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008			130328s2013 gw | s |||| 0|eng d
020			_a9783642354915
024	7		_a10.1007/978-3-642-35491-5 _2doi
040			_dES-MaUEC
050		4	_aQR502 _b.J835 2013
100	1		_aJucker, Mathias. _eeditor literario _985429 _0Local
245	1	0	_aProteopathic Seeds and Neurodegenerative Diseases _cedited by Mathias Jucker, Yves Christen.
260			_aBerlin, Heidelberg _bSpringer International Publishing _c2013
300			_a1 recurso en línea (XI, 155 p.) _b36 ilustraciones, 30 ilustraciones en color
336			_aTexto (visual) _btxt _2rdacontent
337			_aelectrónico _bc _2rdamedia
338			_arecurso electrónico _bcr _2rdacarrier
490	0		_aResearch and Perspectives in Alzheimer's Disease _x0945-6066
505	0		_aPreface -- Widening Spectrum of Prions Causing Neurodegenerative Diseases (Stanley B. Prusiner).-Â{u2B41}myloid Fibril Structures, In Vitro and In Vivo (Robert Tycko).-Â{u3D32}ucture-Activity Relationship of Amyloids (Jason Greenwald and Roland Riek).-Â{u3965}ding and Cross-seeding in Amyloid Diseases (Per Westermark and Gunilla T. Westermark).-Â{u4A25} Prion-like Aspect of Alzheimer Pathology (Sarah K. Fritschi, Bahareh Eftekharzadeh, Giusi Manfredi, Tsuyoshi Hamaguchi, GÃœtz Heilbronner, Amudha Nagarathinam, Franziska Langer, Yvonne S. Eisele, Lary Walker, Mathias Jucker).-Â{u1B79}yloid-β Transmissibility (Duran-Aniotz C, Morales R, Moreno-Gonzalez I, Soto C).-Â{u0CA9}on-like Properties of Assembled Tau Protein (Florence Clavaguera, Markus Tolnay, and Michel Goedert).-Â{u18E3}cumulating Evidence Suggests that ParkinsonÂś Disease is a Prion-like Disorder -- Nolwen L. Rey, Elodie Angot, Christopher Dunning, Jennifer A. Steiner, Patrik Brundin).-Â{u0CAF}pagation and Replication of Misfolded SOD1: Implications for Amyotrophic Lateral Sclerosis (Anne Bertolotti) -- Development of Drugs that Target Proteopathic Seeds Will Require Measurement of Drug Mechanism in Human BrainÂ{u8425}ter T. Lansbury).-Â{u4A25} Role of Functional Prions in the Persistence of Memory Storage (Eric R. Kandel, Irina Derkatch, Elias Pavlopoulos) -- Subject Index.
520			_aThe misfolding and aggregation of specific proteins is an early and obligatory event in many of the age-related neurodegenerative diseases of humans, and appears to occur many years before the onset of clinical symptoms. The initial cause of this pathogenic cascade and the means whereby disease spreads through the nervous system, remain uncertain. A recent surge of research, first instigated by pathologic similarities between prion disease and Alzheimerâ€{u3824}isease, has increasingly implicated corruptive protein templating, or seeding, as a prime factor in the neurodegenerative process. The prion-like corruption of proteins also characterizes such clinically and etiologically diverse neurological disorders as Parkinsonâ€{u3824}isease, Huntingtonâ€{u3824}isease, amyotrophic lateral sclerosis, and frontotemporal lobar degeneration. Understanding the misfolding, aggregation, trafficking and pathogenicity of affected proteins thus could reveal universal principles and common therapeutic targets for some of the most devastating and intractable human brain disorders.
650		7	_2embne _9413113 _aVirología
700	1		_aChristen, Yves _eeditor literario _919362 _0comprobar BNE19912857697
856	4	0	_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://link.springer.com/book/10.1007/978-3-642-35491-5 _zAcceso a este recurso digital (usuarios Universidad Europea de Madrid)
907			_a.b12820714 _b10-10-17 _c01-10-14
942			_2lcc _cLE
945			_aQR502 .J835 2013 EB _g1 _ieBOOK _j0 _lmae _o- _pEUR0.00 _q- _r- _sb _t15 _u0 _v0 _w0 _x0 _y.i11549920 _z06-04-17
988			_aEBSPRINGER
998			_am _a_alco _a_vill _b - - _cm _dz _e- _feng _ggw _h0