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020			_a9789400747401 _99789400747401
024	7		_a10.1007/9789400747401 _2doi
035			_avtls000367349
039		9	_a201509030714 _bVLOAD _c201405070440 _dVLOAD _y201402251618 _zstaff
040			_aMX-SnUAN _bspa _cMX-SnUAN _erda
050		4	_aQP34-38
100	1		_aHenderson, Brian. _eeditor. _9355499
245	1	0	_aCellular Trafficking of Cell Stress Proteins in Health and Disease / _cedited by Brian Henderson, A. Graham Pockley.
264		1	_aDordrecht : _bSpringer Netherlands : _bImprint: Springer, _c2012.
300			_axiii, 297 páginas 28 ilustraciones, 13 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		_aHeat Shock Proteins, _x1877-1246 ; _v6
500			_aSpringer eBooks
505	0		_aPreface -- Contents -- Note on Nomenclature -- Author Addresses -- Section 1 Historical Introduction to Secreted Cell Stress Proteins as Signalling Proteins -- Discovery of the Cellular Secretion of Cell Stress Proteins -- Discovery of the Agonist Activities of Molecular Chaperones and Protein-Folding Catalysts -- Identification of Cell Stress Proteins in Biological Fluids -- Section 2 Intracellular Trafficking of Molecular Chaperones and its Consequences -- Hsp27 Phosphorylation Patterns and Cellular Consequences -- Evidence on Cholesterol-Controlled Lipid Raft Interaction of the Small Heat Shock Protein HSPB11 -- Hsp70 Chaperone Systems in Vesicular Trafficking -- Pathways of Hsp70 Release: Lessons from Cytokine Secretion -- Nucleolin: A Novel Intracellular Transporter of HSPA1A -- The Hsp90-Based Protein Trafficking System and Linkage to Protein Quality Control -- Section 3 Molecular Chaperones as Cell Surface Receptors and Receptor Ligands -- Cell Surface Molecular Chaperones and the LPS Receptor -- Hsp60: An Unexpected Cell Surface Receptor in Prokaryotes and Eukaryotes -- Pathophysiological Barriers Impeding the Delivery of Heat Shock Protein (HSP)-based Macromolecules and Nanotherapeutics to Solid Tumors -- The Chaperokine Activity of HSPA1A -- Molecular Chaperones and Scavenger Receptors: Binding and Trafficking of Molecular Chaperones by Class F and Class H Scavenger Receptors -- Grp78 (BiP): A Multifunctional Cell Surface Receptor -- Section 4 Extracellular Secretion of Molecular Chaperones in Prokaryotes and Eukaryotes -- Mycobacterium Tuberculosis Hsp60 as a Key Virulence Factor in Tuberculosis -- Hsp90 vs Conventional Growth Factors in Acute and Diabetic Wound Healing -- Circulating Molecular Chaperones in Health and Disease -- Index.
520			_aSince the beginning of the 21st Century there has been a rapid increase in our understanding of the cellular trafficking mechanisms of molecular chaperones in eukaryotes and in prokaryotes. In the former, molecular chaperone trafficking can occur between the various cellular compartments, with concomitant movement of other proteins. Such events can also result in the release of molecular chaperones from cells. In bacteria, molecular chaperones are involved in the trafficking of other proteins and are themselves released into the external milieu. The increasing appreciation of the role of molecular chaperones and Protein-Folding Catalysts in the interplay between bacteria and the cells of their hosts is now an important area of research for understanding the mechanisms of infectious diseases. This volume brings together experts in the biochemistry, cellular biology, immunology and molecular biology of molecular chaperones and Protein-Folding Catalysts with a focus on the mechanisms of cellular trafficking of these proteins and the role of these variegated trafficking mechanisms in both human and animal health and disease.
590			_aPara consulta fuera de la UANL se requiere clave de acceso remoto.
700	1		_aPockley, A. Graham. _eeditor. _9351849
710	2		_aSpringerLink (Servicio en línea) _9299170
776	0	8	_iEdición impresa: _z9789400747395
856	4	0	_uhttp://remoto.dgb.uanl.mx/login?url=http://dx.doi.org/10.1007/978-94-007-4740-1 _zConectar a Springer E-Books (Para consulta externa se requiere previa autentificación en Biblioteca Digital UANL)
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