Efficient in vitro amplification of chronic wasting disease PrPRES. - Wikidata - awgldk - TriplyDB

Efficient in vitro amplification of chronic wasting disease PrPRES.

Efficient in vitro amplification of chronic wasting disease PrPRES.

http://www.wikidata.org/entity/Q35948020

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Highly efficient protein misfolding cyclic amplification Detection of sub-clinical CWD infection in conventional test-negative deer long after oral exposure to urine and feces from CWD+ deer.Molecular Mechanisms of Chronic Wasting Disease Prion Propagation.Accelerated high fidelity prion amplification within and across prion species barriers.Detection of CWD prions in urine and saliva of deer by transgenic mouse bioassay.Chronic wasting disease in bank voles: characterisation of the shortest incubation time model for prion diseases.Detection of protease-resistant cervid prion protein in water from a CWD-endemic area Sulfated dextrans enhance in vitro amplification of bovine spongiform encephalopathy PrP(Sc) and enable ultrasensitive detection of bovine PrP(Sc).Protein misfolding cyclic amplification of infectious prions.In vitro amplification of misfolded prion protein using lysate of cultured cells.Highly efficient amplification of chronic wasting disease agent by protein misfolding cyclic amplification with beads (PMCAb).Genotype-dependent molecular evolution of sheep bovine spongiform encephalopathy (BSE) prions in vitro affects their zoonotic potential Rapid assessment of bovine spongiform encephalopathy prion inactivation by heat treatment in yellow grease produced in the industrial manufacturing process of meat and bone meals Detection of chronic wasting disease prions in salivary, urinary, and intestinal tissues of deer: potential mechanisms of prion shedding and transmission.Alteration of the chronic wasting disease species barrier by in vitro prion amplification.Lower specific infectivity of protease-resistant prion protein generated in cell-free reactions.In vitro amplification of scrapie and chronic wasting disease PrP(res) using baculovirus-expressed recombinant PrP as substrate A species barrier limits transmission of chronic wasting disease to mink (Mustela vison).Prions in the environment: occurrence, fate and mitigation Identification of misfolded proteins in body fluids for the diagnosis of prion diseases.Prions are secreted in milk from clinically normal scrapie-exposed sheep.Crossing the species barrier by PrP(Sc) replication in vitro generates unique infectious prions.Enhancement of protein misfolding cyclic amplification by using concentrated cellular prion protein source.Highly infectious prions generated by a single round of microplate-based protein misfolding cyclic amplification.Prion transmission: prion excretion and occurrence in the environment.Insights into Mechanisms of Transmission and Pathogenesis from Transgenic Mouse Models of Prion Diseases.Evolution of Diagnostic Tests for Chronic Wasting Disease, a Naturally Occurring Prion Disease of Cervids.Cyclic amplification of prion protein misfolding.In vitro amplification of prions from milk in the detection of subclinical infections.Assessment of the genetic susceptibility of sheep to scrapie by protein misfolding cyclic amplification and comparison with experimental scrapie transmission studies.Detection of prions in the faeces of sheep naturally infected with classical scrapie.Endemic chronic wasting disease causes mule deer population decline in Wyoming.Protocol for further laboratory investigations into the distribution of infectivity of Atypical BSE Scientific Opinion on a request for a review of a scientific publication concerning the zoonotic potential of ovine scrapie prions Chronic wasting disease (CWD) in cervids Detection of Prions in Blood of Cervids at the Asymptomatic Stage of Chronic Wasting Disease.Estimating chronic wasting disease susceptibility in cervids using real-time quaking-induced conversion.Distinctive properties of plaque-type dura mater graft-associated Creutzfeldt-Jakob disease in cell-protein misfolding cyclic amplification.Ultrasensitive detection of scrapie prion protein derived from ARQ and AHQ homozygote sheep by interspecies in vitro amplification.Sc237 hamster PrPSc and Sc237-derived mouse PrPSc generated by interspecies in vitro amplification exhibit distinct pathological and biochemical properties in tga20 transgenic mice.

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P2860

Efficient in vitro amplification of chronic wasting disease PrPRES.

http://www.wikidata.org/entity/Q35948020

description

2007 nî lūn-bûn

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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2007年论文

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2007年论文

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name

Efficient in vitro amplification of chronic wasting disease PrPRES.

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Efficient in vitro amplification of chronic wasting disease PrPRES.

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Efficient in vitro amplification of chronic wasting disease PrPRES.

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Efficient in vitro amplification of chronic wasting disease PrPRES.

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Efficient in vitro amplification of chronic wasting disease PrPRES.

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Efficient in vitro amplification of chronic wasting disease PrPRES.

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P1433

Journal of Virology

P1476

Efficient in vitro amplification of chronic wasting disease PrPRES.

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P2093

Carol J Wilusz

http://www.w3.org/2001/XMLSchema#string

Edward A Hoover

http://www.w3.org/2001/XMLSchema#string

Glenn C Telling

http://www.w3.org/2001/XMLSchema#string

Jeffrey Wilusz

http://www.w3.org/2001/XMLSchema#string

Mark D Zabel

http://www.w3.org/2001/XMLSchema#string

Matthew R Perrott

http://www.w3.org/2001/XMLSchema#string

Surachai Supattapone

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Timothy D Kurt

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P2860

Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins

Glycosylation influences cross-species formation of protease-resistant prion protein.

Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding.

In vitro generation of infectious scrapie prions.

Detection of prions in blood.

Infectious prions in the saliva and blood of deer with chronic wasting disease.

Transmission of prions from mule deer and elk with chronic wasting disease to transgenic mice expressing cervid PrP.

Sulfated glycans and elevated temperature stimulate PrP(Sc)-dependent cell-free formation of protease-resistant prion protein.

Evidence of a molecular barrier limiting susceptibility of humans, cattle and sheep to chronic wasting disease

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9605-9608

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scholarly article

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10.1128/JVI.00635-07

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17

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81

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2007-06-06T00:00:00Z

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6282699

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17553879

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1951436

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