about
The strain-encoded relationship between PrP replication, stability and processing in neurons is predictive of the incubation period of diseasePrion formation, but not clearance, is supported by protein misfolding cyclic amplification.Abnormal brain iron homeostasis in human and animal prion disordersIn vitro amplification of misfolded prion protein using lysate of cultured cells.Coinfecting prion strains compete for a limiting cellular resource.Effects of solution chemistry and aging time on prion protein adsorption and replication of soil-bound prions.Enzymatic digestion of chronic wasting disease prions bound to soil.Extraneural prion neuroinvasion without lymphoreticular system infection.Interspecies transmission of chronic wasting disease prions to squirrel monkeys (Saimiri sciureus)Occurrence, transmission, and zoonotic potential of chronic wasting diseaseRetrograde transport of transmissible mink encephalopathy within descending motor tracts.Resistance of soil-bound prions to rumen digestion.Rapid prion neuroinvasion following tongue infection.Behavior of prions in the environment: implications for prion biologyReplication efficiency of soil-bound prions varies with soil type.Nasal associated lymphoid tissue of the Syrian golden hamster expresses high levels of PrPC.In vitro detection of prionemia in TSE-infected cervids and hamsters.An enzymatic treatment of soil-bound prions effectively inhibits replication.Mitigation of prion infectivity and conversion capacity by a simulated natural process--repeated cycles of drying and wetting.Tracking protein aggregate interactions.In vitro generation of high-titer prionsPrion interference is due to a reduction in strain-specific PrPSc levels.Environmentally-relevant forms of the prion protein.Investigation of Bovine Serum Albumin (BSA) Attachment onto Self-Assembled Monolayers (SAMs) Using Combinatorial Quartz Crystal Microbalance with Dissipation (QCM-D) and Spectroscopic Ellipsometry (SE).The nasal cavity is a route for prion infection in hamstersFrom Slow Viruses to Prions.PrPSc formation and clearance as determinants of prion tropism.Characterization of conformation-dependent prion protein epitopes.Rapid transepithelial transport of prions following inhalation.Prion strain targeting independent of strain-specific neuronal tropism.Rapid, high-throughput detection of PrPSc by 96-well immunoassay.Specificity, Size, and Frequency of Spaces That Characterize the Mechanism of Bulk Transepithelial Transport of Prions in the Nasal Cavities of Hamsters and Mice.Influence of prion strain on prion protein adsorption to soil in a competitive matrix.Soil-mediated prion transmission: is local soil-type a key determinant of prion disease incidence?Adaptation and selection of prion protein strain conformations following interspecies transmission of transmissible mink encephalopathy.Incongruity between Prion Conversion and Incubation Period following Coinfection.Prion infection of skeletal muscle cells and papillae in the tongue.Immediate and Ongoing Detection of Prions in the Blood of Hamsters and Deer following Oral, Nasal, or Blood Inoculations.Safety and toxicological evaluation of a novel niacin-bound chromium (III) complex.Delay in onset of prion disease for the HY strain of transmissible mink encephalopathy as a result of prior peripheral inoculation with the replication-deficient DY strain.
P50
Q27312083-0F06DA0A-DDCF-47B5-AF31-2A376A8F4A37Q30875331-F2E54D63-3F45-473E-B911-B924D78CF191Q33417668-F104F2F3-C769-4816-BA53-6DC20B56E334Q33862576-7C46A81D-0340-407B-8FCA-CB54FA184F4BQ33877386-E266B4F8-E570-4266-BDA1-2DF3CE6A4A0CQ33883652-DF93AE64-8B11-4058-A95B-B4F2DAB3419AQ33913922-70F7A261-07BD-4C06-81E6-467EE5C49307Q33987431-3B42BD22-EBCF-4EB7-A6A8-175B813B8356Q34092718-79115218-53DF-4616-8ECC-2C9757C24DE6Q34257676-3EE90855-5250-4DC6-8241-DD4D59C9E23CQ34365409-3E9BEC8A-6109-456B-95CB-C07F60B31DDCQ34399654-76E0334B-45C7-46B8-8FB9-EF9E729EBAE1Q34462142-2E2FDD2F-DC8F-4E8F-8E94-666AD9961A3FQ34585664-E2ADDB9B-7A12-4009-A454-B4FEB8C11B3CQ34982680-F18179DC-2964-4FF8-B7ED-56A8ED16E8FFQ35038839-4545E59A-5389-4AA0-A814-909B978AA26EQ35041621-7A38401B-CA8E-4DBD-B8CE-5F3A83D9E598Q35080977-B1F3D7AC-5347-4578-872D-48C0D5B92093Q35104674-5298A9D1-F73E-44ED-8876-897F2D775445Q35194896-3FA8233B-301E-4877-8543-96E4CA4E2B1DQ35599313-832FF80D-399B-4E66-922C-2FB257DA5C03Q35635053-918A635B-7007-4FA2-A94F-CCA9150D8708Q35782128-D450FB17-B2E9-4688-9DFD-C336248D0FF2Q35822663-72051A69-F911-49BF-8DE5-1A06BCCF7184Q35857428-3D05131E-CB79-4C1E-B178-008AEEBDCEE1Q36070377-261635F9-1192-4302-A9F8-2D972C2D07EAQ36326862-A0BB8844-B1AE-4DCA-B157-F83890CA27CFQ36347803-1873F889-8038-4288-8FFD-F4D2C7530401Q36397542-0A4FB8BE-1A94-46A5-BFE5-549D6171F131Q37033154-D8DF2C16-B009-4547-8573-ADD264FE75A4Q37178394-D22FBA43-F864-4031-A878-A6FD9EF7C742Q37224841-4403D7E1-FA86-44EF-83BE-64504BBB6DC2Q37426703-568E849F-7FBF-4BFC-9A23-7679A33E7F1DQ37977718-58FB378C-8448-4B6A-B878-57157D2A772BQ39591398-172C1DE1-A652-41FD-9686-53A51B317AC5Q40725201-6B4FDA45-68D6-4079-83CC-35A51687612EQ40909580-BC7DCAD9-C266-4EB8-B32D-CDCD19664DCDQ41271604-7D7F991F-AD23-492F-A4A4-32BD0D31C717Q46709093-C2E58E1C-AE14-4289-AB5C-8DC33029A9D9Q48096008-8ACF2EAD-46CA-4947-9DF1-95727BE9E827
P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Jason Bartz
@ast
Jason Bartz
@en
Jason Bartz
@es
Jason Bartz
@nl
Jason Bartz
@sl
type
label
Jason Bartz
@ast
Jason Bartz
@en
Jason Bartz
@es
Jason Bartz
@nl
Jason Bartz
@sl
altLabel
Bartz J
@en
Bartz JC
@en
prefLabel
Jason Bartz
@ast
Jason Bartz
@en
Jason Bartz
@es
Jason Bartz
@nl
Jason Bartz
@sl
P106
P1153
7006093504
P21
P31
P496
0000-0003-4081-7886