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001			283536
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008			150903s2007 ne | o |||| 0|eng d
020			_a9781402064012 _99781402064012
024	7		_a10.1007/9781402064012 _2doi
035			_avtls000335609
039		9	_a201509030752 _bVLOAD _c201404300304 _dVLOAD _y201402041304 _zstaff
040			_aMX-SnUAN _bspa _cMX-SnUAN _erda
050		4	_aRC261-271
100	1		_aCalderwood, Stuart K. _eeditor. _9304273
245	1	0	_aHeat Shock Proteins in Cancer / _cedited by Stuart K. Calderwood, Michael Y. Sherman, Daniel R. Ciocca.
264		1	_aDordrecht : _bSpringer Netherlands, _c2007.
300			_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		_aHeat Shock Proteins ; _v2
500			_aSpringer eBooks
505	0		_aThe Hsp90 Chaperone Machinery Acts at Protein Folding Clefts to Regulate Both Signaling Protein Function and Protein Quality Control -- Implications of Heat Shock Proteins in Carcinogenesis and Cancer Progression -- HSF1: An Emerging Factor In Cancer -- Anti-apoptotic, Tumorigenic and Metastatic Potential of Hsp27 (HspB1) and ?B-crystallin (HspB5): Emerging Targets for the Development of New Anti-Cancer Therapeutic Strategies -- Heat Shock Protein-27 (Hsp-27) in Breast Cancers: Regulation of Expression and Function -- Role of Heat Shock Protein Hsp25/27 in~the~Metastatic Spread of Cancer Cells -- Heat shock chaperone mortalin and carcinogenesis -- Role of Molecular Chaperones in Cell Senescence -- Involvement of Heat Shock Proteins in Protection of Tumor Cells from Genotoxic Stresses -- Hsp70 in Tumors: Friend or Foe? -- Hsp70 and Hsp27 as pharmacological targets in apoptosis modulation for cancer therapy -- Heat Shock Protein 90: The Cancer Chaperone -- Targeting Hsp90 Function to Treat Cancer: Much More to Be Learned -- Small-molecule Hsp90 Inhibitors: Applications in Cancer and Neurodegenerative diseases -- Drugging the Hsp90 molecular chaperone machine for cancer treatment -- Cdc37 and protein kinase folding -- The Elevated Levels of Heat Shock Proteins In Cancer: A Suitable Case For Treatment? -- Hsp70-Based Anticancer Vaccines: Chaperoning The Immune Response -- Piloting of exogenous antigen into cross-presentation pathway by heat shock proteins.
520			_aHeat shock proteins are emerging as important molecules in the development of cancer and as key targets in cancer therapy. These proteins enhance the growth of cancer cells and protect tumors from treatments such as drugs or surgery. However, new drugs have recently been developed particularly those targeting heat shock protein 90. As heat shock protein 90 functions to stabilize many of the oncogenes and growth promoting proteins in cancer cells, such drugs have broad specificity in many types of cancer cell and offer the possibility of evading the development of resistance through point mutation or use of compensatory pathways. Heat shock proteins have a further property that makes them tempting targets in cancer immunotherapy. These proteins have the ability to induce an inflammatory response when released in tumors and to carry tumor antigens to antigen presenting cells. They have thus become important components of anticancer vaccines. Overall, heat shock proteins are important new targets in molecular cancer therapy and can be approached in a number of contrasting approaches to therapy.
590			_aPara consulta fuera de la UANL se requiere clave de acceso remoto.
700	1		_aSherman, Michael Y. _eeditor. _9311107
700	1		_aCiocca, Daniel R. _eeditor. _9311108
710	2		_aSpringerLink (Servicio en línea) _9299170
776	0	8	_iEdición impresa: _z9781402064005
856	4	0	_uhttp://remoto.dgb.uanl.mx/login?url=http://dx.doi.org/10.1007/978-1-4020-6401-2 _zConectar a Springer E-Books (Para consulta externa se requiere previa autentificación en Biblioteca Digital UANL)
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