東華大學圖書館 |

語系: 繁體中文

說明(常見問題)

回圖書館首頁

手機版館藏查詢

登入

回首頁

切換: 標籤 | MARC模式 | ISBD

Uptake and trafficking of protein toxins

Barth, Holger.

FindBook

Google Book

Amazon

博客來

Uptake and trafficking of protein toxins

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Uptake and trafficking of protein toxins/ edited by Holger Barth.
其他作者:	Barth, Holger.
出版者:	Cham :Springer International Publishing : : 2017.,
面頁冊數:	vii, 256 p. :ill., digital ;24 cm.
內容註:	Two feet on the membrane: uptake of clostridial neurotoxins -- Receptors and binding structures for Clostridium difficile Toxins A and B -- Cell entry of C3 exoenzyme from Clostridium botulinum -- Receptor-binding and up-take of binary actin-ADP-ribosylating toxins -- Clostridial Binary Toxins: Basic Understandings that Include Cell-Surface Binding and an Internal "Coup de Grace" -- Host cell chaperones Hsp70/Hsp90 and peptidyl-prolyl cis/trans isomerases are required for the membrane translocation of bacterial ADP-ribosylating toxins -- Multivalent Inhibitors of Channel-Forming Bacterial Toxins -- Toxin Transport by A-B Type of Toxins in Eukaryotic Target Cells and its inhibition by Positively Charged Heterocyclic Molecules.
Contained By:	Springer eBooks
標題:	Bacterial toxins. -
電子資源:	http://dx.doi.org/10.1007/978-3-319-58893-3
ISBN:	9783319588933

Uptake and trafficking of protein toxins
Uptake and trafficking of protein toxins[electronic resource] /edited by Holger Barth. - Cham :Springer International Publishing :2017. - vii, 256 p. :ill., digital ;24 cm. - Current topics in microbiology and immunology,v.4060070-217X ;. - Current topics in microbiology and immunology ;v.406..

Two feet on the membrane: uptake of clostridial neurotoxins -- Receptors and binding structures for Clostridium difficile Toxins A and B -- Cell entry of C3 exoenzyme from Clostridium botulinum -- Receptor-binding and up-take of binary actin-ADP-ribosylating toxins -- Clostridial Binary Toxins: Basic Understandings that Include Cell-Surface Binding and an Internal "Coup de Grace" -- Host cell chaperones Hsp70/Hsp90 and peptidyl-prolyl cis/trans isomerases are required for the membrane translocation of bacterial ADP-ribosylating toxins -- Multivalent Inhibitors of Channel-Forming Bacterial Toxins -- Toxin Transport by A-B Type of Toxins in Eukaryotic Target Cells and its inhibition by Positively Charged Heterocyclic Molecules.

This volume focuses on the transport of medically relevant bacterial protein toxins into mammalian cells, and on novel pharmacological strategies to inhibit toxin uptake. The first chapters review our current understanding of the cell-surface receptors and cellular transport processes of Clostridium botulinum neurotoxins, Clostridium botulinum C3 toxin, Clostridium difficile toxins, binary clostridial enterotoxins, anthrax toxins and diphtheria toxin. In brief, specific binding/transport (B) subunits deliver the enzyme (A) subunits into the cytosol, where the latter modify their substrates, producing cytotoxic effects and the characteristic toxin-associated diseases. Key mechanisms for the transport of the A subunits from endosomes into the cytosol and the role of trans-membrane pores formed by the B subunits and host cell chaperones for this process are reviewed. The book's closing chapters focus on compounds which inhibit the transport of the A subunits from endosomes into the cytosol and therefore might lead to novel therapeutic strategies for toxin-associated diseases. These substances include pharmacological inhibitors of the host cell chaperones involved, as well as multivalent and heterocyclic molecules that specifically block the toxins' translocation channels. This volume offers an up-to-date resource for scientists.

ISBN: 9783319588933

Standard No.: 10.1007/978-3-319-58893-3doiSubjects--Topical Terms:

744146
Bacterial toxins.

LC Class. No.: QP632.B3

Dewey Class. No.: 571.957

Uptake and trafficking of protein toxins
LDR:03096nmm a2200325 a 4500 001 2112701
003 DE-He213
005 20171201202012.0
006 m d
007 cr nn 008maaau
008 180719s2017 gw s 0 eng d
020 $a 9783319588933 $q (electronic bk.)
020 $a 9783319588919 $q (paper)
024 7 $a 10.1007/978-3-319-58893-3 $2 doi
035 $a 978-3-319-58893-3
040 $a GP $c GP
041 0 $a eng
050 4 $a QP632.B3
072 7 $a MMFM $2 bicssc
072 7 $a MED052000 $2 bisacsh
082 0 4 $a 571.957 $2 23
090 $a QP632.B3 $b U71 2017
245 0 0 $a Uptake and trafficking of protein toxins $h [electronic resource] / $c edited by Holger Barth.
260 $a Cham : $b Springer International Publishing : $b Imprint: Springer, $c 2017.
300 $a vii, 256 p. : $b ill., digital ; $c 24 cm.
490 1 $a Current topics in microbiology and immunology, $x 0070-217X ; $v v.406
505 0 $a Two feet on the membrane: uptake of clostridial neurotoxins -- Receptors and binding structures for Clostridium difficile Toxins A and B -- Cell entry of C3 exoenzyme from Clostridium botulinum -- Receptor-binding and up-take of binary actin-ADP-ribosylating toxins -- Clostridial Binary Toxins: Basic Understandings that Include Cell-Surface Binding and an Internal "Coup de Grace" -- Host cell chaperones Hsp70/Hsp90 and peptidyl-prolyl cis/trans isomerases are required for the membrane translocation of bacterial ADP-ribosylating toxins -- Multivalent Inhibitors of Channel-Forming Bacterial Toxins -- Toxin Transport by A-B Type of Toxins in Eukaryotic Target Cells and its inhibition by Positively Charged Heterocyclic Molecules.
520 $a This volume focuses on the transport of medically relevant bacterial protein toxins into mammalian cells, and on novel pharmacological strategies to inhibit toxin uptake. The first chapters review our current understanding of the cell-surface receptors and cellular transport processes of Clostridium botulinum neurotoxins, Clostridium botulinum C3 toxin, Clostridium difficile toxins, binary clostridial enterotoxins, anthrax toxins and diphtheria toxin. In brief, specific binding/transport (B) subunits deliver the enzyme (A) subunits into the cytosol, where the latter modify their substrates, producing cytotoxic effects and the characteristic toxin-associated diseases. Key mechanisms for the transport of the A subunits from endosomes into the cytosol and the role of trans-membrane pores formed by the B subunits and host cell chaperones for this process are reviewed. The book's closing chapters focus on compounds which inhibit the transport of the A subunits from endosomes into the cytosol and therefore might lead to novel therapeutic strategies for toxin-associated diseases. These substances include pharmacological inhibitors of the host cell chaperones involved, as well as multivalent and heterocyclic molecules that specifically block the toxins' translocation channels. This volume offers an up-to-date resource for scientists.
650 0 $a Bacterial toxins. $3 744146
650 1 4 $a Biomedicine. $3 890831
650 2 4 $a Medical Microbiology. $3 890951
650 2 4 $a Pharmacology/Toxicology. $3 890953
650 2 4 $a Infectious Diseases. $3 894100
700 1 $a Barth, Holger. $3 3270615
710 2 $a SpringerLink (Online service) $3 836513
773 0 $t Springer eBooks
830 0 $a Current topics in microbiology and immunology ; $v v.406. $3 3270616
856 4 0 $u http://dx.doi.org/10.1007/978-3-319-58893-3
950 $a Biomedical and Life Sciences (Springer-11642)