語系:
繁體中文
English
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
The actin cytoskeleton and bacterial...
~
Mannherz, Hans Georg.
FindBook
Google Book
Amazon
博客來
The actin cytoskeleton and bacterial infection
紀錄類型:
書目-電子資源 : Monograph/item
正題名/作者:
The actin cytoskeleton and bacterial infection/ edited by Hans Georg Mannherz.
其他作者:
Mannherz, Hans Georg.
出版者:
Cham :Springer International Publishing : : 2017.,
面頁冊數:
x, 242 p. :ill., digital ;24 cm.
內容註:
Actin structure and dynamics -- Influence of binary actin-depolymerizing toxins on the microtubule system -- ADP-ribosylation of actin by Photorhabdus luminescens TccC3 inhibits interaction with actin binding proteins essential for treadmilling -- Pathogenic mechanisms of actin cross-linking toxins - peeling away the layers -- New concepts on bacterial effectors targeting Rho GTPases -- Interaction of bacterial ADPribosyltransferases with actin -- Yersinia's ways to activate and inactivate actin rearrangements in host cells -- The role of formins in phagocytosis of Borrelia by macrophages.
Contained By:
Springer eBooks
標題:
Actin. -
電子資源:
http://dx.doi.org/10.1007/978-3-319-50047-8
ISBN:
9783319500478
The actin cytoskeleton and bacterial infection
The actin cytoskeleton and bacterial infection
[electronic resource] /edited by Hans Georg Mannherz. - Cham :Springer International Publishing :2017. - x, 242 p. :ill., digital ;24 cm. - Current topics in microbiology and immunology,v.3990070-217X ;. - Current topics in microbiology and immunology ;v.399..
Actin structure and dynamics -- Influence of binary actin-depolymerizing toxins on the microtubule system -- ADP-ribosylation of actin by Photorhabdus luminescens TccC3 inhibits interaction with actin binding proteins essential for treadmilling -- Pathogenic mechanisms of actin cross-linking toxins - peeling away the layers -- New concepts on bacterial effectors targeting Rho GTPases -- Interaction of bacterial ADPribosyltransferases with actin -- Yersinia's ways to activate and inactivate actin rearrangements in host cells -- The role of formins in phagocytosis of Borrelia by macrophages.
This volume describes the mechanisms which bacteria have created to secure their survival, proliferation and dissemination by subverting the actin cytoskeleton of host cells. Bacteria have developed a veritable arsenal of toxins, effector proteins and virulence factors that allow them to modify the properties of the intracellular actin cytoskeleton for their own purposes. Bacterial factors either modify actin directly as the main component of this part of the cytoskeleton or functionally subvert regulatory or signalling proteins terminating at the actin cytoskeleton. In short, this volume provides an overview of the various tricks bacteria have evolved to "act on actin" in order to hijack this essential host cell component for their own needs. As such, it will be of interest to scientists from many fields, as well as clinicians whose work involves infectious diseases.
ISBN: 9783319500478
Standard No.: 10.1007/978-3-319-50047-8doiSubjects--Topical Terms:
867453
Actin.
LC Class. No.: QP552.A27
Dewey Class. No.: 572.66
The actin cytoskeleton and bacterial infection
LDR
:02502nmm a2200325 a 4500
001
2089998
003
DE-He213
005
20170207130642.0
006
m d
007
cr nn 008maaau
008
171013s2017 gw s 0 eng d
020
$a
9783319500478
$q
(electronic bk.)
020
$a
9783319500461
$q
(paper)
024
7
$a
10.1007/978-3-319-50047-8
$2
doi
035
$a
978-3-319-50047-8
040
$a
GP
$c
GP
041
0
$a
eng
050
4
$a
QP552.A27
072
7
$a
MMFM
$2
bicssc
072
7
$a
MED052000
$2
bisacsh
082
0 4
$a
572.66
$2
23
090
$a
QP552.A27
$b
A188 2017
245
0 4
$a
The actin cytoskeleton and bacterial infection
$h
[electronic resource] /
$c
edited by Hans Georg Mannherz.
260
$a
Cham :
$b
Springer International Publishing :
$b
Imprint: Springer,
$c
2017.
300
$a
x, 242 p. :
$b
ill., digital ;
$c
24 cm.
490
1
$a
Current topics in microbiology and immunology,
$x
0070-217X ;
$v
v.399
505
0
$a
Actin structure and dynamics -- Influence of binary actin-depolymerizing toxins on the microtubule system -- ADP-ribosylation of actin by Photorhabdus luminescens TccC3 inhibits interaction with actin binding proteins essential for treadmilling -- Pathogenic mechanisms of actin cross-linking toxins - peeling away the layers -- New concepts on bacterial effectors targeting Rho GTPases -- Interaction of bacterial ADPribosyltransferases with actin -- Yersinia's ways to activate and inactivate actin rearrangements in host cells -- The role of formins in phagocytosis of Borrelia by macrophages.
520
$a
This volume describes the mechanisms which bacteria have created to secure their survival, proliferation and dissemination by subverting the actin cytoskeleton of host cells. Bacteria have developed a veritable arsenal of toxins, effector proteins and virulence factors that allow them to modify the properties of the intracellular actin cytoskeleton for their own purposes. Bacterial factors either modify actin directly as the main component of this part of the cytoskeleton or functionally subvert regulatory or signalling proteins terminating at the actin cytoskeleton. In short, this volume provides an overview of the various tricks bacteria have evolved to "act on actin" in order to hijack this essential host cell component for their own needs. As such, it will be of interest to scientists from many fields, as well as clinicians whose work involves infectious diseases.
650
0
$a
Actin.
$3
867453
650
0
$a
Cytoskeleton.
$3
549552
650
1 4
$a
Biomedicine.
$3
890831
650
2 4
$a
Medical Microbiology.
$3
890951
650
2 4
$a
Pharmacology/Toxicology.
$3
890953
700
1
$a
Mannherz, Hans Georg.
$3
3221140
710
2
$a
SpringerLink (Online service)
$3
836513
773
0
$t
Springer eBooks
830
0
$a
Current topics in microbiology and immunology ;
$v
v.399.
$3
3221141
856
4 0
$u
http://dx.doi.org/10.1007/978-3-319-50047-8
950
$a
Biomedical and Life Sciences (Springer-11642)
筆 0 讀者評論
館藏地:
全部
電子資源
出版年:
卷號:
館藏
1 筆 • 頁數 1 •
1
條碼號
典藏地名稱
館藏流通類別
資料類型
索書號
使用類型
借閱狀態
預約狀態
備註欄
附件
W9316170
電子資源
11.線上閱覽_V
電子書
EB QP552.A27
一般使用(Normal)
在架
0
1 筆 • 頁數 1 •
1
多媒體
評論
新增評論
分享你的心得
Export
取書館
處理中
...
變更密碼
登入