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020			_a3319500473 _q(electronic bk.)
020			_a9783319500478 _q(electronic bk.)
020			_z3319500465
020			_z9783319500461 _q(print)
035			_a(OCoLC)971891169 _z(OCoLC)972265602 _z(OCoLC)972475641 _z(OCoLC)972620737 _z(OCoLC)972844697 _z(OCoLC)972993309 _z(OCoLC)973114394 _z(OCoLC)985057613 _z(OCoLC)1005822901
040			_aN$T _cN$T _dEBLCP _dGW5XE _dIDEBK _dN$T _dYDX _dOCLCF _dDKU _dCOO _dUPM _dSCB _dIOG _dVT2 _dMERER _dESU _dZ5A _dOCLCO _dOCLCQ _dOCLCO _dJBG _dIAD _dOCLCO _dICW _dOCLCO _dICN _dOCLCQ _dOCLCO _dOTZ _dOCLCQ _dOCLCO _dU3W _dES-MaUEC _bspa
050		4	_aQP552.A27 _bT443 2017 EB
245	0	4	_aThe actin cytoskeleton and bacterial infection _cHans Georg Mannherz, editor.
264		1	_aCham, Switzerland _bSpringer _c2017
300			_a1 recurso en línea (x, 242 páginas) _bilustraciones
336			_aTexto _btxt _2rdacontent
337			_aelectrónico _bc _2rdamedia
338			_arecurso electrónico _bcr _2rdacarrier
347			_atext file _bPDF _2rda
490	0		_aCurrent topics in microbiology and immunology _x0070-217X _vvolume 399
500			_aSpringerLink _bSpringer Biomedical and Life Sciences eBooks 2017 English+International
505	0		_aPreface; Contents; 45 Actin: Structure, Function, Dynamics, and Interactions with Bacterial Toxins; Abstract; 1 Introduction; 2 Actin; 2.1 Actin Structure; 2.2 Binding Sites on Actin for Actin-Binding Proteins; 2.3 Filamentous (F- ) Actin; 2.4 Actin Dynamics: Polymerization Behaviour; 3 Interactions with Actin-Binding Proteins (ABPs); 3.1 G-actin-Sequestering Proteins; 3.2 F-actin-Nucleating Proteins and Their Nucleation-Promoting Factors (NPFs); 3.3 F-actin-Elongating Proteins; 3.4 F-actin-Capping Proteins; 3.5 F-actin-Bundling and Cross-linking Proteins; 3.6 F-actin-Stabilizing Proteins.
505	8		_a3.2 Impaired Interactions of Thr148-ADP-Ribosylated Actin with a Number of Actin-Binding Proteins4 ADP-Ribosylation of Rho GTPases by Photorhabdus luminescens TccC5; 5 Conclusions; References; 23 Comparative Studies of Actin- and Rho-Specific ADP-Ribosylating Toxins: Insight from Structural Biology; Abstract; 1 Introduction; 2 Functional and Structural Studies of Actin- and Rho-Specific ADP-Ribosylating Toxins; 3 Comparative Studies of Substrate Recognition by Actin- and Rho-Specific ARTs; 4 Cell Entry Mechanism Between Actin- and Rho-Specific ARTs; 5 Conclusion; Acknowledgements; References.
505	8		_a3.7 F-actin-Severing Proteins3.8 Regulation of the Activity and Localization of ABPs; 4 Examples of Bacterial Proteins that Subvert the Host Actin Cytoskeleton; 4.1 Direct Interactions of Bacterial Effectors with Actin; 4.1.1 Direct Modifications of G-actin; 4.1.2 F-actin Dynamics Modifying Bacterial Proteins; 4.2 Manipulation of Actin-Binding Proteins by Bacterial Effectors; 4.2.1 Recruitment and Regulation of the Host F-actin Nucleation Machinery; 4.2.2 Interactions of Bacterial Effectors with Actin-Binding Proteins (ABPs).
505	8		_a4.1 Effects of Actin-Depolymerizing Toxins on Microtubules4.2 Mechanisms Involved in Protrusion Formation: A Role for Septins; 4.3 Role and Functions of Toxin-Induced Cell Protrusions; 4.3.1 Re-guidance of Vesicle Traffic; 5 Conclusions; References; 43 Photorhabdus luminescens Toxins TccC3 and TccC5 Affect the Interaction of Actin with Actin-Binding Proteins Essential for Treadmilling; Abstract; 1 Introduction; 2 Life Cycle and Tc Toxins of Photorhabdus luminescens; 3 ADP-Ribosylation of Actin by P. luminescens TccC3; 3.1 Thr148-ADP-Ribosylation Promotes Actin Polymerization.
505	8		_a4.2.3 Manipulation of Host ABP Regulation: Rho GTPases, Kinases, and Phospholipids as Bacterial Targets5 Conclusions; References; 25 Formation of Nanotube-Like Protrusions, Regulation of Septin Organization and Re-guidance of Vesicle Traffic by Depolymerization of the Actin Cytoskeleton Induced by Binary Bacterial Protein Toxins; Abstract; 1 Introduction; 2 Actin-Depolymerizing Toxins; 2.1 Structure of Binary Toxins; 2.2 Receptors and Uptake; 3 Modification of Actin by ADP-Ribosylating Toxins; 4 Cellular Consequences of the ADP-Ribosylation of Actin in Arginine-177.
520	3		_aThis 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 ℓ́ℓact on actinℓ́ℓ 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		7	_aActínidos _2embne _0(OCoLC)fst00796140 _0 _9677518
700	1		_aMannherz, Hans Georg, _eeditor literario
856	4	0	_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=http://link.springer.com/10.1007/978-3-319-50047-8 _zAcceso a este recurso digital (usuarios Universidad Europea de Madrid)
988			_aEBOOK, asignarmaterias, EBSPRINGER_2017B
998			_b02/2018 _dz _e- _zSI
999			_c95348 _d95348 _x1