Ultra-sensitive detection of prion protein fibrils by flow cytometry in blood from cattle affected with bovine spongiform encephalopathy

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Location: Deutsche Nationalbibliothek Frankfurt am Main

ISSN: 1472-6750

Extent: Online-Ressource

Language: Englisch

Notes: online resource.

Bibliographic citation: Ultra-sensitive detection of prion protein fibrils by flow cytometry in blood from cattle affected with bovine spongiform encephalopathy ; volume:5 ; number:1 ; day:04 ; month:10 ; year:2005 ; pages:1-5 ; date:12.2005
BMC biotechnology ; 5, Heft 1 (04.10.2005), 1-5, 12.2005

Creator: Trieschmann, Lothar

Contributor: Santos, Alexander Navarrete
Kaschig, Katja
Torkler, Sandra
Maas, Elke
Schätzl, Hermann
Böhm, Gerald
SpringerLink (Online service)

DOI: 10.1186/1472-6750-5-26

URN: urn:nbn:de:1111-2016072531477

Rights: Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 14.08.2025, 10:49 AM CEST

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Associated

Trieschmann, Lothar
Santos, Alexander Navarrete
Kaschig, Katja
Torkler, Sandra
Maas, Elke
Schätzl, Hermann
Böhm, Gerald
SpringerLink (Online service)

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Ultra-sensitive detection of prion protein fibrils by flow cytometry in blood from cattle affected with bovine spongiform encephalopathy

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Other Objects (12)

Chemical cytometry : ultrasensitive analysis of single cells

Biodegradation of bovine spongiform encephalopathy prions in compost

2.7 Å cryo-EM structure of ex vivo RML prion fibrils

Mechanical Deformation Mechanisms and Properties of Prion Fibrils Probed by Atomistic Simulations

Co-occurrence of chronic traumatic encephalopathy and prion disease

Cryo-EM structure of a natural prion: chronic wasting disease fibrils from deer

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α-Synuclein emulsifies TDP-43 prion-like domain—RNA liquid droplets to promote heterotypic amyloid fibrils

Demonstration of prion-like properties of mutant huntingtin fibrils in both in vitro and in vivo paradigms

Overexpression of mouse prion protein in transgenic mice causes a non-transmissible spongiform encephalopathy

Classical bovine spongiform encephalopathy and chronic wasting disease: two sides of the prion coin

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Chemical cytometry : ultrasensitive analysis of single cells

Biodegradation of bovine spongiform encephalopathy prions in compost

2.7 Å cryo-EM structure of ex vivo RML prion fibrils

Mechanical Deformation Mechanisms and Properties of Prion Fibrils Probed by Atomistic Simulations

Co-occurrence of chronic traumatic encephalopathy and prion disease

Cryo-EM structure of a natural prion: chronic wasting disease fibrils from deer

Prions prions prions

α-Synuclein emulsifies TDP-43 prion-like domain—RNA liquid droplets to promote heterotypic amyloid fibrils

Demonstration of prion-like properties of mutant huntingtin fibrils in both in vitro and in vivo paradigms

Overexpression of mouse prion protein in transgenic mice causes a non-transmissible spongiform encephalopathy

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Chemical cytometry : ultrasensitive analysis of single cells

Biodegradation of bovine spongiform encephalopathy prions in compost

2.7 Å cryo-EM structure of ex vivo RML prion fibrils

Mechanical Deformation Mechanisms and Properties of Prion Fibrils Probed by Atomistic Simulations

Co-occurrence of chronic traumatic encephalopathy and prion disease

Cryo-EM structure of a natural prion: chronic wasting disease fibrils from deer

Prions prions prions

α-Synuclein emulsifies TDP-43 prion-like domain—RNA liquid droplets to promote heterotypic amyloid fibrils

Demonstration of prion-like properties of mutant huntingtin fibrils in both in vitro and in vivo paradigms

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