-
1
-
-
0028952914
-
Structural aspects of the allosteric inhibition of fructose-1,6bisphosphatase by AMP: The binding of both the substrate analogue 2,5-anhydro-o-glucitol 1,6-bisphosphate and catalytic metal ions monitored by X-ray crystallography
-
Villeret V, Huang SH, Zhang YP, Lipscomb WN: Structural aspects of the allosteric inhibition of fructose-1,6bisphosphatase by AMP: the binding of both the substrate analogue 2,5-anhydro-o-glucitol 1,6-bisphosphate and catalytic metal ions monitored by X-ray crystallography. Biochemistry 1995, 34:4307-4315.
-
(1995)
Biochemistry
, vol.34
, pp. 4307-4315
-
-
Villeret, V.1
Huang, S.H.2
Zhang, Y.P.3
Lipscomb, W.N.4
-
2
-
-
0028922940
-
Crystal structure of spinach chloroplast fructose-1,6-biphosphatase at 2.8 angstrom resolution
-
Villeret V, Huang SH, Zhang YP, Lipscomb WN: Crystal structure of spinach chloroplast fructose-1,6-biphosphatase at 2.8 angstrom resolution. Biochemistry 1995, 34:4299-4306.
-
(1995)
Biochemistry
, vol.34
, pp. 4299-4306
-
-
Villeret, V.1
Huang, S.H.2
Zhang, Y.P.3
Lipscomb, W.N.4
-
3
-
-
0026719692
-
An unlikely sugar substrate site in the 1.65 structure of the human aldose reductase holoenzyme implicated in diabetic complications
-
Wilson DK, Bohren KM, Gabbay KH, Quiocho FA: An unlikely sugar substrate site in the 1.65 structure of the human aldose reductase holoenzyme implicated in diabetic complications. Science 1992, 257:81-84.
-
(1992)
Science
, vol.257
, pp. 81-84
-
-
Wilson, D.K.1
Bohren, K.M.2
Gabbay, K.H.3
Quiocho, F.A.4
-
4
-
-
0028331867
-
An anion binding site in human aldose reductase: Mechanistic implications for the binding of citrate, cacodylate, and glucose 6-phosphate
-
Harrison DH, Bohren KM, Ringe D, Petsko GA, Gabbay KH: An anion binding site in human aldose reductase: mechanistic implications for the binding of citrate, cacodylate, and glucose 6-phosphate. Biochemistry 1994, 33:2011-2020.
-
(1994)
Biochemistry
, vol.33
, pp. 2011-2020
-
-
Harrison, D.H.1
Bohren, K.M.2
Ringe, D.3
Petsko, G.A.4
Gabbay, K.H.5
-
5
-
-
0028222097
-
Tyrosine-48 is the proton donor and histidine110 directs substrate selectivity in the reduction reaction of human aldose reductase: Enzyme kinetics and crystal structure of the Y48H mutant enzyme
-
Bohren KM, Grimshaw CE, Lai C-J, Harrison DH, Ringe D, Petsko GA, Gabbay KH: Tyrosine-48 is the proton donor and histidine110 directs substrate selectivity in the reduction reaction of human aldose reductase: enzyme kinetics and crystal structure of the Y48H mutant enzyme. Biochemistry 1994, 33:2021-2032.
-
(1994)
Biochemistry
, vol.33
, pp. 2021-2032
-
-
Bohren, K.M.1
Grimshaw, C.E.2
Lai, C.-J.3
Harrison, D.H.4
Ringe, D.5
Petsko, G.A.6
Gabbay, K.H.7
-
6
-
-
0028155824
-
Structures of human and porcine aldehyde reductase: An enzyme implicated in diabetic complications
-
El-Kabbani O, Green NC, Lin GD, Carson M, Narayana SVL, Moore KM, Flynn TG, DeLucas U: Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications. Acta Crystallogr D 1994, 50:859-868.
-
(1994)
Acta Crystallogr D
, vol.50
, pp. 859-868
-
-
El-Kabbani, O.1
Green, N.C.2
Lin, G.D.3
Carson, M.4
Svl, N.5
Moore, K.M.6
Flynn, T.G.7
Delucas, U.8
-
7
-
-
0011830644
-
Crystallization and preliminary structure of porcine aldehyde reductase-NADPH binary complex
-
El-Kabbani O, Judge K: Crystallization and preliminary structure of porcine aldehyde reductase-NADPH binary complex. Acta Crystallogr D 1995, 51:605-608.
-
(1995)
Acta Crystallogr D
, vol.51
, pp. 605-608
-
-
El-Kabbani, O.1
Judge, K.2
-
8
-
-
0029003606
-
Aldose reductase as a target for drug design: Molecular modeling calculations on the binding of acyclic sugar substrates to the enzyme
-
De Winter HL, Von Itzstein M: Aldose reductase as a target for drug design: molecular modeling calculations on the binding of acyclic sugar substrates to the enzyme. Biochemistry 1995, 34:8299-8308.
-
(1995)
Biochemistry
, vol.34
, pp. 8299-8308
-
-
De Winter, H.L.1
Von Itzstein, M.2
-
9
-
-
85030280763
-
-
The binding conformations of acyclic carbohydrate substrates of aldose reductase are investigated by molecular modelling techniques on the basis of the X-ray crystal structure of the enzyme. Residues His110, Tyr48 form strong hydrogen bonds with the carbonyl oxygen of the substrate and Trp111 appears to be important in the binding of 2'-hydroxyl-containing substrates. His110 is protonated at Ne2 when an aldehyde substrate is bound, and may serve as a proton donor in the catalytic reaction.
-
Residues His
, vol.110
, pp. 48
-
-
-
11
-
-
0028308819
-
Mechanism of aldose reductase inhibition: Binding of NADP+/NADPH and alrestatin-like inhibitors
-
Ehrig T, Bohren KM, Prendergast FG, Gabbay KH: Mechanism of aldose reductase inhibition: binding of NADP+/NADPH and alrestatin-like inhibitors. Biochemistry 1994, 33:7157-7165.
-
(1994)
Biochemistry
, vol.33
, pp. 7157-7165
-
-
Ehrig, T.1
Bohren, K.M.2
Prendergast, F.G.3
Gabbay, K.H.4
-
12
-
-
0027326529
-
Aldose reductase inhibitors: Recent developments
-
Sarges R, Dates PJ: Aldose reductase inhibitors: recent developments. Prog Drug Res 1993, 40:99-161.
-
(1993)
Prog Drug Res
, vol.40
, pp. 99-161
-
-
Sarges, R.1
Dates, P.J.2
-
13
-
-
0028299344
-
General preparation of 7-substituted 4chromanones: Synthesis of a potent aldose reductase inhibitor
-
Koch K, Biggers MS: General preparation of 7-substituted 4chromanones: synthesis of a potent aldose reductase inhibitor. J Org Chem 1994, 59:1216-1 218.
-
(1994)
J Org Chem
, vol.59
, pp. 1216-1218
-
-
Koch, K.1
Biggers, M.S.2
-
14
-
-
0030051224
-
Synthesis of pyrrolo[3,4-c]pyridine derivatives possessing an acid group and their in vitro and in vivo evaluation as aldose reductase inhibitors
-
Da Settimo A, Primofiore G, Da Settimo F, Simorini F, La Motta C, Martinelli A, Boldrini E: Synthesis of pyrrolo[3,4-c]pyridine derivatives possessing an acid group and their in vitro and in vivo evaluation as aldose reductase inhibitors. Eur J Med Chem 1996, 31:49-58.
-
(1996)
Eur J Med Chem
, vol.31
, pp. 49-58
-
-
Da Settimo, A.1
Primofiore, G.2
Da Settimo, F.3
Simorini, F.4
La Motta, C.5
Martinelli, A.6
Boldrini, E.7
-
16
-
-
0029001510
-
Selectin-carbohydrate interactions and the initiation of the inflammatory process
-
Lasky LA: Selectin-carbohydrate interactions and the initiation of the inflammatory process. Annu Rev Biochem 1995, 64:113-139.
-
(1995)
Annu Rev Biochem
, vol.64
, pp. 113-139
-
-
Lasky, L.A.1
-
17
-
-
85030285225
-
-
This is an excellent review which covers much of the recent literature concerning selectin-carbohydrate interactions, and is a 'must read' for researchers involved in the design and synthesis of selectin inhibitors
-
This is an excellent review which covers much of the recent literature concerning selectin-carbohydrate interactions, and is a 'must read' for researchers involved in the design and synthesis of selectin inhibitors.
-
-
-
-
18
-
-
0027957760
-
Insight into E-selectin/ligand interaction from the crystal structure and mutagenesis of the lec/EGF domains
-
Graves BJ, Crowther RL, Chandran C, Rumberger JM, Li S, Huang K-S, Presky DH, Familletti PC, Wolitzky BA, Burns DK: Insight into E-selectin/ligand interaction from the crystal structure and mutagenesis of the lec/EGF domains. Nature 1994, 367:532-538.
-
(1994)
Nature
, vol.367
, pp. 532-538
-
-
Graves, B.J.1
Crowther, R.L.2
Chandran, C.3
Rumberger, J.M.4
Li, S.5
Huang, K.-S.6
Presky, D.H.7
Familletti, P.C.8
Wolitzky, B.A.9
Burns, D.K.10
-
19
-
-
0028242519
-
x: Potent inhibitors of E-selectinmediated cell adhesion; reagent for staining activated endothelial cells
-
x: potent inhibitors of E-selectinmediated cell adhesion; reagent for staining activated endothelial cells. Glycobiology 1994, 4:259-265.
-
(1994)
Glycobiology
, vol.4
, pp. 259-265
-
-
Welply, J.K.1
Zaheer Abbas, S.2
Scudder, P.3
Keene, J.L.4
Broschat, K.5
Casnocha, S.6
Gorka, C.7
Steininger, C.8
Howard, S.C.9
Schmuke, J.J.10
-
20
-
-
0028790945
-
Selectin-saccharide interactions: Revealing structure-function relationships with chemical synthesis
-
Manning DD, Bertozzi CR, Pohl NL, Rosen SD, Kiessling LL: Selectin-saccharide interactions: revealing structure-function relationships with chemical synthesis. J Org Chem 1995, 60:6254-6255.
-
(1995)
J Org Chem
, vol.60
, pp. 6254-6255
-
-
Manning, D.D.1
Bertozzi, C.R.2
Pohl, N.L.3
Rosen, S.D.4
Kiessling, L.L.5
-
21
-
-
0028863975
-
Sulfated disaccharide inhibitors of L-selectin: Deriving structural leads from a physiological selectin ligand
-
Bertozzi CR, Fukuda S, Rosen SD: Sulfated disaccharide inhibitors of L-selectin: deriving structural leads from a physiological selectin ligand. Biochemistry 1995, 34:14271-14278.
-
(1995)
Biochemistry
, vol.34
, pp. 14271-14278
-
-
Bertozzi, C.R.1
Fukuda, S.2
Rosen, S.D.3
-
23
-
-
0028875976
-
Synthesis of a divalent sialyl Lewis x O-glycan, a potent inhibitor of lymphocyte-endothelium adhesion - Evidence that multivalency enhances the saccharide binding to L-selectin
-
Maaheimo H, Renkonen R, Turunen JP, Penttila L, Renkonen O: Synthesis of a divalent sialyl Lewis x O-glycan, a potent inhibitor of lymphocyte-endothelium adhesion - evidence that multivalency enhances the saccharide binding to L-selectin. Eur J Biochem 1995, 234:616-625.
-
(1995)
Eur J Biochem
, vol.234
, pp. 616-625
-
-
Maaheimo, H.1
Renkonen, R.2
Turunen, J.P.3
Penttila, L.4
Renkonen, O.5
-
24
-
-
0028895061
-
Ligand recognition by E-selectin: Synthesis, inhibitory activity, and conformational analysis of bivalent sialyl Lewis x analogs
-
DeFrees SA, Kosch W, Way W, Paulson JC, Sabesan S, Halcomb RL, Huang D-H, Ichikawa Y, Wong C-H: Ligand recognition by E-selectin: synthesis, inhibitory activity, and conformational analysis of bivalent sialyl Lewis x analogs. J Am Chem Soc 1995, 117:66-79.
-
(1995)
J Am Chem Soc
, vol.117
, pp. 66-79
-
-
-
26
-
-
0029056695
-
Synthesis of biologically active sialyl Lewis x mimetics
-
Huang H, Wong C-H: Synthesis of biologically active sialyl Lewis x mimetics. J Org Chem 1995, 60:3100-3106.
-
(1995)
J Org Chem
, vol.60
, pp. 3100-3106
-
-
Huang, H.1
Wong, C.-H.2
-
27
-
-
0030043567
-
Synthesis of a sialyl Lewis x mimic with fixed carboxylic acid group: Chemical approach toward the elucidation of the bioactive conformation of sialyl Lewis x
-
Thoma G, Schwarzenbach F, Duthaler RO: Synthesis of a sialyl Lewis x mimic with fixed carboxylic acid group: chemical approach toward the elucidation of the bioactive conformation of sialyl Lewis x. J Org Chem 1996, 61:514-524.
-
(1996)
J Org Chem
, vol.61
, pp. 514-524
-
-
Thoma, G.1
Schwarzenbach, F.2
Duthaler, R.O.3
-
28
-
-
0029985956
-
Synthesis of deoxygalactose-containing sialyl Lex ganglioside analogues to elucidate the structure necessary for selectin recognition
-
Komba S, Ishida H, Kiso M, Hasegawa A: Synthesis of deoxygalactose-containing sialyl Lex ganglioside analogues to elucidate the structure necessary for selectin recognition. Glycoconjugate J 1996, 13:241-254.
-
(1996)
Glycoconjugate J
, vol.13
, pp. 241-254
-
-
Komba, S.1
Ishida, H.2
Kiso, M.3
Hasegawa, A.4
-
30
-
-
0028925854
-
A sialic acid-derived phosphorate analog inhibits different strains of influenza virus neuraminidase with different efficiencies
-
White CL, Janakiraman MN, Laver WG, Philippen C, Vasella A, Air GM, Luo M: A sialic acid-derived phosphorate analog inhibits different strains of influenza virus neuraminidase with different efficiencies. J Mol S/o/1995, 245:623-634.
-
(1995)
J Mol S/o
, vol.245
, pp. 623-634
-
-
White, C.L.1
Janakiraman, M.N.2
Laver, W.G.3
Philippen, C.4
Vasella, A.5
Air, G.M.6
Luo, M.7
-
31
-
-
0029099621
-
Structure-based inhibitors of influenza virus sialidase
-
Singh S, Jedrzejas MJ, Air GM, Luo M, Laver WG, Brouillette WJ: Structure-based inhibitors of influenza virus sialidase. A benzole acid lead with novel interaction. J Med Chem 1995, 38:3217-3225. Noncarbohydrate-based, aromatic inhibitors of influenza-virus sialidase are presented. This class of compound appears to have reasonable in vitro activity against influenza-virus replication and may provide an alternative template for the discovery of potent sialidase inhibitors.
-
(1995)
A Benzole Acid Lead with Novel Interaction. J Med Chem
, vol.38
, pp. 3217-3225
-
-
Singh, S.1
Jedrzejas, M.J.2
Air, G.M.3
Luo, M.4
Laver, W.G.5
Brouillette, W.J.6
-
32
-
-
0024466223
-
Hemagglutinins from two influenza virus variants bind to sialic acid derivatives with millimolar dissociation constants: A 500-MHz proton nuclear magnetic resonance study
-
Sauter NK, Bednarski MD, Wurzburg BA, Hanson JE, Whitesides GM, Skehel JJ, Wiley DC: Hemagglutinins from two influenza virus variants bind to sialic acid derivatives with millimolar dissociation constants: a 500-MHz proton nuclear magnetic resonance study. Biochemistry 1989, 28:8388-8396.
-
(1989)
Biochemistry
, vol.28
, pp. 8388-8396
-
-
Sauter, N.K.1
Bednarski, M.D.2
Wurzburg, B.A.3
Hanson, J.E.4
Whitesides, G.M.5
Skehel, J.J.6
Wiley, D.C.7
-
33
-
-
0026485171
-
Carbohydrate materials bearing neuraminidaseresistant C-glycosides of sialic acid strongly inhibit the in vitro infectivity of influenza virus
-
Nagy JO, Wang Peng GJH, Schaefer ME, Hill TG, Callstrom MR, Bednarski MD: Carbohydrate materials bearing neuraminidaseresistant C-glycosides of sialic acid strongly inhibit the in vitro infectivity of influenza virus. J Med Chem 1992, 35:4501-4502.
-
(1992)
J Med Chem
, vol.35
, pp. 4501-4502
-
-
Nagy, J.O.1
Gjh, W.P.2
Schaefer, M.E.3
Hill, T.G.4
Callstrom, M.R.5
Bednarski, M.D.6
-
34
-
-
0028805760
-
Effective inhibitors of hemagglutination by influenza virus synthesized from polymers having active ester groups
-
Mammen M, Dahmann G, Whitesides GM: Effective inhibitors of hemagglutination by influenza virus synthesized from polymers having active ester groups. Insight into mechanism of inhibition. J Med Chem 1995, 38:4179-4190. The synthesis and biological evaluation of polyvalent sialosides is described. A range of C-glycosides of N-acetylneuraminic acid are copolymerized with a polymer that is preactivated by the incorporation of active ester groups. Polyvalency enhances the affinity of influenza virus for haemagglutinin and provides a useful model for the design of inhibitors of other microbe-host interactions.
-
(1995)
Insight into Mechanism of Inhibition. J Med Chem
, vol.38
, pp. 4179-4190
-
-
Mammen, M.1
Dahmann, G.2
Whitesides, G.M.3
-
35
-
-
0029994114
-
Polyacrylamides bearing pendant α-sialoside groups strongly inhibit agglutination of erythrocytes by influenza virus: The strong inhibition reflects enhanced binding through cooperative polyvalent interactions
-
Sigal G, Mammen M, Dahmann G, Whitesides GM: Polyacrylamides bearing pendant α-sialoside groups strongly inhibit agglutination of erythrocytes by influenza virus: the strong inhibition reflects enhanced binding through cooperative polyvalent interactions. J Am Chem Soc 1996, 118:3789-3800.
-
(1996)
J Am Chem Soc
, vol.118
, pp. 3789-3800
-
-
Sigal, G.1
Mammen, M.2
Dahmann, G.3
Whitesides, G.M.4
-
38
-
-
0023915219
-
Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid
-
Weis W, Brown JH, Cusack S, Paulson JC, Skehel JJ, Wiley DC: Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid. Nature 1988, 333:426-431.
-
(1988)
Nature
, vol.333
, pp. 426-431
-
-
Weis, W.1
Brown, J.H.2
Cusack, S.3
Paulson, J.C.4
Skehel, J.J.5
Wiley, D.C.6
-
39
-
-
0028874529
-
Glycosylation inhibitors in biology and medicine
-
Jacob GS: Glycosylation inhibitors in biology and medicine. Curr Opin Struct Biol 1995, 5:605-611.
-
(1995)
Curr Opin Struct Biol
, vol.5
, pp. 605-611
-
-
Jacob, G.S.1
-
40
-
-
0028874610
-
Structure of the 70 kDa soluble lytic transglycosylase complexed with bulgecin a
-
Thunnissen AMWH, Rozeboom HJ, Kalk JH, Dijkstra BW: Structure of the 70 kDa soluble lytic transglycosylase complexed with bulgecin A. Implications for the enzymatic mechanism. Biochemistry 1995, 34:12729-12737.
-
(1995)
Implications for the Enzymatic Mechanism. Biochemistry
, vol.34
, pp. 12729-12737
-
-
Amwh, T.1
Rozeboom, H.J.2
Kalk, J.H.3
Dijkstra, B.W.4
-
41
-
-
0029052863
-
The catalytic domain of a bacterial lytic transglycosylase defines a novel class of lysozymes
-
Thunnissen AMWH, Isaacs NW, Kijkstra BW: The catalytic domain of a bacterial lytic transglycosylase defines a novel class of lysozymes. Proteins 1995, 22:245-258.
-
(1995)
Proteins
, vol.22
, pp. 245-258
-
-
Thunnissen, A.M.W.H.1
Isaacs, N.W.2
Kijkstra, B.W.3
-
43
-
-
0026598947
-
Lactose binding to heat-labile enterotoxin revealed by X-ray crystallography
-
Sixma TK, Pronk SE, Kalk KH, Van Zanten BAM, Berghuis AM, Hoi WGJ: Lactose binding to heat-labile enterotoxin revealed by X-ray crystallography. Nature 1992, 355:561-564.
-
(1992)
Nature
, vol.355
, pp. 561-564
-
-
Sixma, T.K.1
Pronk, S.E.2
Kalk, K.H.3
Van Zanten, B.A.M.4
Berghuis, A.M.5
Hoi, W.G.J.6
-
44
-
-
0028267231
-
Crystal structure of cholera toxin B-pentamer bound to receptor GM1 pentasaccharide
-
Merritt EA, Sarfaty S, Van den Akker F, L'hoir C, Martial JA, Hol WGJ: Crystal structure of cholera toxin B-pentamer bound to receptor GM1 pentasaccharide. Protein Sei 1994, 3:166-175.
-
(1994)
Protein Sei
, vol.3
, pp. 166-175
-
-
Merritt, E.A.1
Sarfaty, S.2
Van Den Akker, F.3
L'Hoir, C.4
Martial, J.A.5
Hol, W.G.J.6
-
45
-
-
0024377837
-
Thermodynamics of intersubunit interactions in cholera toxin upon binding to the oligosaccharide portion of its cell surface receptor, ganglioside GM1
-
Schön A, Freire E: Thermodynamics of intersubunit interactions in cholera toxin upon binding to the oligosaccharide portion of its cell surface receptor, ganglioside GM1. Biochemistry 1989, 28:5019-5024.
-
(1989)
Biochemistry
, vol.28
, pp. 5019-5024
-
-
Schön, A.1
Freire, E.2
-
46
-
-
0026498361
-
Purification, crystallization and preliminary crystallographic study of neuraminidase from Vibrio cholerae and Salmonella typhimurium LT2
-
Taylor G, Vimr E, Garman E, Laver G: Purification, crystallization and preliminary crystallographic study of neuraminidase from Vibrio cholerae and Salmonella typhimurium LT2. J Mol Biol 1992, 226:1287-1290.
-
(1992)
J Mol Biol
, vol.226
, pp. 1287-1290
-
-
Taylor, G.1
Vimr, E.2
Garman, E.3
Laver, G.4
-
47
-
-
0027364312
-
Crystal structure of a bacterial sialidase (from Salmonella typhimurium LT2) shows the same fold as an influenza virus neuraminidase
-
Crennell SJ, Garman EF, Laver WG, Vimr ER, Taylor GL: Crystal structure of a bacterial sialidase (from Salmonella typhimurium LT2) shows the same fold as an influenza virus neuraminidase. Proc Natl Acad Sci USA 1993, 90:9852-9856.
-
(1993)
Proc Natl Acad Sci USA
, vol.90
, pp. 9852-9856
-
-
Crennell, S.J.1
Garman, E.F.2
Laver, W.G.3
Vimr, E.R.4
Taylor, G.L.5
-
48
-
-
0028773635
-
Crystal structure of Vibrio cholerae neuraminidase reveals dual lectinlike domains in addition to the catalytic domain
-
Crennell S, Garman E, Laver W, Vimr E, Taylor G: Crystal structure of Vibrio cholerae neuraminidase reveals dual lectinlike domains in addition to the catalytic domain. Structure 1994,2:535-544.
-
(1994)
Structure
, vol.2
, pp. 535-544
-
-
Crennell, S.1
Garman, E.2
Laver, W.3
Vimr, E.4
Taylor, G.5
-
49
-
-
0029645872
-
The three domains of a bacterial sialidase: α β-propeller, an immunoglobulin module and a galactose-binding jelly-roll
-
Gaskell A, Crennell S, Taylor G: The three domains of a bacterial sialidase: α β-propeller, an immunoglobulin module and a galactose-binding jelly-roll. Structure 1995, 3:1197-1205. The X-ray structure of sialidase from Micromonospora virdifaciens is reported. This bacterial sialidase has an additional lectin-like domain, not unlike sialidase from Vibrio cholerae. This combination of an enzyme and lectin domain may be common in bacterial and parasitic sialidases.
-
(1995)
Structure
, vol.3
, pp. 1197-1205
-
-
Gaskell, A.1
Crennell, S.2
Taylor, G.3
-
50
-
-
0030032258
-
Safety and efficacy of the neuraminidase inhibitor GG167 in experimental human influenza
-
Hayden FG, Treanor JJ, Betts RF, Lobo M, Esinhart JD, Hussey EK: Safety and efficacy of the neuraminidase inhibitor GG167 in experimental human influenza. JAMA 1996, 275:295-299. This report details a study of 4-deoxy-4-guanidino-Neu5Ac2en used as an inhibitor in experimental human influenza infection. The data provide support for the effectiveness of the drug candidate for both prevention and early treatment of experimental influenza.
-
(1996)
JAMA
, vol.275
, pp. 295-299
-
-
Hayden, F.G.1
Treanor, J.J.2
Betts, R.F.3
Lobo, M.4
Esinhart, J.D.5
Hussey, E.K.6
|