000 03321nam a22003855i 4500
001 286201
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008 150903s2010 xxu| o |||| 0|eng d
020 _a9781441963277
_99781441963277
024 7 _a10.1007/9781441963277
_2doi
035 _avtls000338632
039 9 _a201509030326
_bVLOAD
_c201404300348
_dVLOAD
_y201402060915
_zstaff
040 _aMX-SnUAN
_bspa
_cMX-SnUAN
_erda
050 4 _aR-RZ
100 1 _aAnderluh, Gregor.
_eeditor.
_9314731
245 1 0 _aProteins Membrane Binding and Pore Formation /
_cedited by Gregor Anderluh, Jeremy Lakey.
264 1 _aNew York, NY :
_bSpringer New York,
_c2010.
300 _axviii, 150 páginas 46 ilustraciones, 3 ilustraciones en color.
_brecurso en línea.
336 _atexto
_btxt
_2rdacontent
337 _acomputadora
_bc
_2rdamedia
338 _arecurso en línea
_bcr
_2rdacarrier
347 _aarchivo de texto
_bPDF
_2rda
490 0 _aAdvances in Experimental Medicine and Biology,
_x0065-2598 ;
_v677
500 _aSpringer eBooks
505 0 _aEnergetics of Peptide and Protein Binding to Lipid Membranes -- Membrane Association and Pore Formation by Alpha-Helical Peptides -- Role of Membrane Lipids for the Activity of Pore Forming Peptides and Proteins -- Cholesterol-Dependent Cytolysins -- Laetiporus sulphureus Lectin and Aerolysin Protein Family -- Interfacial Interactions of Pore-Forming Colicins -- Permeabilization of the Outer Mitochondrial Membrane by Bcl-2 Proteins -- Molecular Mechanism of Sphingomyelin-Specific Membrane Binding and Pore Formation by Actinoporins -- Hemolysin E (HlyE, ClyA, SheA) and Related Toxins -- Pore formation by Cry toxins -- Role of Heparan Sulfates and Glycosphingolipids in the Pore Formation of Basic Polypeptides of Cobra Cardiotoxin -- Amyloid Peptide Pores and the Beta Sheet Conformation.
520 _aThere are currently only two structures of pores available, of ?-toxin from Staphylococcus aureus and hemolysin E from Escherichia coli. So what we know about these proteins was obtained over many years of intense experimentation. We have nevertheless, in the last couple of years, witnessed a significant rise in structural information on the soluble forms of pore-forming proteins. Surprisingly, many unexpected similarities with other proteins were noted, despite extremely low or insignificant sequence similarity. It appears that lipid membrane binding and formation of transmembrane channels is achieved in many cases by a limited repertoire of structures. This book describes how several of the important pore forming toxin families achieve membrane binding and which structural elements are used for formation of transmembrane pores. Our contributors have thus provided the means for a comparative analysis of several unrelated families.
590 _aPara consulta fuera de la UANL se requiere clave de acceso remoto.
700 1 _aLakey, Jeremy.
_eeditor.
_9314732
710 2 _aSpringerLink (Servicio en línea)
_9299170
776 0 8 _iEdición impresa:
_z9781441963260
856 4 0 _uhttp://remoto.dgb.uanl.mx/login?url=http://dx.doi.org/10.1007/978-1-4419-6327-7
_zConectar a Springer E-Books (Para consulta externa se requiere previa autentificación en Biblioteca Digital UANL)
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999 _c286201
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