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001			81405
003			ES-MaUEC
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007			cr nn 008mamaa
008			150706s2015 gw | s |||| 0|eng d
020			_a9783319173443
024	7		_a10.1007/978-3-319-17344-3 _2doi
050		4	_aQP751 _b.L575 2015
245	1	0	_aLipids in Protein Misfolding _cedited by Olga Gursky.
260			_aCham, Switzerland _bSpringer _c2015
300			_a1 recurso en línea (XIII, 260 páginas) _b83 ilustraciones, 57 ilustraciones en color
336			_aTexto _btxt _2rdacontent
337			_aelectrónico _bc _2rdamedia
338			_arecurso electrónico _bcr _2rdacarrier
490	0		_aAdvances in Experimental Medicine and Biology _x0065-2598 _v855
505	0		_aRole of Lipids in Folding, Misfolding and Function of Integral Membrane Proteins -- ProteinÂ{uDA73}sfolding in Lipid-Mimetic Environments.-Â{uCA70}pids in Amyloid-β Processing, Aggregation, and Toxicity -- Role of Cholesterol and Phospholipids in Amylin Misfolding, Aggregation and Etiology of Islet Amyloidosis -- Stability, Oligomerization, and Amyloidogenicity of Apo Serum Amyloid A -- Interactions of Lipid Membranes with Fibrillar Protein Aggregates -- The Role of Lipid in Misfolding and Amyloid Fibril Formation by Apolipoprotein C-II -- Amyloid-Forming Properties of Human Apolipoproteins: Sequence Analyses and Structural Insights -- Computational Approaches to Identification of Aggregation Sites and the Mechanism of Amyloid Growth -- Role of Syndecans in Lipid Metabolism and Human Diseases.
520	3		_aThis book addresses molecular mechanisms of protein misfolding and the role of lipids and related molecules in these complex processes. The focus is on the biophysical and structural studies of proteins that are involved in major human disorders such as Alzheimerâ€{u3824}isease, systemic amyloidoses, diabetes II, inflammation and atherosclerosis. Misfolding often results from protein mutations or modifications. Misfolding of membrane proteins can cause topological changes that target the proteins for degradation. Misfolding of soluble globular proteins and peptides converts them into β-sheet-rich aggregates and amyloid fibrils. This process can disrupt the structural integrity of the lipid membranes and thereby contribute to amyloid toxicity. In turn, lipids and lipid-associated molecules such as apolipoproteins and heparan sulfate proteoglycans, which are ubiquitous constituents of amyloid plaques, can influence protein misfolding via diverse mechanisms that are addressed in this book. The book features chapters describing the role of lipids in the misfolding of a wide range of proteins, including small peptides, globular proteins, lipid surface-binding proteins, and integral membrane proteins. The role of individual lipid molecules, lipid surfaces, and the membrane field is addressed, including specific and non-specific interactions with protein oligomers and mature fibrils. Distinct effects of various lipids on the nucleation and growth of amyloid fibrils are discussed. Modern computational approaches to the analysis of amyloid formation are addressed.The book should be useful to experts in the field but is also accessible to novices.
710	2		_aSpringerLink (Online service) _0Local _9106996
942			_2lcc _cLE
988			_aEBOOK, EBSPRINGER, asignarmaterias_11febrero
650		0	_9668476 _aQuímica bioorgánica _0
650		7	_aProteínas _0 _2embne _9139861
650	2	7	_aProteínas _xEstructura _0 _2embne _9669891
700	1		_aGursky, Olga _eeditor literario _993805 _0Local
856	4	0	_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://link.springer.com/book/10.1007/978-3-319-17344-3 _zAcceso a este recurso digital (usuarios Universidad Europea de Madrid)
907			_a.b12899951 _b10-10-17 _c18-01-16
998			_am _a_alco _a_vill _b - - _cm _dz _e- _feng _ggw _h0
945			_aQP751 .L575 2015 EB _g1 _ieBOOK _j0 _lmae _o- _pEUR0.00 _q- _r- _sb _t15 _u0 _v0 _w0 _x0 _y.i11569578 _z06-04-17
999			_c81405 _d81405 _x1