• Applying the tools of chemistry (mass spectrometry and covalent modification by small molecule reagents) to the detection of prions and the study of their structure
  • Taking advantage of physiological proteolytic processing of the prion protein for a therapeutic perspective in prion and Alzheimer diseases
  • Can plants serve as a vector for prions causing chronic wasting disease?
  • Different misfolding mechanisms converge on common conformational changes: Human prion protein pathogenic mutants Y218N and E196K
  • D-amino acid-based peptide inhibitors as early or preventative therapy in Alzheimer disease

Applying the tools of chemistry (mass spectrometry and covalent modification by small molecule reagents) to the detection of prions and the study of their structure

Christopher J Silva

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Taking advantage of physiological proteolytic processing of the prion protein for a therapeutic perspective in prion and Alzheimer diseases

Maxime Béland and Xavier Roucou

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Can plants serve as a vector for prions causing chronic wasting disease?

Jay Rasmussen, Brandon H Gilroyed, Tim Reuter, Sandor Dudas, Norman F Neumann, Aru Balachandran, Nat NV Kav, Catherine Graham, Stefanie Czub and Tim A McAllister

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Different misfolding mechanisms converge on common conformational changes: Human prion protein pathogenic mutants Y218N and E196K

Chin Jung Cheng and Valerie Daggett

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D-amino acid-based peptide inhibitors as early or preventative therapy in Alzheimer disease

Jitendra Kumar and Valerie Sim

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Current Issue

Prion

January/February 2014

Volume 8, Issue 1

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About the cover image
Native structure of the human PrP. Starting structure for WT PrP MD simulations. Structure of residues 128–228 was obtained from PDB 1QLX. Structure of the flexible N-terminus (residues 90–127), and C-terminus (residues 229–230) were constructed manually. Helices HB and HC are colored in blue and HA is colored in cyan. Native strands (S1 and S2) are colored in dark red. The remaining loop regions are in gray. Mutation sites are indicated in orange. For more information see Cheng et al. 

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