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1
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0029731661
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Cross-talk between bacterial pathogens and their host cells
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of special interest. A comprehensive review that focuses on the Gram-negative pathogens S. flexneri, S. typhimurium, and Yersinia spp. The authors discuss the role of type III secretion systems and translocated bacterial effectors in controlling host signaling pathways mediating bacterial invasion, 'anti-phagocytosis', apoptosis and mammalian gene expression.
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Galan JE, Bliska JB. Cross-talk between bacterial pathogens and their host cells. of special interest Annu Rev Cell Dev Biol. 12:1996;221-255 A comprehensive review that focuses on the Gram-negative pathogens S. flexneri, S. typhimurium, and Yersinia spp. The authors discuss the role of type III secretion systems and translocated bacterial effectors in controlling host signaling pathways mediating bacterial invasion, 'anti-phagocytosis', apoptosis and mammalian gene expression.
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(1996)
Annu Rev Cell Dev Biol
, vol.12
, pp. 221-255
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Galan, J.E.1
Bliska, J.B.2
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2
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0030443711
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Microbial utilization of human signalling molecules
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of outstanding interest. An interesting review that describes mammalian signaling pathways and their possible role in adhesion and the internalisation of a variety of microorganisms, including bacteria, viruses, fungi and parasites. A comparison is made of the various strategies used by different pathogens to interact with integrins and other mammalian cell-surface molecules.
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Virji M. Microbial utilization of human signalling molecules. of outstanding interest Microbiology. 142:1996;3319-3336 An interesting review that describes mammalian signaling pathways and their possible role in adhesion and the internalisation of a variety of microorganisms, including bacteria, viruses, fungi and parasites. A comparison is made of the various strategies used by different pathogens to interact with integrins and other mammalian cell-surface molecules.
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(1996)
Microbiology
, vol.142
, pp. 3319-3336
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Virji, M.1
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3
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0030790687
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Common themes in microbial pathogenicity, II
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of special interest. A broad review that covers many of the important aspects of bacterial pathogenesis, including toxin production, bacterial adhesion and invasion, intra-cellular survival and grwoth, regulation of virulence gene expression and interaction of pathogens with the host immune system.
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Finlay BB, Falkow S. Common themes in microbial pathogenicity, II. of special interest Microbiol Rev. 61:1997;136-169 A broad review that covers many of the important aspects of bacterial pathogenesis, including toxin production, bacterial adhesion and invasion, intra-cellular survival and grwoth, regulation of virulence gene expression and interaction of pathogens with the host immune system.
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(1997)
Microbiol Rev
, vol.61
, pp. 136-169
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Finlay, B.B.1
Falkow, S.2
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4
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0030964241
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Exploitation of mammalian host cell functions by bacterial pathogens
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of special interest. Various aspects of the cell biology of infection are discussed.
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Finlay BB, Cossart P. Exploitation of mammalian host cell functions by bacterial pathogens. of special interest Science. 276:1997;718-725 Various aspects of the cell biology of infection are discussed.
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(1997)
Science
, vol.276
, pp. 718-725
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Finlay, B.B.1
Cossart, P.2
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5
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0025250067
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Multiple chain integrins are receptors for invasin, a protein that promotes bacterial penetration into mammalian cells
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Isberg RR, Leong JM. Multiple chain integrins are receptors for invasin, a protein that promotes bacterial penetration into mammalian cells. Cell. 60:1990;861-871.
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(1990)
Cell
, vol.60
, pp. 861-871
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Isberg, R.R.1
Leong, J.M.2
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6
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0028912193
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The mechanism of phagocytic uptake promoted by invasin - Integrin interaction
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Isberg RR, Tran Van Nhieu G. The mechanism of phagocytic uptake promoted by invasin - integrin interaction. Trends Cell Biol. 5:1995;120-124.
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(1995)
Trends Cell Biol
, vol.5
, pp. 120-124
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Isberg, R.R.1
Tran Van Nhieu, G.2
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7
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0031467678
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Host pathogen interactions during entry and actin-based movement of Listeria monocytogenes
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Ireton K, Cossart P. Host pathogen interactions during entry and actin-based movement of Listeria monocytogenes. Annu Rev Genet. 31:1997;113-138.
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(1997)
Annu Rev Genet
, vol.31
, pp. 113-138
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Ireton, K.1
Cossart, P.2
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8
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0029869384
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E-cadherin is the receptor for internalin, a surface protein required for entry of Listeria monocytogenes into epithelial cells
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of outstanding interest. An affinity chromatography approach (first employed by Isberg and colleagues; see [5]) was used to identify E-cadherin as the receptor for L. monocytogenes. The expression of chicken E-cadherin in fibroblasts that are normally deficient in cadherin expression is sufficient to promote the InIA-mediated uptake of Listeria. In addition, microscopy studies indicate that entry of Listeria is morphologically similar to that of Yersinia, and distinct from that of Salmonella.
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Mengaud J, Ohayon H, Gounon P, Mége RM, Cossart P. E-cadherin is the receptor for internalin, a surface protein required for entry of Listeria monocytogenes into epithelial cells. of outstanding interest Cell. 84:1996;923-932 An affinity chromatography approach (first employed by Isberg and colleagues; see [5]) was used to identify E-cadherin as the receptor for L. monocytogenes. The expression of chicken E-cadherin in fibroblasts that are normally deficient in cadherin expression is sufficient to promote the InIA-mediated uptake of Listeria. In addition, microscopy studies indicate that entry of Listeria is morphologically similar to that of Yersinia, and distinct from that of Salmonella.
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(1996)
Cell
, vol.84
, pp. 923-932
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Mengaud, J.1
Ohayon, H.2
Gounon, P.3
Mége, R.M.4
Cossart, P.5
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9
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0029844602
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The N-domain of the human CD66a adhesion molecule is a target for Opa proteins of Neisseria meningitidis and Neisseria gonorrhoeae
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Virji M, Watt SM, Barker S, Makepeace K, Doyannas R. The N-domain of the human CD66a adhesion molecule is a target for Opa proteins of Neisseria meningitidis and Neisseria gonorrhoeae. Mol Microbiol. 22:1996;929-939.
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(1996)
Mol Microbiol
, vol.22
, pp. 929-939
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Virji, M.1
Watt, S.M.2
Barker, S.3
Makepeace, K.4
Doyannas, R.5
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10
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0029848536
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Carcinoembryonic antigens (CD66) on epithelial cells and neutrophils are receptors for Opa proteins of pathogenic Neisseriae
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of special interest. By screening cells transfected with cDNAs encoding human cell-surface molecules, the authors found that CD66a on epithelial cells and neutrophils is a target for Opa proteins and that this interaction mediates invasion.
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Virji M, Makepeace K, Ferguson DJP, Watt SM. Carcinoembryonic antigens (CD66) on epithelial cells and neutrophils are receptors for Opa proteins of pathogenic Neisseriae. of special interest Mol Microbiol. 22:1996;941-950 By screening cells transfected with cDNAs encoding human cell-surface molecules, the authors found that CD66a on epithelial cells and neutrophils is a target for Opa proteins and that this interaction mediates invasion.
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(1996)
Mol Microbiol
, vol.22
, pp. 941-950
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Virji, M.1
Makepeace, K.2
Ferguson, D.J.P.3
Watt, S.M.4
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11
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0030924679
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Several carcinoembryonic antigens (CD66) serve as receptors for gonococcal opacity proteins
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of special interest. Following the observation that N. gonorrhoeae binds to a 30 kDa protein of polymorphonuclear leucocytes, the authors show that expression of this protein in HeLa cells mediates the binding and internalisation of E. coli expressing a Neisseria Opa protein.
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Chen T, Grunert F, Medina-Marino A, Gotschlich E. Several carcinoembryonic antigens (CD66) serve as receptors for gonococcal opacity proteins. of special interest J Exp Med. 185:1997;1557-1564 Following the observation that N. gonorrhoeae binds to a 30 kDa protein of polymorphonuclear leucocytes, the authors show that expression of this protein in HeLa cells mediates the binding and internalisation of E. coli expressing a Neisseria Opa protein.
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(1997)
J Exp Med
, vol.185
, pp. 1557-1564
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Chen, T.1
Grunert, F.2
Medina-Marino, A.3
Gotschlich, E.4
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12
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0030965374
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CD66 carcinoembryonic antigens mediate interactions between Opa-expressing Neisseria gonorrhoeae and human polymorphonuclear phagocytes
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of special interest. The authors identified surface proteins from activated neutrophils that bound to intact Opa52-expressing bacteria. Western blotting demonstrated that these proteins are members of the CD66 family. Experiments with HeLa cells expressing different members of this family of proteins show that they mediate Opa52-dependent uptake.
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Gray-Owen SD, Dehio C, Haude A, Grunert F, Meyer TF. CD66 carcinoembryonic antigens mediate interactions between Opa-expressing Neisseria gonorrhoeae and human polymorphonuclear phagocytes. of special interest EMBO J. 16:1997;3435-3445 The authors identified surface proteins from activated neutrophils that bound to intact Opa52-expressing bacteria. Western blotting demonstrated that these proteins are members of the CD66 family. Experiments with HeLa cells expressing different members of this family of proteins show that they mediate Opa52-dependent uptake.
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(1997)
EMBO J
, vol.16
, pp. 3435-3445
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Gray-Owen, S.D.1
Dehio, C.2
Haude, A.3
Grunert, F.4
Meyer, T.F.5
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13
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0029027169
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Binding of syndecan like cell surface proteoglycan receptors is required for Neisseria gonorrhoeae entry into human mucosal cells
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Van Putten JPM, Paul SM. Binding of syndecan like cell surface proteoglycan receptors is required for Neisseria gonorrhoeae entry into human mucosal cells. Embo J. 14:1995;2144-2154.
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(1995)
Embo J
, vol.14
, pp. 2144-2154
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Van Putten, J.P.M.1
Paul, S.M.2
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14
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0031029922
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Vitronectin mediates internalization of Neisseria gonorrhoeae by Chinese hamster ovary cells
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Duensing TD, Van Putten JPM. Vitronectin mediates internalization of Neisseria gonorrhoeae by Chinese hamster ovary cells. Infect Immun. 65:1997;964-970.
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(1997)
Infect Immun
, vol.65
, pp. 964-970
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Duensing, T.D.1
Van Putten, J.P.M.2
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15
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1842299317
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Binding of vitronectin to Opa-expressing Neisseria gonorrhoeae mediates invasion of HeLa cells
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Gomez-Duarte OG, Dehio M, Guzman CA, Chhatwal GS, Dhio C, Meyer T. Binding of vitronectin to Opa-expressing Neisseria gonorrhoeae mediates invasion of HeLa cells. Infect Immun. 65:1997;3857-3866.
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(1997)
Infect Immun
, vol.65
, pp. 3857-3866
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Gomez-Duarte, O.G.1
Dehio, M.2
Guzman, C.A.3
Chhatwal, G.S.4
Dhio, C.5
Meyer, T.6
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16
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0029933731
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A pathogenic bacterium triggers epithelial signals to form a functional bacterial receptor that mediates actin pseudopod formation
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of special interest. Various microscopic techniques are used to analyse the structure and composition of actin-rich pedestals induced by EPEC. The authors also use fractionation and an overlay technique to demonstrate that the tyrosine phosphorylated protein (Hp90) is in the mammalian cell membrane and interacts with the bacterial outer membrane protein intimin.
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Rosenshine I, Ruschkowski S, Stein M, Reinscheid DJ, Mills SD, Finlay BB. A pathogenic bacterium triggers epithelial signals to form a functional bacterial receptor that mediates actin pseudopod formation. of special interest EMBO J. 15:1996;2613-2624 Various microscopic techniques are used to analyse the structure and composition of actin-rich pedestals induced by EPEC. The authors also use fractionation and an overlay technique to demonstrate that the tyrosine phosphorylated protein (Hp90) is in the mammalian cell membrane and interacts with the bacterial outer membrane protein intimin.
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(1996)
EMBO J
, vol.15
, pp. 2613-2624
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Rosenshine, I.1
Ruschkowski, S.2
Stein, M.3
Reinscheid, D.J.4
Mills, S.D.5
Finlay, B.B.6
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17
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0030701868
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Enteropathogenic Escherichia coli (EPEC) transfers its receptor for intimate adherence into mammalian cells
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of outstanding interest. Starting with the observation that antibodies against secreted EPEC proteins recognize Hp90, the authors use bacterial genetics and other approaches to convincingly demonstrate that Hp90 is of bacterial origin. The idea that a bacterial protein inserted in the mammalian cell membrane serves as a 'receptor' that mediates downstream signaling is novel. It will be interesting to see if other bacteria use a similar approach to control processes involved in pathogenesis.
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Kenny B, De Vinney R, Stein M, Reinscheid DJ, Frey EA, Finlay BB. Enteropathogenic Escherichia coli (EPEC) transfers its receptor for intimate adherence into mammalian cells. of outstanding interest Cell. 91:1997;511-520 Starting with the observation that antibodies against secreted EPEC proteins recognize Hp90, the authors use bacterial genetics and other approaches to convincingly demonstrate that Hp90 is of bacterial origin. The idea that a bacterial protein inserted in the mammalian cell membrane serves as a 'receptor' that mediates downstream signaling is novel. It will be interesting to see if other bacteria use a similar approach to control processes involved in pathogenesis.
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(1997)
Cell
, vol.91
, pp. 511-520
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-
Kenny, B.1
De Vinney, R.2
Stein, M.3
Reinscheid, D.J.4
Frey, E.A.5
Finlay, B.B.6
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18
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0013549674
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Mutations in the cytoplasmic domain of the integrin β1 chain indicate a role for endocytosis factors in bacterial internalization
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of special interest. A role for endocytic factors in β1 integrin-mediated uptake of Yersinia is suggested by microscopy studies of clathrin localisation during invasion, and inhibition experiments involving potassium depletion and anticlathrin and anti-AP2 antibodies. The authors also demonstrate that an NPXY motif (a sequence involved in endocytosis of some receptors) is needed for bacterial internalisation.
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Tran Van Nhieu G, Krukonis ES, Reszka AA, Horwitz AF, Isberg RR. Mutations in the cytoplasmic domain of the integrin β1 chain indicate a role for endocytosis factors in bacterial internalization. of special interest J Biol Chem. 271:1996;7665-7672 A role for endocytic factors in β1 integrin-mediated uptake of Yersinia is suggested by microscopy studies of clathrin localisation during invasion, and inhibition experiments involving potassium depletion and anticlathrin and anti-AP2 antibodies. The authors also demonstrate that an NPXY motif (a sequence involved in endocytosis of some receptors) is needed for bacterial internalisation.
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(1996)
J Biol Chem
, vol.271
, pp. 7665-7672
-
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Tran Van Nhieu, G.1
Krukonis, E.S.2
Reszka, A.A.3
Horwitz, A.F.4
Isberg, R.R.5
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19
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85030336689
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Cytoskeletal rearrangemens during entry of Shingella flexneri into HeLa cells
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Adam T, Arpin M, Prévost MC, Gounon P, Sansonetti PJ. Cytoskeletal rearrangemens during entry of Shingella flexneri into HeLa cells. J Cell Biol. 15:1995;3315-3321.
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(1995)
J Cell Biol
, vol.15
, pp. 3315-3321
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Adam, T.1
Arpin, M.2
Prévost, M.C.3
Gounon, P.4
Sansonetti, P.J.5
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20
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0030003139
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Bacterial entry into epithelial cells: The paradigm of Shigella
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of special interest. An excellent review that discusses the molecular genetics and the cellular aspects of invasion of mammalian cells by Shigella flexneri.
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Menard R, Dehio C, Sansonetti PJ. Bacterial entry into epithelial cells: the paradigm of Shigella. of special interest Trends Microbiol. 4:1996;220-226 An excellent review that discusses the molecular genetics and the cellular aspects of invasion of mammalian cells by Shigella flexneri.
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(1996)
Trends Microbiol
, vol.4
, pp. 220-226
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Menard, R.1
Dehio, C.2
Sansonetti, P.J.3
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21
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0021346850
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Phagocytosis of the Legionnaires's disease bacterium (Legionella pneumophila occurs by a novel mechanism: Engulfment within a pseudopod coil
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Horwitz MA. Phagocytosis of the Legionnaires's disease bacterium (Legionella pneumophila occurs by a novel mechanism: engulfment within a pseudopod coil. Cell. 36:1984;27-33.
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(1984)
Cell
, vol.36
, pp. 27-33
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Horwitz, M.A.1
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22
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0030865798
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Interaction of Bartonella henselae with endothelial cells results in bacterial aggregation on the cell surface and the subsequent engulfment and internalisation of the bacterial aggregate by a unique structure, the invasome
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of special interest. A nice descriptive study of the formation and engulfment of a bacterial aggregate. It will be interesting to see if this novel type of internalisation involves cooperation or signaling between members of the aggregate.
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Dehio C, Meyer M, Berger J, Schwarz H, Lanz C. Interaction of Bartonella henselae with endothelial cells results in bacterial aggregation on the cell surface and the subsequent engulfment and internalisation of the bacterial aggregate by a unique structure, the invasome. of special interest J Cell Sci. 110:1997;2141-2154 A nice descriptive study of the formation and engulfment of a bacterial aggregate. It will be interesting to see if this novel type of internalisation involves cooperation or signaling between members of the aggregate.
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(1997)
J Cell Sci
, vol.110
, pp. 2141-2154
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Dehio, C.1
Meyer, M.2
Berger, J.3
Schwarz, H.4
Lanz, C.5
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23
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0030830882
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Internalin of Listeria monocytogenes with an intact leucine-rich repeat region is sufficient to promote internalization
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Lecuit M, Ohayon H, Braun L, Mengaud CP. Internalin of Listeria monocytogenes with an intact leucine-rich repeat region is sufficient to promote internalization. Infect Immun. 65:1997;5309-5319.
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(1997)
Infect Immun
, vol.65
, pp. 5309-5319
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Lecuit, M.1
Ohayon, H.2
Braun, L.3
Mengaud, C.P.4
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24
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0031594726
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The InlB protein of Listeria monocytogenes is sufficient to promote entry into mammalian cells
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Braun L, Ohayon H, Cossart P. The InlB protein of Listeria monocytogenes is sufficient to promote entry into mammalian cells. Mol Microbiol. 27:1998;1077-1088.
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(1998)
Mol Microbiol
, vol.27
, pp. 1077-1088
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Braun, L.1
Ohayon, H.2
Cossart, P.3
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25
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0030994387
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Modulation of bacterial entry in epithelial cells by association between vinculin and the Shigella IpaA invasin
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of outstanding interest. Cell lines expressing different amounts of vinculin are used to demonstate a role for this mammalian protein in the entry of Shigella. The bacterial protein IpaA is shown to interact with vinculin in vivo and in vitro. Confocal microscopy studies indicate that vinculin is recruited to bacterial entry sites, and the authors propose that IpaA might affect vinculin activity after this recruitment step.
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Tran Van Nhieu G, Ben-Ze'ev A, Sansonetti PJ. Modulation of bacterial entry in epithelial cells by association between vinculin and the Shigella IpaA invasin. of outstanding interest EMBO J. 16:1997;2717-2729 Cell lines expressing different amounts of vinculin are used to demonstate a role for this mammalian protein in the entry of Shigella. The bacterial protein IpaA is shown to interact with vinculin in vivo and in vitro. Confocal microscopy studies indicate that vinculin is recruited to bacterial entry sites, and the authors propose that IpaA might affect vinculin activity after this recruitment step.
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(1997)
EMBO J
, vol.16
, pp. 2717-2729
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Tran Van Nhieu, G.1
Ben-Ze'Ev, A.2
Sansonetti, P.J.3
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26
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0030032067
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The secreted lpa complex of Shigella flexneri promotes entry into mammalian cells
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of special interest. Beads coupled to an immunopurified IpaB-C complex induce membrane ruffling and are internalised by HeLa cells. The bacterial toxin ToxB is used to show that the cytoskeletal changes and uptake promoted by IpaB-C requires the activity of a rho family GTPase.
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Ménard R, Prévost MC, Gounon P, Sansonetti P, Dehio C. The secreted lpa complex of Shigella flexneri promotes entry into mammalian cells. of special interest Proc Natl Acad Sci USA. 93:1996;1254-1258 Beads coupled to an immunopurified IpaB-C complex induce membrane ruffling and are internalised by HeLa cells. The bacterial toxin ToxB is used to show that the cytoskeletal changes and uptake promoted by IpaB-C requires the activity of a rho family GTPase.
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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 1254-1258
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Ménard, R.1
Prévost, M.C.2
Gounon, P.3
Sansonetti, P.4
Dehio, C.5
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27
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0029915666
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Interaction of lpa proteins of Shigella flexneri with α5β1 integrin promotes entry of the bacterial into mammalian cells
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of special interest. The authors demonstrate that integrin engagement is involved in the invasion of CHO cells by Shigella flexneri. A secreted complex of IpaB, C and D proteins is shown to interact with purified α5β1 integrin, and transfection experiments demonstrates that increasing expression of this integrin augments the uptake of Shigella. In addition, bacterial infection stimulates clustering of α5β1, tyrosine phosphorylation of FAK and paxillin, and the reorganization of the actin cytoskeleton.
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Watarai M, Funato S, Sasakawa C. Interaction of lpa proteins of Shigella flexneri with α5β1 integrin promotes entry of the bacterial into mammalian cells. of special interest J Exp Med. 183:1996;991-999 The authors demonstrate that integrin engagement is involved in the invasion of CHO cells by Shigella flexneri. A secreted complex of IpaB, C and D proteins is shown to interact with purified α5β1 integrin, and transfection experiments demonstrates that increasing expression of this integrin augments the uptake of Shigella. In addition, bacterial infection stimulates clustering of α5β1, tyrosine phosphorylation of FAK and paxillin, and the reorganization of the actin cytoskeleton.
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(1996)
J Exp Med
, vol.183
, pp. 991-999
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Watarai, M.1
Funato, S.2
Sasakawa, C.3
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28
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0030913232
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Cas as a substrate of Yersinia YopH(Yop51), a bacterial protein tyrosine phosphatase that translocates into mammalian cells and targets focal adhesions
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Cas directly interact in vitro is also presented.
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Cas directly interact in vitro is also presented.
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(1997)
EMBO J
, vol.16
, pp. 2730-2744
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Black, D.S.1
Bliska, J.B.2
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29
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0030978909
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Cas and FAK, and the associated accumulation of these proteins in peripheral focal adhesions
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Cas and FAK may be involved in invasin-mediated entry is presented.
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Cas and FAK may be involved in invasin-mediated entry is presented.
-
(1997)
EMBO J
, vol.16
, pp. 2307-2318
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Persson, C.1
Carballeira, N.2
Wolf-Watz, H.3
Fällmann, M.4
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30
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0029958304
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A role for phosphoinositide 3-kinase in bacterial invasion
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3, indicate that bacteria stimulate PI 3-kinase activity.
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3, indicate that bacteria stimulate PI 3-kinase activity.
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(1996)
Science
, vol.274
, pp. 780-782
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Ireton, K.1
Payrastre, B.2
Chap, H.3
Ogawa, W.4
Sakue, H.5
Kasuga, M.6
Cossart, P.7
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31
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0030992837
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Signalling through the lipid products of phosphoinositide-3-OH kinase
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Toker A, Cantley LG. Signalling through the lipid products of phosphoinositide-3-OH kinase. Nature. 387:1997;673-676.
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(1997)
Nature
, vol.387
, pp. 673-676
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Toker, A.1
Cantley, L.G.2
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32
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0030474160
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D3 phosphoinositides and outside-in integrin signaling by glycoprotein Ilb-Illa mediate platelet actin assembly and filopodial extension induced by phorbol 12-myristate 13-acetate
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Hartwig JH, Kung S, Kovacsovics T, Janmey PA, Cantley LC, Stossel TP, Toker A. D3 phosphoinositides and outside-in integrin signaling by glycoprotein Ilb-Illa mediate platelet actin assembly and filopodial extension induced by phorbol 12-myristate 13-acetate. J Biol Chem. 271:1996;32986-32993.
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J Biol Chem
, vol.271
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Hartwig, J.H.1
Kung, S.2
Kovacsovics, T.3
Janmey, P.A.4
Cantley, L.C.5
Stossel, T.P.6
Toker, A.7
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34
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0031052018
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Rho, a small GTP-binding protein, is essential for Shigella invasion of epithelial cells
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of outstanding interest. These investigators use C3 toxin and microinjection of CHO cells with a constitutively active form of rho to demonstrate that this GTPase is required for invasion by Shigella. Evidence that rho activity is also needed for Shigella-induced tyrosine phosphorylation of FAK and paxillin and assembly of focal adhesion-like structures is presented.
-
Watarai M, Kamata Y, Kozaki S, Sasakawa C. rho, a small GTP-binding protein, is essential for Shigella invasion of epithelial cells. of outstanding interest J Exp Med. 185:1997;281-292 These investigators use C3 toxin and microinjection of CHO cells with a constitutively active form of rho to demonstrate that this GTPase is required for invasion by Shigella. Evidence that rho activity is also needed for Shigella-induced tyrosine phosphorylation of FAK and paxillin and assembly of focal adhesion-like structures is presented.
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(1997)
J Exp Med
, vol.185
, pp. 281-292
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-
Watarai, M.1
Kamata, Y.2
Kozaki, S.3
Sasakawa, C.4
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36
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0030015626
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Rho-dependent membrane folding causes Shigella entry into epithelial cells
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of special interest. C3 toxin is used to show that invasion by Shigella flexneri requres rho activity. The authors also use transient expression of epitop-tagged rho isoforms (rhoA, RhoB and RhoC) to demonstrate that these isoforms are differentially recruited to bacterial entry sites. Labeling of F-actin with S1-myosin decoration suggests that rho is not involved in the initial step of actin nucleation, but rather in subsequent actin filament formation.
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Adam T, Giry M, Boquet P, Sansonetti P. Rho-dependent membrane folding causes Shigella entry into epithelial cells. of special interest EMBO J. 15:1996;3315-3321 C3 toxin is used to show that invasion by Shigella flexneri requres rho activity. The authors also use transient expression of epitop-tagged rho isoforms (rhoA, RhoB and RhoC) to demonstrate that these isoforms are differentially recruited to bacterial entry sites. Labeling of F-actin with S1-myosin decoration suggests that rho is not involved in the initial step of actin nucleation, but rather in subsequent actin filament formation.
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(1996)
EMBO J
, vol.15
, pp. 3315-3321
-
-
Adam, T.1
Giry, M.2
Boquet, P.3
Sansonetti, P.4
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37
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Rho, rac, and cdc42 GTPases regulate the organization of the actin cytoskeleton
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Tapon N, Hall A. Rho, rac, and cdc42 GTPases regulate the organization of the actin cytoskeleton. Curr Opin Cell Biol. 9:1997;86-92.
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Tapon, N.1
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0028961293
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Rho rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filapodia
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Nobes CD, Hall A. Rho rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filapodia. Cell. 81:1995;53-62.
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Nobes, C.D.1
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Rho- And rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: An essential role for ezrin/radixin/moesin proteins
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MacKay DJG, Esch F, Furthmayr H, Hall A. Rho- and rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: an essential role for ezrin/radixin/moesin proteins. J Cell Biol. 138:1997;927-938.
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MacKay, D.J.G.1
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Furthmayr, H.3
Hall, A.4
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0027374555
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Salmonella typhimurium induces membrane ruffling by a growth factor independent mechanisms
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Jones BD, Paterson HF, Hall F, Falkow S. Salmonella typhimurium induces membrane ruffling by a growth factor independent mechanisms. Proc Natl Acad Sci USA. 90:1993;10390-10394.
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41
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0030448437
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Requirement of cdc42 for Salmonella-induced cytostkeletal and nuclear responses
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of outstanding interest. Cells transfected with dominant negative and constitutively active forms of cdc42 were used to convincingly demonstrate that this GTPase is required for Salmonella invasion and cytoskeletal rearrangements. A more minor role for rac is suggested. In addition, infection with Salmonella results in cdc42-mediated stimulation of JNK activity, which may control mammalian gene expression involved in some aspects of Salmonella pathogenesis.
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Chen L-M, Hobbie S, Galan JE. Requirement of cdc42 for Salmonella-induced cytostkeletal and nuclear responses. of outstanding interest Science. 274:1996;2115-2118 Cells transfected with dominant negative and constitutively active forms of cdc42 were used to convincingly demonstrate that this GTPase is required for Salmonella invasion and cytoskeletal rearrangements. A more minor role for rac is suggested. In addition, infection with Salmonella results in cdc42-mediated stimulation of JNK activity, which may control mammalian gene expression involved in some aspects of Salmonella pathogenesis.
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Chen L-M1
Hobbie, S.2
Galan, J.E.3
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0026685068
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Rosenshine I, Duronio V, Finlay BB. Protein tyrosine kinase inhibitors block invasin-promoted bacterial uptake by epithelial cells. Infect Immun. 60:1992;2211-2217.
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Finlay, B.B.3
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43
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0032518818
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52 Neisseria gonorrhoeae requires a Src-like tyrosine kinase and Rac1-dependent signalling pathway
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of outstanding interest. Opsonin-independent phagocytosis of Neisseria mediated by CD66 results in activation of the Src-family kinases Hck and Fgr. The GTPase rac is also potently activated by Neisseria, and this activation correlates with increased activity of two rac targets, PAK and Jun amino-terminal kinase (JNK). Inhibition studies also suggest a role for Src family kinases and rac in the uptake of Neisseria. An impressive technical accomplishment in this work is the measurement of 'GTP loading', a direct indicator of the activation state of rac. Previous work required the use of transfected cell lines that stably overexpress rac to detect GTP loading
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52 Neisseria gonorrhoeae requires a Src-like tyrosine kinase and Rac1-dependent signalling pathway. of outstanding interest EMBO J. 17:1998;443-454 Opsonin-independent phagocytosis of Neisseria mediated by CD66 results in activation of the Src-family kinases Hck and Fgr. The GTPase rac is also potently activated by Neisseria, and this activation correlates with increased activity of two rac targets, PAK and Jun amino-terminal kinase (JNK). Inhibition studies also suggest a role for Src family kinases and rac in the uptake of Neisseria. An impressive technical accomplishment in this work is the measurement of 'GTP loading', a direct indicator of the activation state of rac. Previous work required the use of transfected cell lines that stably overexpress rac to detect GTP loading.
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Hauck, C.R.1
Meyer, T.F.2
Lang, F.3
Gulbins, E.4
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44
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0030775369
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Acidic shingomyelinase mediates entry of Neisseria gonorrhoeae into non-phagocytic cells
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of special interest. The authors combine pharmacological inhibition, genetic experiments and measurements of lipid metabolism to demonstrate that ceramide production by ASM is needed for the uptake of Neisseria by epithelial cells.
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Grassmé H, Gulbins E, Brenner B, Ferlinz K, Sandhoff K, Harzer K, Lang F, Meyer TF. Acidic shingomyelinase mediates entry of Neisseria gonorrhoeae into non-phagocytic cells. of special interest Cell. 31:1997;605-615 The authors combine pharmacological inhibition, genetic experiments and measurements of lipid metabolism to demonstrate that ceramide production by ASM is needed for the uptake of Neisseria by epithelial cells.
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Grassmé, H.1
Gulbins, E.2
Brenner, B.3
Ferlinz, K.4
Sandhoff, K.5
Harzer, K.6
Lang, F.7
Meyer, T.F.8
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Hannun YA. Functions of ceramide in coordinating cellular responses to stress. Science. 274:1996;1855-1859.
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Hannun, Y.A.1
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Intimin-dependent binding of enteropathogenic Escherichia coli to host cells triggers novel signalling events, including tyrosine phosphorylation of phospholipase C-γ1
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Kenny B, Finlay BB. Intimin-dependent binding of enteropathogenic Escherichia coli to host cells triggers novel signalling events, including tyrosine phosphorylation of phospholipase C-γ1. Infect Immun. 65:1997;2528-2536.
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Kenny, B.1
Finlay, B.B.2
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47
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0029117595
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Thrombin receptor ligation and activated rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets
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Hartwig JH, Bokoch G, Carpenter CL, Janmey PA, Taylor LA, Toker A, Stossel TP. Thrombin receptor ligation and activated rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets. Cell. 82:1995;643-653.
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Hartwig, J.H.1
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Janmey, P.A.4
Taylor, L.A.5
Toker, A.6
Stossel, T.P.7
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