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Jan Bieschke

Showing results (31-40 of 47) with videos related to

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Elife|August 7, 2024
Syntaxin-6 delays prion protein fibril formation and prolongs the presence of toxic aggregation intermediatesDaljit Sangar, Elizabeth Hill, Kezia Jack, et al.
Nature Structural & Molecular Biology|May 31, 2008
EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomersDagmar E Ehrnhoefer, Jan Bieschke, Annett Boeddrich, et al.
Chembiochem : a European Journal of Chemical Biology|February 4, 2011
Bacterial inclusion bodies of Alzheimer's disease β-amyloid peptides can be employed to study native-like aggregation intermediate statesMuralidhar Dasari, Alba Espargaro, Raimon Sabate, et al.
Journal of Molecular Biology|November 19, 2020
Megadalton-sized Dityrosine Aggregates of α-Synuclein Retain High Degrees of Structural Disorder and Internal DynamicsSilvia Verzini, Maliha Shah, Francois-Xavier Theillet, et al.
Journal of Molecular Biology|May 27, 2023
Loss of Residues 119-136, Including the First β-strand of Human Prion Protein, Generates an Aggregation-competent Partially "Open" FormLaszlo L P Hosszu, Daljit Sangar, Mark Batchelor, et al.
Proceedings of the National Academy of Sciences of the United States of America|June 30, 2006
Structure-function-folding relationship in a WW domainMarcus Jäger, Yan Zhang, Jan Bieschke, et al.
Journal of Virology|May 28, 2005
Systematic identification of antiprion drugs by high-throughput screening based on scanning for intensely fluorescent targetsUwe Bertsch, Konstanze F Winklhofer, Thomas Hirschberger, et al.
The Journal of Biological Chemistry|May 15, 2026
Prion propagation is controlled by discrete structural regions of PrP rather than overall stabilitySavroop K Bhamra, Parineeta Arora, May Liew, et al.
The Journal of Biological Chemistry|March 3, 2019
Detection of TAR DNA-binding protein 43 (TDP-43) oligomers as initial intermediate species during aggregate formationRachel L French, Zachary R Grese, Himani Aligireddy, et al.
Proceedings of the National Academy of Sciences of the United States of America|March 23, 2004
Metabolite-initiated protein misfolding may trigger Alzheimer's diseaseQinghai Zhang, Evan T Powers, Jorge Nieva, et al.
Pageof 5

Showing results (31-40 of 47) with videos related to

Sort By:
Pageof 5
Elife|August 7, 2024
Syntaxin-6 delays prion protein fibril formation and prolongs the presence of toxic aggregation intermediatesDaljit Sangar, Elizabeth Hill, Kezia Jack, et al.
Nature Structural & Molecular Biology|May 31, 2008
EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomersDagmar E Ehrnhoefer, Jan Bieschke, Annett Boeddrich, et al.
Chembiochem : a European Journal of Chemical Biology|February 4, 2011
Bacterial inclusion bodies of Alzheimer's disease β-amyloid peptides can be employed to study native-like aggregation intermediate statesMuralidhar Dasari, Alba Espargaro, Raimon Sabate, et al.
Journal of Molecular Biology|November 19, 2020
Megadalton-sized Dityrosine Aggregates of α-Synuclein Retain High Degrees of Structural Disorder and Internal DynamicsSilvia Verzini, Maliha Shah, Francois-Xavier Theillet, et al.
Journal of Molecular Biology|May 27, 2023
Loss of Residues 119-136, Including the First β-strand of Human Prion Protein, Generates an Aggregation-competent Partially "Open" FormLaszlo L P Hosszu, Daljit Sangar, Mark Batchelor, et al.
Proceedings of the National Academy of Sciences of the United States of America|June 30, 2006
Structure-function-folding relationship in a WW domainMarcus Jäger, Yan Zhang, Jan Bieschke, et al.
Journal of Virology|May 28, 2005
Systematic identification of antiprion drugs by high-throughput screening based on scanning for intensely fluorescent targetsUwe Bertsch, Konstanze F Winklhofer, Thomas Hirschberger, et al.
The Journal of Biological Chemistry|May 15, 2026
Prion propagation is controlled by discrete structural regions of PrP rather than overall stabilitySavroop K Bhamra, Parineeta Arora, May Liew, et al.
The Journal of Biological Chemistry|March 3, 2019
Detection of TAR DNA-binding protein 43 (TDP-43) oligomers as initial intermediate species during aggregate formationRachel L French, Zachary R Grese, Himani Aligireddy, et al.
Proceedings of the National Academy of Sciences of the United States of America|March 23, 2004
Metabolite-initiated protein misfolding may trigger Alzheimer's diseaseQinghai Zhang, Evan T Powers, Jorge Nieva, et al.
Pageof 5