000 04381nam a22005295i 4500
001 978-1-4614-5305-5
003 DE-He213
005 20140220082819.0
007 cr nn 008mamaa
008 121205s2013 xxu| s |||| 0|eng d
020 _a9781461453055
_9978-1-4614-5305-5
024 7 _a10.1007/978-1-4614-5305-5
_2doi
050 4 _aRC321-580
072 7 _aPSAN
_2bicssc
072 7 _aMED057000
_2bisacsh
082 0 4 _a612.8
_223
100 1 _aZou, Wen-Quan.
_eeditor.
245 1 0 _aPrions and Diseases
_h[electronic resource] :
_bVolume 1, Physiology and Pathophysiology /
_cedited by Wen-Quan Zou, Pierluigi Gambetti.
264 1 _aNew York, NY :
_bSpringer New York :
_bImprint: Springer,
_c2013.
300 _aIX, 241 p. 36 illus., 28 illus. in color.
_bonline resource.
336 _atext
_btxt
_2rdacontent
337 _acomputer
_bc
_2rdamedia
338 _aonline resource
_bcr
_2rdacarrier
347 _atext file
_bPDF
_2rda
505 0 _aTransmissible Spongiform Encephalopathy: from the High Middle Ages to Daniel Carlton Gajdusek -- The Rich Chemistry of the Copper and Zinc Sites in Cellular Prion Protein -- Role of Cellular Prion Protein in the Amyloid-ß Oligomer Pathophysiology of Alzheimer’s Disease -- Cellular Prion Protein and Cancers -- Insoluble Cellular Prion Protein -- Protein Misfolding Cyclic Amplification -- Cofactor Involvement in Prion Propagation -- Prion Protein Conversion and Lipids -- New Perspectives on Prion Conversion: Introducing a Mechanism of Deformed Templating -- Infectious and Pathogenic Forms of Prion Protein -- Cellular Mechanisms of Propagation and Clearance -- Molecular Mechanisms Encoding Quantitative and Qualitative Traits of Prion Strains -- Modeling the Cell Biology of Prions -- Prion Strain Interference -- Introduction to Yeast and Fungal Prions -- Yeast Prions are Pathogenic, in-register Parallel Amyloids.
520 _aTransmissible spongiform encephalopathies (TSE), now broadly known as prion diseases, have been recognized for nearly 300 years in animals and almost 100 years in humans. However, the nature of the transmissible agent had largely remained a mystery until Stanley Prusiner discovered the infectious isoform of the prion protein (PrP), named prion or scrapie PrP (PrPSc), in 1982. The subsequent modern studies with protein chemistry and molecular biology in cell culture, transgenic animals, and cell-free systems, including the revolutionary protein-misfolding cyclic amplification (PMCA), have greatly advanced our understanding of the pathogenesis of prion diseases and facilitated the identification of new prion diseases in animals and humans. In Prions and Prion Diseases, more than 60 leading researchers and clinicians worldwide provide an up-to-date development in many aspects of these unique infectious pathogens and their associated diseases. Volume I highlights the association of the cellular prion protein (PrPC) with copper and zinc, the potential roles of PrPC in Alzheimer’s disease and cancers, insoluble PrPC, PMCA, molecular and cellular mechanisms of PrPSc formation and clearance, possible co-factors involved in the conversion of PrPC into PrPSc, infectious and pathogenic forms of PrP, cell biology of prions, prion strains and their interference, as well as yeast prions and their inheritable and structural traits. This unique volume covers history from the high Middle Ages to the TSE era of Daniel Carleton Gajdusek, followed by the prion era of Stanley Prusiner whose extraordinary discovery opened a new chapter in prion research. Volume I will take you through the fascinating chronicle of prions in mammals, yeast, and fungi.
650 0 _aMedicine.
650 0 _aHuman physiology.
650 0 _aNeurosciences.
650 0 _aNeurology.
650 0 _aBiochemistry.
650 0 _aAnimal Physiology.
650 1 4 _aBiomedicine.
650 2 4 _aNeurosciences.
650 2 4 _aHuman Physiology.
650 2 4 _aNeurology.
650 2 4 _aProtein Science.
650 2 4 _aAnimal Physiology.
650 2 4 _aBiochemistry, general.
700 1 _aGambetti, Pierluigi.
_eeditor.
710 2 _aSpringerLink (Online service)
773 0 _tSpringer eBooks
776 0 8 _iPrinted edition:
_z9781461453048
856 4 0 _uhttp://dx.doi.org/10.1007/978-1-4614-5305-5
912 _aZDB-2-SBL
999 _c95374
_d95374