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007			cr nn 008mamaa
008			130919s2014 ne | s |||| 0|eng d
020			_a9789400774384
024	7		_a10.1007/978-94-007-7438-4 _2doi
040			_dES-MaUEC
050		4	_aQR201.M3 _bS566 2014
100	1		_aShonhai, Addmore. _eeditor literario _986238 _0Local
245	1	0	_aHeat Shock Proteins of Malaria _cedited by Addmore Shonhai, Gregory L. Blatch.
260			_aDordrecht, Netherlands _bSpringer International Publishing _c2014
300			_a1 recurso en línea (VIII, 223 p.) _b35 ilustraciones, 33 ilustraciones en color
336			_aTexto (visual) _btxt _2rdacontent
337			_aelectrónico _bc _2rdamedia
338			_arecurso electrónico _bcr _2rdacarrier
505	0		_aIntroduction: The importance of molecular chaperones in survival and pathogenesis of the malaria parasite Plasmodium falciparum -- General structural and functional features of molecular chaperones -- The role of Hsp70s in the development and pathogenicity of Plasmodium species -- Role of the Hsp40 family of proteins in the survival and pathogenesis of the malaria parasite -- Role of Hsp90 in Plasmodium falciparum malaria -- The role of parasite heat shock proteins in protein trafficking and host cell remodeling -- Role of heat shock proteins in immune modulation in malaria -- Establishment of Plasmodium falciparum extracellular compartments in its host erythrocyte -- Chaperones and Proteases of Plasmodium falciparum -- Heat shock proteins as targets for novel anti-malarial drugs -- What do we know, what do we not know, and what should the future focus be?.
520			_aThis book describes the role of heat shock proteins in the life cycle of malaria parasites. The work includes a general introduction on the structural and functional features of heat shock proteins. The main focus is on the role of heat shock protein families from Plasmodium falciparum, their role in protein folding and in the development of malaria pathology. The functions of individual families of heat shock proteins from plasmodium species and their cooperation in functional networks is described. Subcellular and extracellular organelles such as the apicoplast and the Maurerâ€{u3803}lefts which are associated with plasmodium species, are discussed in detail. The role of heat shock proteins in the development and function of these organelles structures are highlighted. Although conceding that heat shock proteins may not be ideal antimalarial drug targets, prospects of targeting heat shock proteins in antimalarial drug discovery either directly and/or in combination therapies are explored.
650		7	_2embne _aPaludismo _9672093
700			_aBlatch, Gregory Lloyd _eeditor literario _0Local _993629
856	4	0	_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://link.springer.com/book/10.1007/978-94-007-7438-4 _zAcceso a este recurso digital (usuarios Universidad Europea de Madrid)
907			_a.b1282494x _b10-10-17 _c01-10-14
942			_2lcc _cLE
945			_aQR201.M3 S566 2014 EB _g1 _ieBOOK _j0 _lmae _o- _pEUR0.00 _q- _r- _sb _t15 _u0 _v0 _w0 _x0 _y.i11554150 _z06-04-17
988			_aEBSPRINGER
998			_am _a_alco _a_vill _b - - _cm _dz _e- _feng _gne _h0