Literature references that cite this PDB file's
key reference
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PubMed id
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Reference
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G.R.Vasta
(2009).
Roles of galectins in infection.
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Nat Rev Microbiol, 7,
424-438.
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H.Ahmed,
S.J.Du,
and
G.R.Vasta
(2009).
Knockdown of a galectin-1-like protein in zebrafish (Danio rerio) causes defects in skeletal muscle development.
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Glycoconj J, 26,
277-283.
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M.C.Miller,
I.V.Nesmelova,
D.Platt,
A.Klyosov,
and
K.H.Mayo
(2009).
The carbohydrate-binding domain on galectin-1 is more extensive for a complex glycan than for simple saccharides: implications for galectin-glycan interactions at the cell surface.
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Biochem J, 421,
211-221.
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R.D.Cummings
(2009).
The repertoire of glycan determinants in the human glycome.
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Mol Biosyst, 5,
1087-1104.
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D.Zhou,
H.Ge,
J.Sun,
Y.Gao,
M.Teng,
and
L.Niu
(2008).
Crystal structure of the C-terminal conserved domain of human GRP, a galectin-related protein, reveals a function mode different from those of galectins.
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Proteins, 71,
1582-1588.
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PDB code:
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E.M.Rapoport,
O.V.Kurmyshkina,
and
N.V.Bovin
(2008).
Mammalian galectins: structure, carbohydrate specificity, and functions.
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Biochemistry (Mosc), 73,
393-405.
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L.A.Earl,
and
L.G.Baum
(2008).
CD45 glycosylation controls T-cell life and death.
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Immunol Cell Biol, 86,
608-615.
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M.A.Wälti,
S.Thore,
M.Aebi,
and
M.Künzler
(2008).
Crystal structure of the putative carbohydrate recognition domain of human galectin-related protein.
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Proteins, 72,
804-808.
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PDB code:
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M.Tamura,
K.Kasai,
T.Itagaki,
T.Nonaka,
and
Y.Arata
(2008).
Identification of a second, non-conserved amino acid that contributes to the unique sugar binding properties of the nematode galectin LEC-1.
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Biol Pharm Bull, 31,
1254-1257.
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S.Bi,
L.A.Earl,
L.Jacobs,
and
L.G.Baum
(2008).
Structural features of galectin-9 and galectin-1 that determine distinct T cell death pathways.
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J Biol Chem, 283,
12248-12258.
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Y.Arata,
N.Ishii,
M.Tamura,
T.Nonaka,
and
K.Kasai
(2007).
Identification of the amino acid residue in the nematode galectin LEC-1 responsible for its unique sugar binding property: analysis by combination of site-directed mutagenesis and frontal affinity chromatography.
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Biol Pharm Bull, 30,
2012-2017.
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T.Shirai,
C.Shionyu-Mitsuyama,
T.Ogawa,
and
K.Muramoto
(2006).
Structure based studies of the adaptive diversification process of congerins.
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Mol Divers, 10,
567-573.
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M.S.Sujatha,
and
P.V.Balaji
(2004).
Identification of common structural features of binding sites in galactose-specific proteins.
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Proteins, 55,
44-65.
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N.G.Than,
E.Pick,
S.Bellyei,
A.Szigeti,
O.Burger,
Z.Berente,
T.Janaky,
A.Boronkai,
H.Kliman,
H.Meiri,
H.Bohn,
G.N.Than,
and
B.Sumegi
(2004).
Functional analyses of placental protein 13/galectin-13.
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Eur J Biochem, 271,
1065-1078.
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D.D.Leonidas,
B.M.Swamy,
A.G.Bhat,
S.R.Inamdar,
M.N.Kosmopoulou,
E.D.Chrysina,
and
N.G.Oikonomakos
(2003).
Crystallization and preliminary X-ray crystallographic analysis of Sclerotium rolfsii lectin.
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Acta Crystallogr D Biol Crystallogr, 59,
363-365.
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L.He,
S.André,
H.C.Siebert,
H.Helmholz,
B.Niemeyer,
and
H.J.Gabius
(2003).
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.
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Biophys J, 85,
511-524.
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M.G.Ford,
T.Weimar,
T.Köhli,
and
R.J.Woods
(2003).
Molecular dynamics simulations of galectin-1-oligosaccharide complexes reveal the molecular basis for ligand diversity.
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Proteins, 53,
229-240.
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J.S.Richardson,
and
D.C.Richardson
(2002).
Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation.
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Proc Natl Acad Sci U S A, 99,
2754-2759.
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K.Scott,
and
J.Zhang
(2002).
Partial identification by site-directed mutagenesis of a cell growth inhibitory site on the human galectin-1 molecule.
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BMC Cell Biol, 3,
3.
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H.Ponstingl,
K.Henrick,
and
J.M.Thornton
(2000).
Discriminating between homodimeric and monomeric proteins in the crystalline state.
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Proteins, 41,
47-57.
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H.Zhang,
K.Huang,
Z.Li,
L.Banerjei,
K.E.Fisher,
N.V.Grishin,
E.Eisenstein,
and
O.Herzberg
(2000).
Crystal structure of YbaK protein from Haemophilus influenzae (HI1434) at 1.8 A resolution: functional implications.
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Proteins, 40,
86-97.
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PDB codes:
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M.A.Bianchet,
H.Ahmed,
G.R.Vasta,
and
L.M.Amzel
(2000).
Soluble beta-galactosyl-binding lectin (galectin) from toad ovary: crystallographic studies of two protein-sugar complexes.
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Proteins, 40,
378-388.
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PDB codes:
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E.García-Hernández,
and
A.Hernández-Arana
(1999).
Structural bases of lectin-carbohydrate affinities: comparison with protein-folding energetics.
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Protein Sci, 8,
1075-1086.
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M.M.Prabu,
K.Suguna,
and
M.Vijayan
(1999).
Variability in quaternary association of proteins with the same tertiary fold: a case study and rationalization involving legume lectins.
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Proteins, 35,
58-69.
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D.D.Leonidas,
E.H.Vatzaki,
H.Vorum,
J.E.Celis,
P.Madsen,
and
K.R.Acharya
(1998).
Structural basis for the recognition of carbohydrates by human galectin-7.
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Biochemistry, 37,
13930-13940.
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PDB codes:
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F.P.Schwarz,
H.Ahmed,
M.A.Bianchet,
L.M.Amzel,
and
G.R.Vasta
(1998).
Thermodynamics of bovine spleen galectin-1 binding to disaccharides: correlation with structure and its effect on oligomerization at the denaturation temperature.
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Biochemistry, 37,
5867-5877.
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R.Y.Yang,
P.N.Hill,
D.K.Hsu,
and
F.T.Liu
(1998).
Role of the carboxyl-terminal lectin domain in self-association of galectin-3.
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Biochemistry, 37,
4086-4092.
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A.Vyakarnam,
S.F.Dagher,
J.L.Wang,
and
R.J.Patterson
(1997).
Evidence for a role for galectin-1 in pre-mRNA splicing.
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Mol Cell Biol, 17,
4730-4737.
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H.C.Siebert,
R.Adar,
R.Arango,
M.Burchert,
H.Kaltner,
G.Kayser,
E.Tajkhorshid,
C.W.von der Lieth,
R.Kaptein,
N.Sharon,
J.F.Vliegenthart,
and
H.J.Gabius
(1997).
Involvement of laser photo-CIDNP (chemically induced dynamic nuclear polarization)-reactive amino acid side chains in ligand binding by galactoside-specific lectins in solution.
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Eur J Biochem, 249,
27-38.
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H.J.Gabius
(1997).
Animal lectins.
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Eur J Biochem, 243,
543-576.
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T.C.Umland,
L.M.Wingert,
S.Swaminathan,
W.F.Furey,
J.J.Schmidt,
and
M.Sax
(1997).
Structure of the receptor binding fragment HC of tetanus neurotoxin.
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Nat Struct Biol, 4,
788-792.
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PDB code:
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M.Cho,
and
R.D.Cummings
(1996).
Characterization of monomeric forms of galectin-1 generated by site-directed mutagenesis.
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Biochemistry, 35,
13081-13088.
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M.Muraki,
K.Harata,
N.Sugita,
and
K.Sato
(1996).
Origin of carbohydrate recognition specificity of human lysozyme revealed by affinity labeling.
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Biochemistry, 35,
13562-13567.
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PDB codes:
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P.E.Johnson,
M.D.Joshi,
P.Tomme,
D.G.Kilburn,
and
L.P.McIntosh
(1996).
Structure of the N-terminal cellulose-binding domain of Cellulomonas fimi CenC determined by nuclear magnetic resonance spectroscopy.
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Biochemistry, 35,
14381-14394.
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PDB codes:
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R.Adar,
and
N.Sharon
(1996).
Mutational studies of the amino acid residues in the combining site of Erythrina corallodendron lectin.
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Eur J Biochem, 239,
668-674.
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S.Rosén,
M.Kata,
Y.Persson,
P.H.Lipniunas,
M.Wikström,
M.J.Van Den Hondel,
J.Van Den Brink,
L.Rask,
L.O.Hedén,
and
A.Tunlid
(1996).
Molecular characterization of a saline-soluble lectin from a parasitic fungus. Extensive sequence similarities between fungal lectins.
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Eur J Biochem, 238,
822-829.
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T.L.Blundell,
and
N.Srinivasan
(1996).
Symmetry, stability, and dynamics of multidomain and multicomponent protein systems.
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Proc Natl Acad Sci U S A, 93,
14243-14248.
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L.G.Baum,
M.Pang,
N.L.Perillo,
T.Wu,
A.Delegeane,
C.H.Uittenbogaart,
M.Fukuda,
and
J.J.Seilhamer
(1995).
Human thymic epithelial cells express an endogenous lectin, galectin-1, which binds to core 2 O-glycans on thymocytes and T lymphoblastoid cells.
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J Exp Med, 181,
877-887.
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M.Menéndez,
M.Gasset,
J.Laynez,
C.López-Zumel,
P.Usobiaga,
E.Töpfer-Petersen,
and
J.J.Calvete
(1995).
Analysis of the structural organization and thermal stability of two spermadhesins. Calorimetric, circular dichroic and Fourier-transform infrared spectroscopic studies.
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Eur J Biochem, 234,
887-896.
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H.J.Hoppe,
and
K.B.Reid
(1994).
Collectins--soluble proteins containing collagenous regions and lectin domains--and their roles in innate immunity.
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Protein Sci, 3,
1143-1158.
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L.Holm,
and
C.Sander
(1994).
Searching protein structure databases has come of age.
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Proteins, 19,
165-173.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
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Where a reference describes a PDB structure, the PDB
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shown on the right.
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