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Prion

Vimses are one of the smallest biological entities (except viroids and prions) that carry all the iaformation necessary for thek own reproduction. They are unique, differing from procaryotes and eucaryotes ia that they carry only one type of nucleic acid as genetic material, which can be transported by the vims from one cell to another. Vimses are composed of a shell of proteki enclosing a core of nucleic acid, either ribonucleic acid (RNA) or deoxyribonucleic acid (DNA), that codes for vkal reproduction. The outer shell serves as a protective coat to keep the nucleic acid kitact and safe from enzymatic destmction. In addition to thek proteki coat, some vimses contain an outer covering known as an outer envelope. This outer envelope consists of a Hpid or polysaccharide material. [Pg.302]

Y Levy, OM Becker. Wild-type and mutant prion proteins Insights from energy landscape analysis. In E Katzir, B Solomon, A Taraboulos, eds. Conformational Diseases. In press. [Pg.391]

Cohen, RE., et al. Structural clues to prion replication. Science 264 530-531, 1994. [Pg.119]

These results indicate that is it possible to change the fold of a protein by changing a restricted set of residues. They also confirm the validity of the rules for stability of helical folds that have been obtained by analysis of experimentally determined protein structures. One obvious impliction of this work is that it might be possible, by just changing a few residues in Janus, to design a mutant that flip-flops between a helical and p sheet structures. Such a polypeptide would be a very interesting model system for prions and other amyloid proteins. [Pg.370]

The transmissible spongiform encephalopathies, or prion diseases, are fatal neurodegenerative diseases characterized by spongiform changes, astrocytic gliomas, and neuronal loss resulting from the deposition of insoluble protein aggregates in neural cells. They include Creutzfeldt-Jakob disease in humans, scrapie in... [Pg.37]

Prions—protein particles that lack nucleic acid— cause fatal transmissible spongiform encephalopathies such as Creutzfeldt-Jakob disease, scrapie, and bovine spongiform encephalopathy. Prion diseases involve an altered secondary-tertiary strucmre of a namrally occurring protein, PrPc. When PrPc interacts with its pathologic isoform PrPSc, its conformation is transformed from a predominantly a-helical strucmre to the P-sheet strucmre characteristic of PrPSc. [Pg.39]

Burkhard P, Stetefeld J, Strelkov SV Coiled coils A highly versatile protein folding motif. Trends Cell Biol 2001 11 82. Collinge J Prion diseases of humans and animals Their causes and molecular basis. Annu RevNeurosci 2001 24 519. [Pg.39]

Soto C Alzheimer s and prion disease as disorders of protein conformation Implications for the design of novel therapeutic... [Pg.39]

There has been great concern over the large-scale outbreak of BSE that occurred in the UK from 1988 as a result of feeding cattle with supplements prepared fiom sheep and cattle offal. Brain extracts firm BSE cattle have transmitted the disease to mice, sheep, cattle, pigs and monkeys. Studies of 12 recent cases of atypical CJD in the UK have provided evidence that the bovine prions have infected humans through the consumption of contaminated beef... [Pg.73]

Prusiner S.B. (1996) Molecular biology and pathogenesis of prion disease. Trends Biochem Sci, 21, 482-487. [Pg.74]

Microorganisms surviving M. tuberculosis Bacterial spores HBV and prions as in Creutzfeldt-Jakob disease Bacterial spores Prions Extreme challenge of resistant bacterial spores Prions (insufficient data)... [Pg.203]

Spore structure 9 Activity of biocides against prions... [Pg.263]

The most resistant of all infectious agents to chemical inactivation are the prions, which cause transmissible degenerative encephalopathies. [Pg.264]

Prions are responsible for the so-ealled slow virus diseases, a distinet group of unusual neurologieal disorders. They are believed to be markedly resistant to inactivation by many ehemieal and physical agents but because they have not been purified, it is at present diffieult to state whether this is an intrinsic property of prions or whether it results fkm the proteetive effect of host tissue present. Certainly very high coneentrations of a bioeide aeting for long periods may be necessary to produee inactivation. [Pg.276]

Beekes, M., Lemmer, K., Thomzig, A., Joncic, M., Tintelnot, K., and Mielke, M. (2010). Fast, broad-range disinfection of bacteria, fungi, viruses and prions. /. Gen. Virol. 91, 580-589. [Pg.22]

Leishmania spp., Rickettsia, Parvovirus spp., plasmodia and Toxoplasma spp., and prions... [Pg.84]

Prion diseases resulting in encephalopathy can be transmitted between individuals within species (more rarely between species) [26-28], A conformational variant of the normal cellular protein PrPs (PrPc) (protease-sensitive or cellular) is believed to catalyze [29] or nucleate [30-33] conversion to the pathological form, PrPR (protease-resistant). This highly unusual nongenetic mode of transmission of an infectious agent has been strongly debated [29]. The observation of multiple examples of nucleated catalysis of aberrant polymerization of protein subunits has... [Pg.251]


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A Brain Protein Prion

Accessory Molecules in Scrapie Prions

Acquired Human Prion Diseases

Amyloid diseases prion evidence

Amyloid prion protein

Animal models prion diseases

Biosynthesis prion protein

Bovine prion protein

Bovine prion protein structure

Bovine prions

Bovine related prion diseases

Brain prion disease

Cellular form of prion

Conformations of prion proteins

Creutzfeldt-Jakob disease, prion peptide

Disease prion diseases

Drug Design Targeting Prions

Experimentally Derived Constraints on Prion Filament Structure

Familial Human Prion Diseases

Fungal prions

Fungal prions filament polymorphism

Fungal prions prion domains

Further Genetic Evidence That Is a Prion

Genetic Criteria for Yeast Prions

Genetic Susceptibility to Acquired and Sporadic Human Prion Disease

Genetic and Cell Biological Support for as a Yeast Prion

Human prion diseases

Human prion diseases, atypical

Human prion protein

Human prion protein disease link

Human prion protein pathogenic mutations

Human prion protein structure

Human prion protein transgenic studies

Human prions

Infectious agent transmission prion diseases

Inherited prion disease

Jakob and Other Prion Diseases

Kuru human prion disease

Mammalian prion

Mink prions

Murine prion protein

Peripheral Prion Replication and Neuroinvasion

Podospora anserina prions

Podospora anserina prions function

Preservatives prions

Prion Hypothesis

Prion Protein Structure and the Species Barrier

Prion amyloids

Prion based diseases

Prion cellular form

Prion composition

Prion containment

Prion conversion

Prion definition

Prion diseases

Prion diseases (transmissible spongiform

Prion diseases acquired

Prion diseases cell death

Prion diseases diversity

Prion diseases familial

Prion diseases feature

Prion diseases history

Prion diseases iatrogenic

Prion diseases neuropathology

Prion diseases pathogenic mutation

Prion diseases protein polymorphism

Prion diseases protein-only hypothesis

Prion diseases sporadic etiology

Prion diseases transmission barriers

Prion disorders

Prion domain

Prion domains prions

Prion encephalopathy

Prion fibrils

Prion fibrils structural studies

Prion knockout mice

Prion mutation

Prion of the Fungus Podospora anserina, Is Necessary for a Normal Function

Prion pathology

Prion precursor protein

Prion propagation

Prion protein

Prion protein amyloid, structural models

Prion protein cell membrane interactions

Prion protein cellular biology

Prion protein conformation analysis

Prion protein description

Prion protein disulfide bond

Prion protein diversity

Prion protein encephalopathies

Prion protein fibrils

Prion protein folding dynamics

Prion protein formation

Prion protein fragments

Prion protein gene

Prion protein human disease-associated mutations

Prion protein induced conversions

Prion protein isoform interactions

Prion protein molecular basis

Prion protein self-replication

Prion protein strain differences

Prion protein strain types

Prion protein structural analysis

Prion protein transmissible spongiform

Prion protein, cellular

Prion proteinc mass spectrometric analysis

Prion proteinc overview

Prion proteins amyloid fiber

Prion proteins genetic mutations

Prion proteins infectious

Prion proteins interaction

Prion proteins interaction with

Prion proteins residues

Prion proteins structure

Prion proteins, conversion

Prion proteins, conversion folding

Prion replication, models

Prion scrapie form

Prion scrapie susceptibility

Prion seeded conversion

Prion strains

Prion strains diversity

Prion structural biology

Prion variants

Prion, Antarctic

Prion, pathogenic

Prion-forming domains

Prion-mediated disease

Prion-related peptides

Prion-related protein

Prion-related protein scrapie

Prions Creutzfeldt-Jakob disease

Prions environment

Prions fatal familial insomnia

Prions infectivity

Prions molecular mechanism

Prions of Ure2p and Sup35p, Respectively

Prions replication

Prions stability

Prions sterilization resistance

Prions synthetic mammalian

Prions types

Prions, phenothiazines

Protease prion protein resistance

Protease prion protein sensitive

Protease yeast prion resistance

Protease-resistant prion proteins

Protein folding prion

Proteins prion diseases

Saccharomyces cerevisiae, prions

Scrapie disease prion

Scrapie prion protein

Spongiform encephalopathies, transmissible prion diseases)

Sporadic Human Prion Diseases

Structural Models for Prion Amyloid Filaments

Structure prion diseases associated with

Subviral Agents Prions

Syrian hamster prion protein

Syrian hamster prion protein structure

Thermodynamics, recombinant prion

Trafficking of the Prion Agent to Secondary Lymphoid Tissues

Transgenics artificial prions

Transmissible spongiform encephalopathy prions

UV-Induced Aggregation of Prion Protein

Vaccine for the Treatment of Prion Diseases

Viruses prions

Yeast Ure2p prion

Yeast prions

Yeast prions chaperones

Yeast prions emergence

Yeast prions function

Yeast prions models

Yeast prions prion evidence

Yeast prions region

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