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008			140505s2014 ne | s |||| 0|eng d
020			_a9789401788816
024	7		_a10.1007/978-94-017-8881-6 _2doi
040			_dES-MaUEC
050		4	_aQP551 _b.A534 2014
100	1		_aAnderluh, Gregor _eeditor literario _0Local _986346
245	1	0	_aMACPF/CDC Proteins - Agents of Defence, Attack and Invasion _cedited by Gregor Anderluh, Robert Gilbert.
260			_aDordrecht, Netherlands _bSpringer International Publishing _c2014
300			_a1 recurso en línea (XI, 329 p.) _b57 ilustraciones, 52 ilustraciones en color
336			_aTexto (visual) _btxt _2rdacontent
337			_aelectrónico _bc _2rdamedia
338			_arecurso electrónico _bcr _2rdacarrier
490	0		_aSubcellular Biochemistry _x0306-0225 _v80
505	0		_aPart I: Overview of MACPF/CDCs -- Introduction: Brief Historical Overview -- Distribution of MACPF/CDC proteins -- Evolution of the Complement System -- Part II: Structures of MACPF/CDCs -- Structural Features of Cholesterol Dependent Cytolysins and Comparison to other MACPF-domain containing proteins -- Perfringolysin O Structure and Mechanism of Pore Formation as a Paradigm for Cholesterol-Dependent Cytolysins -- Structural Biology of the Membrane Attack Complex -- Part III: Functional aspect -- Â?mbrane Interactions and Cellular Effects of MACPF/CDC Proteins -- The Biology of Pneumolysin -- Multifaceted Activity of Listeriolysin O, the Cholesterol-Dependent Cytolysin of Listeria monocytogenes -- Perforin - a Key Pore-Forming Protein for Immune Control of Viruses and Cancer -- Perforin and Human Diseases -- The role of MACPF Proteins in the Biology of Malaria and other Apicomplexan Parasites -- Chlamydial MACPF Protein CT153 -- Fungal MACPF-Like Proteins and Aegerolysins: Bi-Component Pore-Forming Proteins? -- Fluorescence Imaging of MACPF/CDC Proteins: New Techniques and Their Application.
520			_aThis book focusses on evolutionary, structural and functional aspects of pore-forming proteins, bringing together prominent researchers in the fields of structural biology and cellular and biophysical techniques. The focus is on the MACPF/CDC protein superfamily that was originally discovered because of unexpected structural similarity between a domain present in bacterial cholesterol-dependent cytolysins (CDC) and proteins of the membrane attack complex/perforin (MACPF) family. Members of the MACPF/CDC superfamily are crucial for many biological processes, being efficient agents of development, defence, attack and invasion of cells and tissues. However, their best-known role is in bacterial pathogenesis and the proper functioning of the vertebrate immune system, via formation of transmembrane pores in target cell membranes. The book contains chapters on the distribution of MACPF/CDC proteins and on aspects of their evolution and structural properties, the similarities between different superfamily members and functional properties of some of the best known examples. The book also contains an overview of biophysical approaches that may be used in the future to provide further insights into how these interesting proteins function. Â
650		7	_2embne _aProteínas _9139861
700	1		_aGilbert, Robert _eeditor literario _921303 _0comprobar BNE19973429019
856	4	0	_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://link.springer.com/book/10.1007/978-94-017-8881-6 _zAcceso a este recurso digital (usuarios Universidad Europea de Madrid)
901			_ai9789401788816
907			_a.b1282558x _b10-10-17 _c01-10-14
942			_2lcc _cLE
945			_aQP551 .A534 2014 EB _g1 _ieBOOK _j0 _lmae _o- _pEUR0.00 _q- _r- _sb _t15 _u0 _v0 _w0 _x0 _y.i11554794 _z06-04-17
988			_aEBSPRINGER
998			_am _a_alco _a_vill _b - - _cm _dz _e- _feng _gne _h0