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008			130708s2013 ne | s |||| 0|eng d
020			_a9789400767874
024	7		_a10.1007/978-94-007-6787-4 _2doi
040			_dES-MaUEC
050		4	_aQP552.H43 _bH463 2013
100	1		_aHenderson, Brian. _eeditor literario _935363 _0comprobar BNE20031680779
245	1	0	_aMoonlighting Cell Stress Proteins in Microbial Infections _cedited by Brian Henderson.
260			_aDordrecht, Netherlands _bSpringer International Publishing _c2013
300			_a1 recurso en línea (XVII, 406 p.) _b55 ilustraciones, 33 ilustraciones en color
336			_aTexto (visual) _btxt _2rdacontent
337			_aelectrónico _bc _2rdamedia
338			_arecurso electrónico _bcr _2rdacarrier
490	0		_aHeat Shock Proteins _x1877-1246 _v7
505	0		_aBacterial Cell Stress Responses -- A Brief Introduction to Eukaryotic Cell Stress Proteins -- New Thoughts on Protein Moonlighting -- Chaperonin 10 a Pro- and Anti-inflammatory Host Modulator -- Helicobacter pylori peptidyl prolyl cis, trans isomerase: a modulator of the host immune response -- Macrophage Infectivity Promoter: An FK506-Binding Peptidylprolyl Isomerase with Collagen-Binding and Transmigrating Activity -- Evolution of Bacterial Chaperonin 60 Paralogues and Moonlighting Activity -- Mycobacterium tuberculosis Chaperonins as Novel Virulence Factors -- Legionella pneumophila Chaperonin 60: A Multifunctional Virulence Protein -- Chaperonin 60.1 of the Chlamydiae (cHSP60) as a Major Virulence Determinant -- Symbiotic Bacterial Chaperonin 60 and Plant Virus Transmission -- Histoplasma capsulatum Chaperonin 60: A Novel Adhesin and Vaccine Candidate -- The role of stress-induced activation of HSP70 in dendritic cells, CD4+ T cell memory and adjuvanticity -- Candida albicans Ssa: A Hsp70 Homologue and Virulence Factor -- Hsp90 plays a role in host-bacterial interactions: Insight gained from Acanthamoeba castellanii -- Role of Peptidyl-Prolyl cis/trans Isomerases in Cellular Uptake of Bacterial Protein Toxins -- Listeria monocytogenes and Host Hsp60 - an Invasive Pairing -- Cell Surface Stress Proteins and the Receptor for Lipopolysaccharide -- Grp78 (BiP) a Cell Surface Receptor for Viruses -- BiP (Grp78): a Target for Escherichia coli Subtilase Cytotoxin -- Cholera Toxin Interactions with Host Cell Stress Proteins -- Endoplasmic reticulum stress-associated Gp96 chaperone is a host receptor for Adherent-Invasive E. coli -- Escherichia coli K1 Meningitis and Heat Shock Protein, Gp96 -- Bacterial Cell Stress Protein Clp: A Novel Antibiotic Target -- Host Neuroendocrine Stress Hormones Driving Bacterial Behaviour and Virulence.
520			_aMicrobial infection is increasingly seen as a problem as we begin to run out of antibiotics. Understanding how microbes cause disease is essential. In recent years it has begun to emerge that bacteria, fungi, protozoa and viruses can use their cell stress proteins to cause infection. This volume brings together the world's leading experts in the study of the microbial and human cell stress proteins that are involved in enabling microorganisms to infect humans and cause serious disease.
650		7	_2embne _aProteínas _9139861
856	4	0	_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://link.springer.com/book/10.1007/978-94-007-6787-4 _zAcceso a este recurso digital (usuarios Universidad Europea de Madrid)
907			_a.b12824495 _b10-10-17 _c01-10-14
942			_2lcc _cLE
945			_aQP552.H43 H463 2013 EB _g1 _ieBOOK _j0 _lmae _o- _pEUR0.00 _q- _r- _sb _t15 _u0 _v0 _w0 _x0 _y.i11553704 _z06-04-17
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