-
1
-
-
0028774043
-
Crystal structures of influenza virus hemagglutinin in complex with high-affinity receptor analogs
-
Re-examination at 2.15 Å resolution of the binding site for sialic acid revealed important details of the NeuAc interaction. Four high-affinity analogs with substitutions of the NeuAc at the 2 and/or 4 positions with naphtalene or dansyl groups showed hydrophilic and hydrophobic interactions with hemagglutinin outside the NeuAc site. A hybrid analog with substitutions at both positions showed a 1000-fold higher affinity in hemagglutination inhibition; this is the most effective monovalent sialoside identified so far. Additional high-affinity analogs were proposed for synthesis, based on a combination of the properties found. of outstanding interest
-
(1994)
Structure
, vol.2
, pp. 719-731
-
-
Watowich1
Skehel2
Wiley3
-
2
-
-
0028023726
-
Structure of influenza hemagglutinin at the pH of membrane fusion
-
The crystal structure of the hemagglutinin conformation induced at the low pH of endosomal fusion demonstrates a major refolding of the secondary and tertiary structure, and movement of the apolar fusion peptide by 100 Å towards the tip of the molecule, i.e. into a position that would permit virus penetration. of outstanding interest
-
(1994)
Nature
, vol.371
, pp. 37-43
-
-
Bullough1
Hughson2
Skehel3
Wiley4
-
3
-
-
0027967960
-
Insertion of a coiled-coil peptide from influenza virus hemagglutinin into membranes
-
Using liposomal membranes under endosomal pH conditions, EPR and spin-labeled synthetic hemagglutinin peptides, the authors obtain interaction data which suggest how viral and host-cell membrane may come closer together to facilitate fusion. of special interest
-
(1994)
Science
, vol.266
, pp. 274-276
-
-
Gyu1
King2
Shin3
-
4
-
-
0028910054
-
Influenza hemagglutinin-mediated membrane fusion: influence of receptor binding on the lag phase preceding fusion
-
(1995)
Biochemistry
, vol.34
, pp. 1825-1832
-
-
Stegmann1
Bartoldus2
Zumbrunn3
-
5
-
-
0028813628
-
Influenza type A virus neuraminidase does not play a role in viral entry, replication, assembly, or budding
-
A neuraminidase-deficient mutant is shown to be infectious in cell cultures and in mice. The titers are lowered, however, as a result of the formation of virus aggregates, which are induced by hemagglutinin-sialic acid interactions between viral particles. of special interest
-
(1995)
J Virol
, vol.69
, pp. 1099-1106
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-
Liu1
Eichelberger2
Compans3
Air4
-
7
-
-
0027158246
-
A sialic acid analogue acting as a receptor determinant for binding but not for infection by influenza C virus
-
(1993)
FEBS Lett
, vol.323
, pp. 96-98
-
-
Brossmer1
Isecke2
Herrler3
-
10
-
-
0027930960
-
Structure of influenza virus neuraminidase B/Lee/40 complexed with sialic acid and a dehydro analog at 1.8 Å resolution: implications for the catalytic mechanism
-
(1994)
Biochemistry
, vol.33
, pp. 8172-8179
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-
Janakiraman1
White2
Laver3
Air4
Luo5
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11
-
-
0028325249
-
Molecular modeling studies on ligand binding to sialidase from influenza virus and the mechanism of catalysis
-
(1994)
J Med Chem
, vol.37
, pp. 616-624
-
-
Taylor1
von Itzstein2
-
12
-
-
0028303852
-
Structure of murine polyomavirus complexed with an oligosaccharide receptor fragment
-
The virus structure in complex with sialyl-3 lactose and modeling reveals interesting features, which differ from those of sialyl conjugate interaction with influenza virus. A virulence difference between small and large plaque strains may be related to distinct differences in the recognition of receptor saccharide side chains. of outstanding interest
-
(1994)
Nature
, vol.369
, pp. 160-163
-
-
Stehle1
Yan2
Benjamin3
Harrison4
-
13
-
-
0027257854
-
Binding to sialic acids is not an essential step for the entry of animal rotaviruses to epithelial cells in culture.
-
(1993)
J Virol
, vol.67
, pp. 5253-5259
-
-
Méndez1
Arias2
López3
-
14
-
-
0028986231
-
Activation of the Sendai virus fusion protein by receptor binding
-
On the basis of studies of virus interaction with red cells, a model is proposed for the stepwise mechanism, involving peptide conformational changes, of paramyxovirus entrance into cells, in analogy with the low-pH-induced mechanism for influenza virus. of outstanding interest
-
(1995)
Biochem Biophys Res Commun
, vol.208
, pp. 36-41
-
-
Dallocchio1
Tomasi2
Bellini3
-
15
-
-
0028986694
-
The role of the ganglioside GD1a as a receptor for Sendai virus
-
The receptor ganglioside enhances virus binding to liposomes, but fusion rate constants are paradoxically reduced after the density of the receptor increases, as a result of the effects of gangliosides on the membrane matrix properties. of special interest
-
(1995)
Biochemistry
, vol.34
, pp. 1084-1089
-
-
Epand1
Nir2
Parolini3
Flanagan4
-
16
-
-
0028199032
-
Membrane fusion of Semliki Forest virus requires sphingolipids in the target membrane
-
Cholesterol in the target membrane, or in the liposome, is necessary for the low-pH-dependent fusion to take place. Strong evidence supports the assertion that sphingolipid (minimium requirement is the ceramide part) is essential for fusion; cholesterol is sufficient for the binding to the membrane, and sphingolipid is confined to the actual fusion event. of outstanding interest
-
(1994)
EMBO J
, vol.13
, pp. 2797-2808
-
-
Nieva1
Bron2
Corver3
Wilschut4
-
17
-
-
0028953947
-
Sphingolipid-dependent fusion of Semliki Forest virus with cholesterol-containg liposomes requires both the 3-hydroxyl group and the double bond of the sphingolipid backbone
-
The structural requirement associated with dependence on sphingosine is documented. The low amount (1–2 mol%) of sphingolipid needed in the target membrane suggests a peptide—sphingolipid recognition event in the fusion mechanism, rather than a membrane matrix effect. of special interest
-
(1995)
J Virol
, vol.69
, pp. 3220-3223
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-
Corver1
Moesby2
Erukulla3
Reddy4
Bittman5
Wilschut6
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22
-
-
0028207130
-
Heparin specifically inhibits binding of V3 loop antibodies to HIV-1 gp120, an effect potentiated by CD4 binding
-
(1994)
AIDS
, vol.8
, pp. 183-192
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-
Harrop1
Coombe2
Rider3
-
25
-
-
0028129972
-
Characterization of human immunodeficiency virus type 1 gp120 binding to liposomes containing galactosylceramide
-
A possible role of Galβ1, 1Cer in the penetration of HIV-1 into host cells is further supported by careful studies of the binding of gp120 using various liposomal conditions and receptor candidates. Only Galβ1, 1Cer shows strong and consistent binding, the biological meaning of which is discussed. of outstanding interest
-
(1994)
J Virol
, vol.68
, pp. 5890-5898
-
-
Long1
Berson2
Cook3
Doms4
-
30
-
-
0028267231
-
Crystal structure of cholera toxin B-pentamer bound to receptor GM1 pentasaccharide
-
The first structure of a bacterial toxin in complex with a functional receptor saccharide. The five bound saccharides are located at the base and towards the side of the B-pentamer ring. Thus CT binds to cells with the toxic A-subunit on top of the ring, pointing away from the membrane. Details of the interaction of the toxin with the receptor allow interpretations of crossbindings in the case of LT, a close relative of CT, in which Arg13 is the only important difference at the binding site compared to CT. of outstanding interest
-
(1994)
Protein Sci
, vol.3
, pp. 166-175
-
-
Merritt1
Sarfaty2
van den Akker3
Ihoir4
Martial5
Hol6
-
31
-
-
0028500699
-
Structure of a pertussis toxin—sugar complex as a model for receptor binding
-
5 structure has a heterogeneous B-subunit composition but is very similar in overall structure to CT and LT. The 6-sialyl Gal of a transferrin undecasaccharide is bound at equivalent sites on subunits S2 and S3. The nature of the functional receptor is still unknown. of outstanding interest
-
(1994)
Nature Struct Biol
, vol.1
, pp. 591-596
-
-
Stein1
Boodhoo2
Armstrong3
Heerze4
Cockle5
Klein6
Read7
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33
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0027492707
-
Comparison of the B-pentamers of heat-labile enterotoxin and Verotoxin-1: Two structures with remarkable similarity and dissimilarity
-
(1993)
Biochemistry
, vol.32
, pp. 191-198
-
-
Sixma1
Stein2
Hol3
Read4
-
34
-
-
0028596536
-
Interaction of the Shiga-like toxin type 1 B-subunit with its carbohydrate receptor
-
Changes in the properties of the B-subunit upon low-affinity interaction with Galα1,4Galβ1,4GlcβMe enable the authors to propose an interesting model for toxin penetration, a model of general relevance for phenomena mediated by low-affinity protein—carbohydrate interaction. of outstanding interest
-
(1994)
Biochemistry
, vol.33
, pp. 14452-14463
-
-
St Hilaire1
Boyd2
Toone3
-
35
-
-
0028176046
-
Glycoproteins with Galα4Gal are absent from human erythrocyte membranes, indicating that glycolipids are the sole carriers of blood group P activities
-
Solid-phase binding to glycoproteins of specific antibodies and of Galα1,4Gal-recognizing E. coli bacteria makes it likely that this disccharide sequence is not expressed normally in human glycoproteins. In this way, some bacterial adhesins and toxins bind exclusively to glycolipid epitopes located close to membranes and lipid bilayers. of special interest
-
(1994)
J Biol Chem
, vol.269
, pp. 14620-14624
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-
Yang1
Bergström2
Karlsson3
-
36
-
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0027933527
-
Lipid modulation of glycolipid receptor function. Availability of Gal(α1–4)Gal disaccharide for Verotoxin binding in natural and synthetic glycolipids
-
(1994)
Eur J Biochem
, vol.223
, pp. 873-878
-
-
Boyd1
Magnusson2
Zhiuyan3
Lingwood4
-
37
-
-
0027157682
-
Alteration of the glycolipid binding specificity of the pig edema toxin from globotetraosyl to globotriaosyl ceramide alters in vivo tissue targetting and results in a Verotoxin 1-like disease in pigs
-
(1993)
J Exp Med
, vol.177
, pp. 1745-1753
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-
Boyd1
Tyrrell2
Maloney3
Gyles4
Brunton5
Lingwood6
-
39
-
-
0029034518
-
Digalactosylceramide is the receptor for staphylococcal enterotoxin-B in human kidney proximal tubular cells
-
(1995)
Glycobiology
, vol.5
, pp. 327-333
-
-
Chatterjee1
Khullar2
Shi3
-
41
-
-
0028123001
-
Galactose-binding site in Escherichia coli heat-labile enterotoxin (LT) and cholera toxin (CT)
-
This detailed crystallographic study of the strong Gal interaction with the binding site of LT and CT forms an interesting basis for the possible design of high-affinity receptor analogs. of outstanding interest
-
(1994)
Mol Microbiol
, vol.13
, pp. 745-753
-
-
Merritt1
Sixma2
Kalk3
van Zanten4
Hol5
-
42
-
-
0027943084
-
Delineation and comparison of ganglioside-binding epitopes for the toxins of Vibrio cholerae, Escherichia coli, and Clostridium tetani: evidence for overlapping epitopes.
-
Data from a detailed study of the binding of toxins to defined glycolipids, combined with molecular modeling, show overlapping binding epitopes on GM1 for CT and LT and on GQ1b for tetanus toxin. This suggests similarities among the still unknown binding site of tetanus toxin and those of CT and LT, despite their distinctly separate tropisms and mechanisms of action. of outstanding interest
-
(1994)
Proceedings of the National Academy of Sciences
, vol.91
, pp. 11859-11863
-
-
Ångström1
Teneberg2
Karlsson3
-
43
-
-
0028558414
-
Comparison of the glycolipid-binding specificities of cholera toxin and porcine Escherichia coli heat-labile enterotoxin: identification of a receptor-active non-ganglioside glycolipid for the heat-labile toxin in infant rabbit small intestine
-
Overlay of LT on thin-layer plates detects Galβ1,4GlcNAcβ1,3Galβ1,4Glcβ1,1Cer as a receptor-active glycolipid in target cells. Molecular modeling of the tetrasaccharide in the known binding site of LT indicates hydrogen bonding between Arg13 and the hydroxymethyl group of GlcNAc, explaining why this crossbinding is shown by LT but not by CT (His13). of outstanding interest
-
(1994)
Glycoconjuate J
, vol.11
, pp. 533-540
-
-
Teneberg1
Hirst2
Ångström3
Karlsson4
-
44
-
-
0027959631
-
The Heat-Labile Enterotoxin of Escherichia coli Binds to Polylactosaminoglycan-Containing Receptors in CaCo-2 Human Intestinal Epithelial Cells
-
Western blots probed with LT identify polylactosamine-type glycoproteins in cell culture as crossbinding receptors for the toxin. of special interest
-
(1994)
Biochemistry
, vol.33
, pp. 12886-12895
-
-
Orlandi1
Critchley2
Fishman3
-
45
-
-
0028172870
-
The Gal(α1-4)Gal-specific tip adhesin of Escherichia coli P-fimbriae is needed for pyelonephritis to occur in the normal urinary tract
-
A mutant E. coli strain with a deletion early in the papG gene, which abolishes the binding to Galα1,4Gal-containing isoreceptors when tested in vitro, is unable to induce pyelonephritis in cynomolgus monkeys, unlike the corresponding wild-type strain. of special interest
-
(1994)
Proc Natl Acad Sci USA
, vol.91
, pp. 11893-11899
-
-
Roberts1
Marklund2
Ilver3
Haslam4
Kaack5
Baskin6
Louis7
Möllby8
Winberg9
Normark10
-
46
-
-
0028949737
-
Glycoconjugate receptors for P-fimbriated Escherichia coli in the mouse. An animal model of urinary tract infection
-
In a mouse strain, used as an infection model for human urinary infection, the glycolipid isoreceptor pattern is distinctly different from that of human or monkey. An additional difference is that receptor activity is expressed also in mouse glycoproteins. The mouse is therefore not an ideal model for infection in the human. of special interest
-
(1995)
J Biol Chem
, vol.270
, pp. 9017-9025
-
-
Lanne1
Olsson2
Jovall3
Ångström4
Linder5
Marklund6
Bergström7
Karlsson8
-
47
-
-
0028120498
-
Epithelial glucosphingolipid expression as a determinant of bacterial adherence and cytokine production
-
An inhibitor of glycolipid synthesis decreases the expression of receptor-active glycolipids for E. coli on cultured cells, and in parallel reduces bacterial binding and the activation of cytokine production. No effect is observed on the corresponding behaviour of type 1-fimbriated E. coli. of special interest
-
(1994)
Infect Immun
, vol.62
, pp. 4404-4410
-
-
Svensson1
Lindstedt2
Radin3
Svanborg4
-
48
-
-
0028172418
-
Oligosaccharide-receptor interaction of the Galα1-4Gal binding adhesin of Streptococcus suis. Combining site architecture and characterization of two variant adhesin specificities
-
P-fimbriated E. coli and this bacterium recognize specifically the same disaccharide. However, using synthetic disaccharide analogs it is shown that the two bacteria recognize distinctly different epitopes. of outstanding interest
-
(1994)
J Biol Chem
, vol.269
, pp. 27466-27472
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-
Haataja1
Tikkanen2
Nilsson3
Magnusson4
Karlsson5
Finne6
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53
-
-
0028986626
-
b-containing glycoconjugates: A potential transgenic mouse model for studying Helicobacter pylori infection
-
Receptor-active Lewis-b-containing glycoconjugates, which are restricted in their natural expression to primates, are expressed in the gastrointestinal tract of transgenic mice and shown by in situ studies to bind specifically to the bacterium. of special interest
-
(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 1515-1519
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Falk1
Bry2
Holgersson3
Gordon4
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55
-
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0028148526
-
Sulfated glycoconjugate receptors for the Bordetella pertussis adhesin filamentous hemagglutinin (FHA) and mapping of the heparin-binding domain on FHA
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(1994)
Infect Immun
, vol.62
, pp. 5010-5019
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Hannah1
Menozzi2
Renauld3
Locht4
Brennan5
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57
-
-
0028245424
-
The pili of Pseudomonas aeruginosa strains PAK and PAO bind specifically to the carbohydrate sequence βGalNAc(1–4)βGal found in glycosphingolipids asialo-GM1 and asialo-GM2
-
Binding of the saccharide receptor for the major pilin subunit is demonstrated only at the tip of the pilus, and is mapped to a limited sequence in the subunit's C-terminal region. A corresponding synthetic peptide is able to inhibit the pilus—saccharide interaction. of special interest
-
(1994)
Mol Microbiol
, vol.11
, pp. 715-723
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-
Sheth1
Lee2
Wong3
Srivastava4
Hindsgaul5
Hodges6
Paranchych7
Irvin8
-
58
-
-
0028126792
-
Adherence of Pseudomonas aeruginosa and Candida albicans to glycosphingolipid (asialo-GM1) receptors is achieved by a conserved receptor-binding domain present on their adhesins
-
Antibodies against a defined peptide sequence show a similar mode of inhibition of binding to a GalNAcβ1,4Gal-containing synthetic glycoconjugate for the two microbes, indicating that that these two unrelated organisms may posess adhesins that are structurally similar to one another. of special interest
-
(1994)
Infect Immun
, vol.62
, pp. 5213-5219
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-
Yu1
Lee2
Hodges3
Paranchych4
Irvin5
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60
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0027428606
-
Pseudomonas aeruginosa pili bind to asialo GM1 which is increased on the surface of cystic fibrosis epithelial cells
-
(1993)
J Clin Invest
, vol.92
, pp. 1875-1880
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Saiman1
Prince2
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62
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0027253492
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Piglet ileal mucus contains protein and glycolipid (galactosylceramide) receptors specific for Escherichia coli K88 fimbriae
-
(1993)
Infect Immun
, vol.61
, pp. 2526-2531
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Blomberg1
Krivan2
Cohen3
Conway4
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63
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0028027760
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Age-related resistance to 987P fimbria-mediated colonization correlates with specific glycolipid receptors in intestinal mucus in swine.
-
(1994)
Infect Immun
, vol.62
, pp. 4789-4794
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Dean-Nyström1
Samuel2
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64
-
-
0028010076
-
Type 1 fimbrial shafts of Escherichia coli and Klebsiella pneumoniae influence sugar-binding specificities of their FimH adhesins
-
Detailed differences in the specificity of binding to mannose (Man)-containing synthetic assay conjugates for two recombinant fimbriae are shown to depend on the presence of the fimbrial shaft subunit, rather than on the Man-binding subunit. of special interest
-
(1994)
Infect Immun
, vol.62
, pp. 843-848
-
-
Madison1
Ofek2
Clegg3
Abraham4
-
65
-
-
0028953265
-
High affinity binding of the Entamoeba histolytica lectin to polyvalent N-acetylgalactosaminides
-
Polyvalent synthetic neoglycoprotein (39 residues of GalNAc linked to bovine serum albumin) is shown to be several hundred thousand-fold better inhibitors of binding than Gal or GalNAc. Synthetic multivalent ligands with defined epitope and spacing, which were shown before to be high-affinity inhibitors of the mammalian hepatic Gal/GalNAc lectin, are only moderate binders of the parasite adhesin. of special interest
-
(1995)
J Biol Chem
, vol.270
, pp. 5164-5171
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Adler1
Wood2
Lee3
Lee4
Petri5
Schnaar6
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66
-
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0028920556
-
A recombinant cystein-rich section of the Entamoeba histolytica galactose-inhibitable lectin is efficacious as a subunit vaccine in the gerbil model of amebic liver abscess
-
A vaccine constructed from the Gal/GalNAc-specific adhesin provides protective immunity against intrahepatic challenge with parasites in a gerbil infection model. of special interest
-
(1995)
J Infect Dis
, vol.171
, pp. 645-651
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Soong1
Kain2
Abd-Alla3
Jackson4
Ravdin5
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67
-
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0027326632
-
Thrombospondin related anonymous protein (TRAP) of Plasmodium falciparum binds specifically to sulfated glycoconjugates and to HepG2 hepatoma cells suggesting a role for this molecule in sporozoite invasion of hepatocytes.
-
(1993)
EMBO J
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Müller1
Reckman2
Hollingdale3
Bujard4
Robson5
Crisanti6
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69
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0028122878
-
Receptor and ligand domains for invasion of erythrocytes by Plasmodium falciparum
-
A cystein-rich receptor-active domain is defined in the NeuAc-binding surface protein EBA-175, after expression of truncated portions in COS cells and interaction with cells and glycoconjugates. A mechanism for recognition involving both sialic acid and the peptide is proposed. of special interest
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(1994)
Science
, vol.264
, pp. 1941-1944
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Sim1
Chitnis2
Wasniowska3
Hadley4
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71
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Glycoprotein glycans that inhibit adhesion of Escherichia coli mediated by K99 fimbriae: Treatment of experimental colibacillosis
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Infect Immun
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Mouricout1
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Julien4
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