Pages that link to "Q46940738"

The following pages link to Elongated oligomers assemble into mammalian PrP amyloid fibrils (Q46940738):

Displaying 35 items.

• The Structural Architecture of an Infectious Mammalian Prion Using Electron Cryomicroscopy (Q27312168) (← links)
• Ex vivo mammalian prions are formed of paired double helical prion protein fibrils. (Q27336314) (← links)
• Globular domain of the prion protein needs to be unlocked by domain swapping to support prion protein conversion (Q30468679) (← links)
• The structure of the infectious prion protein: experimental data and molecular models (Q30768165) (← links)
• Probing structural differences in prion protein isoforms by tyrosine nitration (Q33280623) (← links)
• N-terminal domain of prion protein directs its oligomeric association (Q34170632) (← links)
• Structural dependence of HET-s amyloid fibril infectivity assessed by cryoelectron microscopy (Q34602521) (← links)
• Disulfide mapping reveals the domain swapping as the crucial process of the structural conversion of prion protein (Q35194900) (← links)
• A novel and rapid method for obtaining high titre intact prion strains from mammalian brain. (Q35580105) (← links)
• Molecular architecture of human prion protein amyloid: a parallel, in-register beta-structure (Q36277140) (← links)
• Insights into the architecture of the Ure2p yeast protein assemblies from helical twisted fibrils (Q36458069) (← links)
• Folding versus aggregation: polypeptide conformations on competing pathways (Q36858313) (← links)
• Nanoimaging in protein-misfolding and -conformational diseases (Q36988337) (← links)
• Globular tetramers of beta(2)-microglobulin assemble into elaborate amyloid fibrils (Q37305282) (← links)
• Conformational properties of beta-PrP. (Q37372182) (← links)
• Prion protein misfolding and disease (Q37373871) (← links)
• Natural and synthetic prion structure from X-ray fiber diffraction (Q37386047) (← links)
• Comparison of Alzheimer Abeta(1-40) and Abeta(1-42) amyloid fibrils reveals similar protofilament structures (Q37394004) (← links)
• The diversity and relationship of prion protein self-replicating states (Q38259891) (← links)
• The structure of human prions: from biology to structural models-considerations and pitfalls (Q38261710) (← links)
• Regulation of PrP(C) signaling and processing by dimerization (Q38264472) (← links)
• Mammalian prions and their wider relevance in neurodegenerative diseases (Q39004344) (← links)
• Structural Biology of PrP Prions (Q39047631) (← links)
• Toward the Atomic Structure of PrPSc (Q39092670) (← links)
• Left handed beta helix models for mammalian prion fibrils (Q41853771) (← links)
• Massive conformation change in the prion protein: Using dual-basin structure-based models to find misfolding pathways (Q46106488) (← links)
• Curcumin binds to the alpha-helical intermediate and to the amyloid form of prion protein - a new mechanism for the inhibition of PrP(Sc) accumulation (Q46905202) (← links)
• In situ Abeta pores in AD brain are cylindrical assembly of Abeta protofilaments (Q48809829) (← links)
• A new era for understanding amyloid structures and disease (Q57787227) (← links)
• From Molecular to Supramolecular Amyloid Structures: Contributions from Fiber Diffraction and Electron Microscopy (Q57944846) (← links)
• Structural features distinguishing infectious ex vivo mammalian prions from non-infectious fibrillar assemblies generated in vitro (Q61445208) (← links)
• Corrigendum to “Elongated Oligomers Assemble into Mammalian PrP Amyloid Fibrils” [J. Mol. Biol. 357 (2006) 975–985] (Q61685341) (← links)
• Cryo-EM structure of a human prion fibril with a hydrophobic, protease-resistant core (Q91875083) (← links)
• Recent Advances in Understanding Mammalian Prion Structure: A Mini Review (Q92135625) (← links)
• Cryo-EM structure of an amyloid fibril formed by full-length human prion protein (Q96230993) (← links)