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Quantitative detection and biological propagation of scrapie seeding activity in vitro facilitate use of prions as model pathogens for disinfection

PloS one, 2011-05, Vol.6 (5), p.e20384-e20384

2011

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Sialylation Controls Prion Fate in Vivo

The Journal of biological chemistry, 2017-02, Vol.292 (6), p.2359-2368

2017

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Reversible off and on switching of prion infectivity via removing and reinstalling prion sialylation

Scientific reports, 2016-09, Vol.6 (1), p.33119-33119, Article 33119

2016

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Disease Transmission by Misfolded Prion-Protein Isoforms, Prion-Like Amyloids, Functional Amyloids and the Central Dogma

Biology, 2016-01, Vol.5 (1), p.2

Daus, Martin L

2016

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Presence and seeding activity of pathological prion protein (PrP(TSE)) in skeletal muscles of white-tailed deer infected with chronic wasting disease

PloS one, 2011-04, Vol.6 (4), p.e18345-e18345

2011

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Infrared Microspectroscopy Detects Protein Misfolding Cyclic Amplification (PMCA)-induced Conformational Alterations in Hamster Scrapie Progeny Seeds

The Journal of biological chemistry, 2013-12, Vol.288 (49), p.35068-35080

2013

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Maltose binding protein (MalE) interacts with periplasmic loops P2 and P1 respectively of the MalFG subunits of the maltose ATP binding cassette transporter (MalFGK₂) from Escherichia coli/Salmonella during the transport cycle

Molecular microbiology, 2007-12, Vol.66 (5), p.1107-1122

2007

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Periplasmic Loop P2 of the MalF Subunit of the Maltose ATP Binding Cassette Transporter Is Sufficient To Bind the Maltose Binding Protein MalE

Biochemistry (Easton), 2009-03, Vol.48 (10), p.2216-2225

2009

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Towards further reduction and replacement of animal bioassays in prion research by cell and protein misfolding cyclic amplification assays

Laboratory animals (London), 2013-04, Vol.47 (2), p.106-115

2013

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ATP-driven MalK Dimer Closure and Reopening and Conformational Changes of the “EAA” Motifs Are Crucial for Function of the Maltose ATP-binding Cassette Transporter (MalFGK2)

The Journal of biological chemistry, 2007-08, Vol.282 (31), p.22387-22396

2007

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ATP Induces Conformational Changes of Periplasmic Loop Regions of the Maltose ATP-binding Cassette Transporter

The Journal of biological chemistry, 2006-02, Vol.281 (7), p.3856-3865

2006

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Chronic wasting disease: Fingerprinting the culprit in risk assessments

Prion, 2012-01, Vol.6 (1), p.17-22

2012

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Techniques to elucidate the conformation of prions

World journal of biological chemistry, 2015-08, Vol.6 (3), p.218-222

Daus, Martin L

2015

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Journal Club

Biospektrum, 2023-10, Vol.29 (6), p.640-643

2023

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Journal Club

Biospektrum, 2023-10, Vol.29 (6), p.640-643

2023

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The MalF P2 Loop of the ATP-Binding Cassette Transporter MalFGK2 from Escherichia coli and Salmonella enterica Serovar Typhimurium Interacts with Maltose Binding Protein (MalE) throughout the Catalytic Cycle

Journal of Bacteriology, 2009-02, Vol.191 (3), p.754-761

2009

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Synthetic Scrapie Infectivity: Interaction between Recombinant PrP and Scrapie Brain-Derived RNA

Virulence, 2015-02, Vol.6 (2), p.132-144

2015

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Journal Club

Biospektrum, 2023, Vol.29 (6), p.640-643

2023

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Journal Club

Biospektrum, 2021-11, Vol.27 (7), p.728-733

2021

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Journal Club

Biospektrum, 2021, Vol.27 (7), p.728-733

2021

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Journal Club

Biospektrum, 2021-11, Vol.27 (7), p.728-733

2021

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Journal Club

Biospektrum, 2019-11, Vol.25 (7), p.744-750

2019

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Infrarotspektroskopie zur Strukturuntersuchung von Prionen: Proteinstruktur

Biospektrum, 2014-02, Vol.20 (1), p.36-38

2014

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Infrarotspektroskopie zur Strukturuntersuchung von Prionen

Biospektrum, 2014-02, Vol.20 (1), p.36-38

2014

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Journal Club

Biospektrum, 2020-05, Vol.26 (3), p.280-286

2020

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Quantitative detection and biological propagation of scrapie seeding activity in vitro facilitate use of prions as model pathogens for disinfection

Sialylation Controls Prion Fate in Vivo

Reversible off and on switching of prion infectivity via removing and reinstalling prion sialylation

Disease Transmission by Misfolded Prion-Protein Isoforms, Prion-Like Amyloids, Functional Amyloids and the Central Dogma

Presence and seeding activity of pathological prion protein (PrP(TSE)) in skeletal muscles of white-tailed deer infected with chronic wasting disease

Infrared Microspectroscopy Detects Protein Misfolding Cyclic Amplification (PMCA)-induced Conformational Alterations in Hamster Scrapie Progeny Seeds

Maltose binding protein (MalE) interacts with periplasmic loops P2 and P1 respectively of the MalFG subunits of the maltose ATP binding cassette transporter (MalFGK₂) from Escherichia coli/Salmonella during the transport cycle

Periplasmic Loop P2 of the MalF Subunit of the Maltose ATP Binding Cassette Transporter Is Sufficient To Bind the Maltose Binding Protein MalE

Towards further reduction and replacement of animal bioassays in prion research by cell and protein misfolding cyclic amplification assays

ATP-driven MalK Dimer Closure and Reopening and Conformational Changes of the “EAA” Motifs Are Crucial for Function of the Maltose ATP-binding Cassette Transporter (MalFGK2)

ATP Induces Conformational Changes of Periplasmic Loop Regions of the Maltose ATP-binding Cassette Transporter

Chronic wasting disease: Fingerprinting the culprit in risk assessments

Techniques to elucidate the conformation of prions

Journal Club

Journal Club

The MalF P2 Loop of the ATP-Binding Cassette Transporter MalFGK2 from Escherichia coli and Salmonella enterica Serovar Typhimurium Interacts with Maltose Binding Protein (MalE) throughout the Catalytic Cycle

Synthetic Scrapie Infectivity: Interaction between Recombinant PrP and Scrapie Brain-Derived RNA

Journal Club

Journal Club

Journal Club

Journal Club

Journal Club

Infrarotspektroskopie zur Strukturuntersuchung von Prionen: Proteinstruktur

Infrarotspektroskopie zur Strukturuntersuchung von Prionen

Journal Club

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