Thiol-activated cytolysins: structure, function and role in pathogenesis
Members of the thiol-activated family of cytolysins are involved in the mechanism of pathogenesis of a number of Gram-positive species. While they are pore-forming toxins, their major pathogenic effects may be more subtle than simple lysis of host cells, and may include interference with immune cell...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Billington, Stephen J. [verfasserIn] Jost, B.Helen [verfasserIn] Songer, J.Glenn [verfasserIn] |
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| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 2000 |
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| Schlagwörter: |
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| Umfang: |
Online-Ressource |
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| Reproduktion: |
2006 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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| Übergeordnetes Werk: |
In: FEMS microbiology letters - Federation of European Microbiological Societies ; GKD-ID: 114439X, Oxford [u.a.] : Wiley-Blackwell, 1977, 182(2000), 2, Seite 0 |
| Übergeordnetes Werk: |
volume:182 ; year:2000 ; number:2 ; pages:0 |
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| DOI / URN: |
10.1111/j.1574-6968.2000.tb08895.x |
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| 520 | |a Members of the thiol-activated family of cytolysins are involved in the mechanism of pathogenesis of a number of Gram-positive species. While they are pore-forming toxins, their major pathogenic effects may be more subtle than simple lysis of host cells, and may include interference with immune cell function and cytokine induction. Crystal structure, electron microscopy, mutagenesis and antibody binding studies have led to the modeling of a novel mechanism of pore formation, encompassing membrane-binding, membrane insertion and oligomerization. Despite their designation as thiol-activated cytolysins, it is now clear that thiol activation is not an important property of this group of toxins. | ||
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10.1111/j.1574-6968.2000.tb08895.x doi (DE-627)NLEJ242901913 DE-627 ger DE-627 rakwb Billington, Stephen J. verfasserin aut Thiol-activated cytolysins: structure, function and role in pathogenesis Oxford, UK Blackwell Publishing Ltd 2000 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Members of the thiol-activated family of cytolysins are involved in the mechanism of pathogenesis of a number of Gram-positive species. While they are pore-forming toxins, their major pathogenic effects may be more subtle than simple lysis of host cells, and may include interference with immune cell function and cytokine induction. Crystal structure, electron microscopy, mutagenesis and antibody binding studies have led to the modeling of a novel mechanism of pore formation, encompassing membrane-binding, membrane insertion and oligomerization. Despite their designation as thiol-activated cytolysins, it is now clear that thiol activation is not an important property of this group of toxins. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Pathogenesis Jost, B.Helen verfasserin aut Songer, J.Glenn verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 182(2000), 2, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:182 year:2000 number:2 pages:0 http://dx.doi.org/10.1111/j.1574-6968.2000.tb08895.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 182 2000 2 0 |
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10.1111/j.1574-6968.2000.tb08895.x doi (DE-627)NLEJ242901913 DE-627 ger DE-627 rakwb Billington, Stephen J. verfasserin aut Thiol-activated cytolysins: structure, function and role in pathogenesis Oxford, UK Blackwell Publishing Ltd 2000 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Members of the thiol-activated family of cytolysins are involved in the mechanism of pathogenesis of a number of Gram-positive species. While they are pore-forming toxins, their major pathogenic effects may be more subtle than simple lysis of host cells, and may include interference with immune cell function and cytokine induction. Crystal structure, electron microscopy, mutagenesis and antibody binding studies have led to the modeling of a novel mechanism of pore formation, encompassing membrane-binding, membrane insertion and oligomerization. Despite their designation as thiol-activated cytolysins, it is now clear that thiol activation is not an important property of this group of toxins. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Pathogenesis Jost, B.Helen verfasserin aut Songer, J.Glenn verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 182(2000), 2, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:182 year:2000 number:2 pages:0 http://dx.doi.org/10.1111/j.1574-6968.2000.tb08895.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 182 2000 2 0 |
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10.1111/j.1574-6968.2000.tb08895.x doi (DE-627)NLEJ242901913 DE-627 ger DE-627 rakwb Billington, Stephen J. verfasserin aut Thiol-activated cytolysins: structure, function and role in pathogenesis Oxford, UK Blackwell Publishing Ltd 2000 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Members of the thiol-activated family of cytolysins are involved in the mechanism of pathogenesis of a number of Gram-positive species. While they are pore-forming toxins, their major pathogenic effects may be more subtle than simple lysis of host cells, and may include interference with immune cell function and cytokine induction. Crystal structure, electron microscopy, mutagenesis and antibody binding studies have led to the modeling of a novel mechanism of pore formation, encompassing membrane-binding, membrane insertion and oligomerization. Despite their designation as thiol-activated cytolysins, it is now clear that thiol activation is not an important property of this group of toxins. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Pathogenesis Jost, B.Helen verfasserin aut Songer, J.Glenn verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 182(2000), 2, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:182 year:2000 number:2 pages:0 http://dx.doi.org/10.1111/j.1574-6968.2000.tb08895.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 182 2000 2 0 |
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10.1111/j.1574-6968.2000.tb08895.x doi (DE-627)NLEJ242901913 DE-627 ger DE-627 rakwb Billington, Stephen J. verfasserin aut Thiol-activated cytolysins: structure, function and role in pathogenesis Oxford, UK Blackwell Publishing Ltd 2000 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Members of the thiol-activated family of cytolysins are involved in the mechanism of pathogenesis of a number of Gram-positive species. While they are pore-forming toxins, their major pathogenic effects may be more subtle than simple lysis of host cells, and may include interference with immune cell function and cytokine induction. Crystal structure, electron microscopy, mutagenesis and antibody binding studies have led to the modeling of a novel mechanism of pore formation, encompassing membrane-binding, membrane insertion and oligomerization. Despite their designation as thiol-activated cytolysins, it is now clear that thiol activation is not an important property of this group of toxins. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Pathogenesis Jost, B.Helen verfasserin aut Songer, J.Glenn verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 182(2000), 2, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:182 year:2000 number:2 pages:0 http://dx.doi.org/10.1111/j.1574-6968.2000.tb08895.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 182 2000 2 0 |
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10.1111/j.1574-6968.2000.tb08895.x doi (DE-627)NLEJ242901913 DE-627 ger DE-627 rakwb Billington, Stephen J. verfasserin aut Thiol-activated cytolysins: structure, function and role in pathogenesis Oxford, UK Blackwell Publishing Ltd 2000 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Members of the thiol-activated family of cytolysins are involved in the mechanism of pathogenesis of a number of Gram-positive species. While they are pore-forming toxins, their major pathogenic effects may be more subtle than simple lysis of host cells, and may include interference with immune cell function and cytokine induction. Crystal structure, electron microscopy, mutagenesis and antibody binding studies have led to the modeling of a novel mechanism of pore formation, encompassing membrane-binding, membrane insertion and oligomerization. Despite their designation as thiol-activated cytolysins, it is now clear that thiol activation is not an important property of this group of toxins. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Pathogenesis Jost, B.Helen verfasserin aut Songer, J.Glenn verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 182(2000), 2, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:182 year:2000 number:2 pages:0 http://dx.doi.org/10.1111/j.1574-6968.2000.tb08895.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 182 2000 2 0 |
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Members of the thiol-activated family of cytolysins are involved in the mechanism of pathogenesis of a number of Gram-positive species. While they are pore-forming toxins, their major pathogenic effects may be more subtle than simple lysis of host cells, and may include interference with immune cell function and cytokine induction. Crystal structure, electron microscopy, mutagenesis and antibody binding studies have led to the modeling of a novel mechanism of pore formation, encompassing membrane-binding, membrane insertion and oligomerization. Despite their designation as thiol-activated cytolysins, it is now clear that thiol activation is not an important property of this group of toxins. |
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Members of the thiol-activated family of cytolysins are involved in the mechanism of pathogenesis of a number of Gram-positive species. While they are pore-forming toxins, their major pathogenic effects may be more subtle than simple lysis of host cells, and may include interference with immune cell function and cytokine induction. Crystal structure, electron microscopy, mutagenesis and antibody binding studies have led to the modeling of a novel mechanism of pore formation, encompassing membrane-binding, membrane insertion and oligomerization. Despite their designation as thiol-activated cytolysins, it is now clear that thiol activation is not an important property of this group of toxins. |
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Members of the thiol-activated family of cytolysins are involved in the mechanism of pathogenesis of a number of Gram-positive species. While they are pore-forming toxins, their major pathogenic effects may be more subtle than simple lysis of host cells, and may include interference with immune cell function and cytokine induction. Crystal structure, electron microscopy, mutagenesis and antibody binding studies have led to the modeling of a novel mechanism of pore formation, encompassing membrane-binding, membrane insertion and oligomerization. Despite their designation as thiol-activated cytolysins, it is now clear that thiol activation is not an important property of this group of toxins. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ242901913</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707165730.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">120427s2000 xx |||||o 00| ||und c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1111/j.1574-6968.2000.tb08895.x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ242901913</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Billington, Stephen J.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Thiol-activated cytolysins: structure, function and role in pathogenesis</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Oxford, UK</subfield><subfield code="b">Blackwell Publishing Ltd</subfield><subfield code="c">2000</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Members of the thiol-activated family of cytolysins are involved in the mechanism of pathogenesis of a number of Gram-positive species. While they are pore-forming toxins, their major pathogenic effects may be more subtle than simple lysis of host cells, and may include interference with immune cell function and cytokine induction. Crystal structure, electron microscopy, mutagenesis and antibody binding studies have led to the modeling of a novel mechanism of pore formation, encompassing membrane-binding, membrane insertion and oligomerization. Despite their designation as thiol-activated cytolysins, it is now clear that thiol activation is not an important property of this group of toxins.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="d">2006</subfield><subfield code="f">Blackwell Publishing Journal Backfiles 1879-2005</subfield><subfield code="7">|2006||||||||||</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Pathogenesis</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Jost, B.Helen</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Songer, J.Glenn</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">In</subfield><subfield code="a">Federation of European Microbiological Societies ; GKD-ID: 114439X</subfield><subfield code="t">FEMS microbiology letters</subfield><subfield code="d">Oxford [u.a.] : Wiley-Blackwell, 1977</subfield><subfield code="g">182(2000), 2, Seite 0</subfield><subfield code="h">Online-Ressource</subfield><subfield code="w">(DE-627)NLEJ243927053</subfield><subfield code="w">(DE-600)1501716-3</subfield><subfield code="x">1574-6968</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:182</subfield><subfield code="g">year:2000</subfield><subfield code="g">number:2</subfield><subfield code="g">pages:0</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1111/j.1574-6968.2000.tb08895.x</subfield><subfield code="q">text/html</subfield><subfield code="x">Verlag</subfield><subfield code="z">Deutschlandweit zugänglich</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-DJB</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">182</subfield><subfield code="j">2000</subfield><subfield code="e">2</subfield><subfield code="h">0</subfield></datafield></record></collection>
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