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1
A carbohydrate domain common to both sialyl Le(a) and sialyl Le(X) is recognized by the endothelial cell leukocyte adhesion molecule ELAM-1
A carbohydrate domain common to both sialyl Le(a) and sialyl Le(X) is recognized by the endothelial cell leukocyte adhesion molecule ELAM-1
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A carbohydrate domain common to both sialyl Le(a) and sialyl Le(X) is recognized by the endothelial cell leukocyte adhesion molecule ELAM-1

Berg, E L ; Robinson, M K ; Mansson, O ; Butcher, E C ; Magnani, J L

The Journal of biological chemistry, 1991-08, Vol.266 (23), p.14869-14872 [Periódico revisado por pares]

United States: American Society for Biochemistry and Molecular Biology

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2
Characterization of a series of novel fucose-containing glycosphingolipid immunogens from eggs of Schistosoma mansoni
Characterization of a series of novel fucose-containing glycosphingolipid immunogens from eggs of Schistosoma mansoni
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Characterization of a series of novel fucose-containing glycosphingolipid immunogens from eggs of Schistosoma mansoni

LEVERY, SB ; WEISS, JB ; SALYAN, MEK ; ROBERTS, CE ; HAKOMORI, S ; MAGNANI, JL ; STRAND, M

The Journal of biological chemistry, 1992-03, Vol.267 (8), p.5542-5551 [Periódico revisado por pares]

ROCKVILLE: American Society for Biochemistry and Molecular Biology

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3
A monoclonal antibody-defined antigen associated with gastrointestinal cancer is a ganglioside containing sialylated lacto-N-fucopentaose II
A monoclonal antibody-defined antigen associated with gastrointestinal cancer is a ganglioside containing sialylated lacto-N-fucopentaose II
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A monoclonal antibody-defined antigen associated with gastrointestinal cancer is a ganglioside containing sialylated lacto-N-fucopentaose II

Magnani, J L ; Nilsson, B ; Brockhaus, M ; Zopf, D ; Steplewski, Z ; Koprowski, H ; Ginsburg, V

The Journal of biological chemistry, 1982-12, Vol.257 (23), p.14365-14369 [Periódico revisado por pares]

United States: Elsevier Inc

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4
Monoclonal antibodies directed against the human Leb blood group antigen
Monoclonal antibodies directed against the human Leb blood group antigen
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Monoclonal antibodies directed against the human Leb blood group antigen

Brockhaus, M ; Magnani, J L ; Blaszczyk, M ; Steplewski, Z ; Koprowski, H ; Karlsson, K A ; Larson, G ; Ginsburg, V

The Journal of biological chemistry, 1981-12, Vol.256 (24), p.13223-13225 [Periódico revisado por pares]

United States: American Society for Biochemistry and Molecular Biology

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5
A monoclonal antibody that precipitates the glycoprotein receptor for epidermal growth factor is directed against the human blood group H type 1 antigen
A monoclonal antibody that precipitates the glycoprotein receptor for epidermal growth factor is directed against the human blood group H type 1 antigen
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A monoclonal antibody that precipitates the glycoprotein receptor for epidermal growth factor is directed against the human blood group H type 1 antigen

Fredman, P ; Richert, N D ; Magnani, J L ; Willingham, M C ; Pastan, I ; Ginsburg, V

The Journal of biological chemistry, 1983-09, Vol.258 (18), p.11206-11210 [Periódico revisado por pares]

Bethesda, MD: Elsevier Inc

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6
Monoclonal antibody 18B8, which detects synapse-associated antigens, binds to ganglioside GT3 (II3 (NeuAc)3LacCer)
Monoclonal antibody 18B8, which detects synapse-associated antigens, binds to ganglioside GT3 (II3 (NeuAc)3LacCer)
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Monoclonal antibody 18B8, which detects synapse-associated antigens, binds to ganglioside GT3 (II3 (NeuAc)3LacCer)

Dubois, C ; Magnani, J L ; Grunwald, G B ; Spitalnik, S L ; Trisler, G D ; Nirenberg, M ; Ginsburg, V

The Journal of biological chemistry, 1986-03, Vol.261 (8), p.3826-3830 [Periódico revisado por pares]

Bethesda, MD: Elsevier Inc

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7
Monoclonal antibody Leo Mel 3, which inhibits killing of human melanoma cells by anomalous killer cells, binds to a sugar sequence in GD2 (II3(NeuAc)2-GgOse3Cer) and several other gangliosides
Monoclonal antibody Leo Mel 3, which inhibits killing of human melanoma cells by anomalous killer cells, binds to a sugar sequence in GD2 (II3(NeuAc)2-GgOse3Cer) and several other gangliosides
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Monoclonal antibody Leo Mel 3, which inhibits killing of human melanoma cells by anomalous killer cells, binds to a sugar sequence in GD2 (II3(NeuAc)2-GgOse3Cer) and several other gangliosides

Fukuta, S. ; Werkmeister, J.A. ; Burns, G.F. ; Ginsburg, V. ; Magnani, J.L.

The Journal of biological chemistry, 1987-04, Vol.262 (10), p.4800-4803 [Periódico revisado por pares]

Bethesda, MD: Elsevier Inc

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8
Interaction of cholera toxin with rat intestinal brush border membranes. Relative roles of gangliosides and galactoproteins as toxin receptors
Interaction of cholera toxin with rat intestinal brush border membranes. Relative roles of gangliosides and galactoproteins as toxin receptors
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Interaction of cholera toxin with rat intestinal brush border membranes. Relative roles of gangliosides and galactoproteins as toxin receptors

Critchley, D R ; Magnani, J L ; Fishman, P H

The Journal of biological chemistry, 1981-08, Vol.256 (16), p.8724-8731 [Periódico revisado por pares]

United States

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9
Evidence for the allosteric regulation of glycogen synthesis in the intact Escherichia coli cell. Agreement of the values of the parameters of the Hill equation fitted to data for glycogen synthesis in vivo with the abailable values obtained in vitro with adenosine diphosphoglucose synthetase
Evidence for the allosteric regulation of glycogen synthesis in the intact Escherichia coli cell. Agreement of the values of the parameters of the Hill equation fitted to data for glycogen synthesis in vivo with the abailable values obtained in vitro with adenosine diphosphoglucose synthetase
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Evidence for the allosteric regulation of glycogen synthesis in the intact Escherichia coli cell. Agreement of the values of the parameters of the Hill equation fitted to data for glycogen synthesis in vivo with the abailable values obtained in vitro with adenosine diphosphoglucose synthetase

Dietzler, D N ; Leckie, M P ; Lais, C J ; Magnani, J L

The Journal of biological chemistry, 1975-03, Vol.250 (6), p.2383-2387 [Periódico revisado por pares]

United States: American Society for Biochemistry and Molecular Biology

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10
Evidence for the coordinate control of glycogen synthesis, glucose utilization, and glycolysis in Escherichia coli. II. Quantitative correlation of the inhibition of glycogen synthesis and the stimulation of glucose utilization by 2,4-dinitrophenol with the effects on the cellular levels of glucose 6-phosphate, fructose, 1,6-diphosphate, and total adenylates
Evidence for the coordinate control of glycogen synthesis, glucose utilization, and glycolysis in Escherichia coli. II. Quantitative correlation of the inhibition of glycogen synthesis and the stimulation of glucose utilization by 2,4-dinitrophenol with the effects on the cellular levels of glucose 6-phosphate, fructose, 1,6-diphosphate, and total adenylates
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Evidence for the coordinate control of glycogen synthesis, glucose utilization, and glycolysis in Escherichia coli. II. Quantitative correlation of the inhibition of glycogen synthesis and the stimulation of glucose utilization by 2,4-dinitrophenol with the effects on the cellular levels of glucose 6-phosphate, fructose, 1,6-diphosphate, and total adenylates

Dietzler, D N ; Leckie, M P ; Magnani, J L ; Sughrue, M J ; Bergstein, P E

The Journal of biological chemistry, 1975-09, Vol.250 (18), p.7195-7203 [Periódico revisado por pares]

United States: American Society for Biochemistry and Molecular Biology

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