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Laszlo L P Hosszu

Showing results (1-10 of 19) with videos related to

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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|March 27, 2009
Folding kinetics of the human prion protein probed by temperature jumpTanya Hart, Laszlo L P Hosszu, Clare R Trevitt, et al.
Magnetic Resonance (Gottingen, Germany)|October 31, 2023
High-affinity tamoxifen analogues retain extensive positional disorder when bound to calmodulinLilia Milanesi, Clare R Trevitt, Brian Whitehead, et al.
The Biochemical Journal|July 11, 2006
A reassessment of copper(II) binding in the full-length prion proteinMark A Wells, Graham S Jackson, Samantha Jones, et al.
The Biochemical Journal|August 24, 2006
Multiple forms of copper (II) co-ordination occur throughout the disordered N-terminal region of the prion protein at pH 7.4Mark A Wells, Clare Jelinska, Laszlo L P Hosszu, 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|April 17, 2009
Conformational properties of beta-PrPLaszlo L P Hosszu, Clare R Trevitt, Samantha Jones, et al.
Biochemistry|December 14, 2005
Definable equilibrium states in the folding of human prion proteinLaszlo L P Hosszu, Mark A Wells, Graham S Jackson, et al.
The Journal of Biological Chemistry|May 5, 2004
The residue 129 polymorphism in human prion protein does not confer susceptibility to Creutzfeldt-Jakob disease by altering the structure or global stability of PrPCLaszlo L P Hosszu, Graham S Jackson, Clare R Trevitt, et al.
Biochemistry|August 20, 2010
The H187R mutation of the human prion protein induces conversion of recombinant prion protein to the PrP(Sc)-like formLaszlo L P Hosszu, M Howard Tattum, Samantha Jones, et al.
Pageof 2

Showing results (1-10 of 19) with videos related to

Sort By:
Pageof 2
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|March 27, 2009
Folding kinetics of the human prion protein probed by temperature jumpTanya Hart, Laszlo L P Hosszu, Clare R Trevitt, et al.
Magnetic Resonance (Gottingen, Germany)|October 31, 2023
High-affinity tamoxifen analogues retain extensive positional disorder when bound to calmodulinLilia Milanesi, Clare R Trevitt, Brian Whitehead, et al.
The Biochemical Journal|July 11, 2006
A reassessment of copper(II) binding in the full-length prion proteinMark A Wells, Graham S Jackson, Samantha Jones, et al.
The Biochemical Journal|August 24, 2006
Multiple forms of copper (II) co-ordination occur throughout the disordered N-terminal region of the prion protein at pH 7.4Mark A Wells, Clare Jelinska, Laszlo L P Hosszu, 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|April 17, 2009
Conformational properties of beta-PrPLaszlo L P Hosszu, Clare R Trevitt, Samantha Jones, et al.
Biochemistry|December 14, 2005
Definable equilibrium states in the folding of human prion proteinLaszlo L P Hosszu, Mark A Wells, Graham S Jackson, et al.
The Journal of Biological Chemistry|May 5, 2004
The residue 129 polymorphism in human prion protein does not confer susceptibility to Creutzfeldt-Jakob disease by altering the structure or global stability of PrPCLaszlo L P Hosszu, Graham S Jackson, Clare R Trevitt, et al.
Biochemistry|August 20, 2010
The H187R mutation of the human prion protein induces conversion of recombinant prion protein to the PrP(Sc)-like formLaszlo L P Hosszu, M Howard Tattum, Samantha Jones, et al.
Pageof 2