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020 _a9789400767874
_9978-94-007-6787-4
024 7 _a10.1007/978-94-007-6787-4
_2doi
050 4 _aR-RZ
072 7 _aMBGR
_2bicssc
072 7 _aMED000000
_2bisacsh
082 0 4 _a610
_223
245 1 0 _aMoonlighting Cell Stress Proteins in Microbial Infections
_h[electronic resource] /
_cedited by Brian Henderson.
264 1 _aDordrecht :
_bSpringer Netherlands :
_bImprint: Springer,
_c2013.
300 _aXVII, 406 p.
_bonline resource.
336 _atext
_btxt
_2rdacontent
337 _acomputer
_bc
_2rdamedia
338 _aonline resource
_bcr
_2rdacarrier
347 _atext file
_bPDF
_2rda
490 1 _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 0 _aMedicine.
650 0 _aProteins.
650 0 _aMicrobiology.
650 0 _aBacteriology.
650 1 4 _aBiomedicine.
650 2 4 _aBiomedicine general.
650 2 4 _aProtein Science.
650 2 4 _aMicrobiology.
650 2 4 _aBacteriology.
700 1 _aHenderson, Brian.
_eeditor.
710 2 _aSpringerLink (Online service)
773 0 _tSpringer eBooks
776 0 8 _iPrinted edition:
_z9789400767867
830 0 _aHeat Shock Proteins,
_x1877-1246 ;
_v7
856 4 0 _uhttp://dx.doi.org/10.1007/978-94-007-6787-4
912 _aZDB-2-SBL
942 _2Dewey Decimal Classification
_ceBooks
999 _c48934
_d48934