-514.
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(1991)
Phytochemistry
, vol.30
, pp. 509-514
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Van Damme, E.J.M.1
Goldstein, I.J.2
Peumans, W.J.3
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23
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0025937103
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Biosynthesis, primary structure and molecular cloning of snowdrop (Galanthus nivalis) lectin
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Van Damme EJM, Kaku H, Perini F, Goldstein IJ, Peeters B, Yagi F, Decock B, Peumans WJ. Biosynthesis, primary structure and molecular cloning of snowdrop (Galanthus nivalis) lectin. Eur J Biochem. 202:1991;23-30.
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(1991)
Eur J Biochem
, vol.202
, pp. 23-30
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Van Damme, E.J.M.1
Kaku, H.2
Perini, F.3
Goldstein, I.J.4
Peeters, B.5
Yagi, F.6
Decock, B.7
Peumans, W.J.8
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24
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0028355084
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Characterization and molecular cloning of mannose-binding lectins of the Orchidaceae species Listera ovata, Epipactis belleborine and Cymbidium hybrid
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Van Damme EJM, Smeets K, Torrekens S, Van Leuven F, Peumans WJ. Characterization and molecular cloning of mannose-binding lectins of the Orchidaceae species Listera ovata, Epipactis belleborine and Cymbidium hybrid. Eur J Biochem. 93:1993;769-777.
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Eur J Biochem
, vol.93
, pp. 769-777
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Van Damme, E.J.M.1
Smeets, K.2
Torrekens, S.3
Van Leuven, F.4
Peumans, W.J.5
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25
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84989666997
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Lectins of members of the Amaryllidaceae are encoded by multigene families which show extensive homology
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Van Damme EJM, Goldstein IJ, Vercammen G, Vuylsteke J, Peumans WJ. Lectins of members of the Amaryllidaceae are encoded by multigene families which show extensive homology. Physiol Plant. 86:1992;245-252.
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(1992)
Physiol Plant
, vol.86
, pp. 245-252
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Van Damme, E.J.M.1
Goldstein, I.J.2
Vercammen, G.3
Vuylsteke, J.4
Peumans, W.J.5
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26
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0028358720
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Lectin effects on HIV-1 infectivity
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Hammaar L, Hirsch I, Machado A, De Mareuil J, Baillon J, Chermann JC. Lectin effects on HIV-1 infectivity. Ann New York Acad Sci. 724:1994;166-169.
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(1994)
Ann New York Acad Sci
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, pp. 166-169
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Hammaar, L.1
Hirsch, I.2
Machado, A.3
De Mareuil, J.4
Baillon, J.5
Chermann, J.C.6
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27
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0029008975
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Structure of mannose-specific Snowdrop (Galanthus nivalis) lectin is representative of a new plant lectin Family
-
Hester G, Kaku H, Goldstein IJ, Wright CS. Structure of mannose-specific Snowdrop (Galanthus nivalis) lectin is representative of a new plant lectin Family. Nat Struct Biol. 2:1995;472-479.
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(1995)
Nat Struct Biol
, vol.2
, pp. 472-479
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Hester, G.1
Kaku, H.2
Goldstein, I.J.3
Wright, C.S.4
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28
-
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0030568976
-
The mannose-specific bulb lectin from Galanthus nivalis (snowdrop) binds mono- And dimannosides at distinct sites. Structure analysis of refined complexes at 2.3 and 3.0 Å resolution
-
13). Unusual features include one of the independent subunits being much less ordered than the second one, and the dimannoside molecule mediating all crucial lattice contacts. It binds with highest occupancy at site 3 (subdomain 3) where the reducing mannose is positioned in the conserved binding pocket. of outstanding interest
-
13). Unusual features include one of the independent subunits being much less ordered than the second one, and the dimannoside molecule mediating all crucial lattice contacts. It binds with highest occupancy at site 3 (subdomain 3) where the reducing mannose is positioned in the conserved binding pocket. of outstanding interest.
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(1996)
J Mol Biol
, vol.262
, pp. 516-531
-
-
Hester, G.1
Wright, C.S.2
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29
-
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0029658497
-
The 2.0 Å structure of a cross-linked complex between snowdrop lectin and a branched mannopentaose: Evidence for two unique binding modes
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122). The structure illustrates how large branched oligosaccharides can form supermolecular structures consistent with the crystal symmetry by forming crossbridges between neighboring lectin molecules in the lattice. The mannopentaose binds with high occupancy at two of the binding sites in each subunit. One of these (site 1) has a preference for nonreducing terminal Man and is involved in crossbridge formation, whereas the second one (site 3) is extended and accommodates the whole outer tri-mannose arm of the oligosaccharide. of outstanding interest
-
122). The structure illustrates how large branched oligosaccharides can form supermolecular structures consistent with the crystal symmetry by forming crossbridges between neighboring lectin molecules in the lattice. The mannopentaose binds with high occupancy at two of the binding sites in each subunit. One of these (site 1) has a preference for nonreducing terminal Man and is involved in crossbridge formation, whereas the second one (site 3) is extended and accommodates the whole outer tri-mannose arm of the oligosaccharide. of outstanding interest.
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(1996)
Structure
, vol.4
, pp. 1339-1352
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Wright, C.S.1
Hester, G.2
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30
-
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0030499408
-
X-ray structure solution of Amaryllis lectin by molecular replacement with only 4% of the total diffracting matter
-
α coordinates of snowdrop lectin as the molecular replacement search model (85% homology). The structure is in good agreement with that of GNA except that eight residues are missing at the C-terminal end. of outstanding interest
-
α coordinates of snowdrop lectin as the molecular replacement search model (85% homology). The structure is in good agreement with that of GNA except that eight residues are missing at the C-terminal end. of outstanding interest.
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(1996)
Acta Crystallogr D
, vol.52
, pp. 1146-1152
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-
Chantalat, L.1
Wood, S.D.2
Rizkallah, P.3
Reynolds, C.D.4
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31
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0030477903
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Purification, crystallization and preliminary X-ray analysis of a mannose-binding lectin from bluebell (Scilla campanulata) bulbs
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Wright LM, Wood SD, Reynolds CD, Rizkallah PJ, Peumans WJ, Van Damme EJM, Allen AK. Purification, crystallization and preliminary X-ray analysis of a mannose-binding lectin from bluebell (Scilla campanulata) bulbs. Acta Crystallogr D. 52:1996;1021-1023.
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(1996)
Acta Crystallogr D
, vol.52
, pp. 1021-1023
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Wright, L.M.1
Wood, S.D.2
Reynolds, C.D.3
Rizkallah, P.J.4
Peumans, W.J.5
Van Damme, E.J.M.6
Allen, A.K.7
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32
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0028298498
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The composition and properties of jacalin, a lectin of diverse applications obtained from jackfruit (Artocarpus heterophyllus) seeds
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Kabir S, Daar AS. The composition and properties of jacalin, a lectin of diverse applications obtained from jackfruit (Artocarpus heterophyllus) seeds. Immunol Invest. 23:1994;167-188.
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(1994)
Immunol Invest
, vol.23
, pp. 167-188
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Kabir, S.1
Daar, A.S.2
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33
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0029941757
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A novel mode of carbohydrate recognition in jacalin, a Moraceae plant lectin with a β-prism fold
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522) of jacalin (two tetramers per asymmetric unit) complexed with Me-α-D-Gal is determined at 2.4 Å resolution by multiple isomorphous replacement techniques. Each subunit consists of an α chain (133 residues) and a short β chain (20 residues), as a result of proteolysis. Interesting structural features discussed are that the β-prism fold is a new structural fold for plant lectins and representative of all Moraceae lectins. The single binding site per subunit is located at the entrance of the prism fold and has an unusual structure in that the N-terminal amino group of the α chain interacts directly with bound MeGal. of outstanding interest
-
522) of jacalin (two tetramers per asymmetric unit) complexed with Me-α-D-Gal is determined at 2.4 Å resolution by multiple isomorphous replacement techniques. Each subunit consists of an α chain (133 residues) and a short β chain (20 residues), as a result of proteolysis. Interesting structural features discussed are that the β-prism fold is a new structural fold for plant lectins and representative of all Moraceae lectins. The single binding site per subunit is located at the entrance of the prism fold and has an unusual structure in that the N-terminal amino group of the α chain interacts directly with bound MeGal. of outstanding interest.
-
(1996)
Nat Struct Biol
, vol.3
, pp. 596-603
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Sankaranarayanan, R.1
Sekar, K.2
Banerjee, R.3
Sharma, V.4
Surolia, A.5
Vijayan, M.6
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34
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0024820574
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Crystallization and preliminary X-ray diffraction studies of the complex of Maclura pomifera agglutinin with the disaccharide Gal-β1,3-GalNac.
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Lee X, Johnston R, Rose DR, Young MN. Crystallization and preliminary X-ray diffraction studies of the complex of Maclura pomifera agglutinin with the disaccharide Gal-β1,3-GalNac. J Mol Biol. 210:1989;685-686.
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(1989)
J Mol Biol
, vol.210
, pp. 685-686
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Lee, X.1
Johnston, R.2
Rose, D.R.3
Young, M.N.4
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35
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0026050639
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Crystal structure of insecticidal δ-endotoxin from Bacillus thuringiensis at 2.5 Å resolution
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Li J, Carroll J, Ellar DJ. Crystal structure of insecticidal δ-endotoxin from Bacillus thuringiensis at 2.5 Å resolution. Nature. 353:1991;815-821.
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(1991)
Nature
, vol.353
, pp. 815-821
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Li, J.1
Carroll, J.2
Ellar, D.J.3
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36
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0028297019
-
Crystal structure of vitelline membrane outer layer protein I (VMO-I): A folding motif with homologous Greek key structures related by an internal three-fold symmetry
-
Shimizu T, Vassylyev DG, Kido S, Doi Y, Morikawa K. Crystal structure of vitelline membrane outer layer protein I (VMO-I): a folding motif with homologous Greek key structures related by an internal three-fold symmetry. EMBO J. 13:1994;1003-1010.
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EMBO J
, vol.13
, pp. 1003-1010
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Shimizu, T.1
Vassylyev, D.G.2
Kido, S.3
Doi, Y.4
Morikawa, K.5
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37
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0025245801
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Physicochemical properties of amaranthin, the Lectin from Amaranthus caudatus seeds
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Rinderle SJ, Goldstein IJ, Remsen EE. Physicochemical properties of amaranthin, the Lectin from Amaranthus caudatus seeds. Biochemistry. 29:1990;10555-10561.
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(1990)
Biochemistry
, vol.29
, pp. 10555-10561
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Rinderle, S.J.1
Goldstein, I.J.2
Remsen, E.E.3
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38
-
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0031252619
-
Amaranthus lectin structure at 2.2 Å reveals T-antigen disaccharide bound to β-trefoil domains
-
The 2.2 Å structure is determined using multiple isomorphous replacement methods. This is the first crystal structure of a T-antigen - lectin complex. The subunit consists of two β-trefoil domains which dimerize via an extensive interface. The two T-antigen-binding sites are located in this interface at equivalent twofold related positions. Both sugar residues (Gal and GalNAc) are in intimate contact with the protein surface. The structural fold is compared with those of other β-trefoil proteins (ricin and fibroblast growth factor). of outstanding interest
-
Transue TR, Smith AK, Mo H, Goldstein IJ, Saper MA. Amaranthus lectin structure at 2.2 Å reveals T-antigen disaccharide bound to β-trefoil domains. Nat Struct Biol. 4:1997; The 2.2 Å structure is determined using multiple isomorphous replacement methods. This is the first crystal structure of a T-antigen - lectin complex. The subunit consists of two β-trefoil domains which dimerize via an extensive interface. The two T-antigen-binding sites are located in this interface at equivalent twofold related positions. Both sugar residues (Gal and GalNAc) are in intimate contact with the protein surface. The structural fold is compared with those of other β-trefoil proteins (ricin and fibroblast growth factor). of outstanding interest.
-
(1997)
Nat Struct Biol
, vol.4
-
-
Transue, T.R.1
Smith, A.K.2
Mo, H.3
Goldstein, I.J.4
Saper, M.A.5
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39
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0030035805
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3 domain: A flexible lectin scaffold
-
The β-trefoil folding motif is predicted for 45 carbohydrate-binding proteins on the basis of amino acid sequence database searches. The QxW tripeptide, first observed in the ricin B-chain, appears to be a characteristic sequence present in each of the subdomains of this protein fold. For the identification of more distantly related proteins, the Hidden Markov model is used. of special interest
-
3 domain: a flexible lectin scaffold. Protein Sci. 5:1996;1490-1501 The β-trefoil folding motif is predicted for 45 carbohydrate-binding proteins on the basis of amino acid sequence database searches. The QxW tripeptide, first observed in the ricin B-chain, appears to be a characteristic sequence present in each of the subdomains of this protein fold. For the identification of more distantly related proteins, the Hidden Markov model is used. of special interest.
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(1996)
Protein Sci
, vol.5
, pp. 1490-1501
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Hazes, B.1
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40
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0026556882
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β-trefoil fold: Patterns of structure and sequence in the Kunitz inhibitors, interleukins-1-β And 1-α, and fibroblast growth factors
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Murzin AG, Lesk AM, Chothia C. β-trefoil fold: patterns of structure and sequence in the Kunitz inhibitors, interleukins-1-β and 1-α, and fibroblast growth factors. J Mol Biol. 223:1992;531-543.
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(1992)
J Mol Biol
, vol.223
, pp. 531-543
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Murzin, A.G.1
Lesk, A.M.2
Chothia, C.3
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41
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0025939115
-
Structure of ricin B-chain at 2.5 Å resolution
-
Rutenber E, Robertus JD. Structure of ricin B-chain at 2.5 Å resolution. Proteins. 10:1991;260-269.
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(1991)
Proteins
, vol.10
, pp. 260-269
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Rutenber, E.1
Robertus, J.D.2
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42
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0029114697
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Crystal structure of abrin-a at 2.14 Å
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Tahirow TH, Lu T-H, Liaw Y-C, Chen Y-L, Lin J-Y. Crystal structure of abrin-a at 2.14 Å J Mol Biol. 250:1995;354-367.
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J Mol Biol
, vol.250
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Tahirow, T.H.1
Lu, T.-H.2
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