Two amyloid states of the prion protein display significantly different folding patterns
VG Ostapchenko, MR Sawaya, N Makarava… - Journal of molecular …, 2010 - Elsevier
It has been well established that a single amino acid sequence can give rise to several
conformationally distinct amyloid states. The extent to which amyloid structures formed …
conformationally distinct amyloid states. The extent to which amyloid structures formed …
Two amyloid States of the prion protein display significantly different folding patterns.
VG Ostapchenko, MR Sawaya, N Makarava… - Journal of Molecular …, 2010 - europepmc.org
It has been well established that a single amino acid sequence can give rise to several
conformationally distinct amyloid states. The extent to which amyloid structures formed …
conformationally distinct amyloid states. The extent to which amyloid structures formed …
[PDF][PDF] Two Amyloid States of the Prion Protein Display Significantly Different Folding Patterns
IV Baskakov - J. Mol. Biol, 2010 - Citeseer
It has been well established that conformationally different amyloid states can be produced
by the same amino acid sequence. 1–5 The principle underlying the ability of a protein to …
by the same amino acid sequence. 1–5 The principle underlying the ability of a protein to …
Two Amyloid States of the Prion Protein Display Significantly Different Folding Patterns
VG Ostapchenko, MR Sawaya, N Makarava… - Journal of Molecular …, 2010 - infona.pl
It has been well established that a single amino acid sequence can give rise to several
conformationally distinct amyloid states. The extent to which amyloid structures formed …
conformationally distinct amyloid states. The extent to which amyloid structures formed …
[HTML][HTML] Two amyloid states of the prion protein display significantly different folding patterns
VG Ostapchenko, MR Sawaya… - Journal of molecular …, 2010 - ncbi.nlm.nih.gov
It has been well established that a single amino acid sequence can give rise to several
conformationally distinct amyloid states. The extent to which amyloid structures formed …
conformationally distinct amyloid states. The extent to which amyloid structures formed …
Two amyloid States of the prion protein display significantly different folding patterns
VG Ostapchenko, MR Sawaya… - Journal of …, 2010 - pubmed.ncbi.nlm.nih.gov
It has been well established that a single amino acid sequence can give rise to several
conformationally distinct amyloid states. The extent to which amyloid structures formed …
conformationally distinct amyloid states. The extent to which amyloid structures formed …
[引用][C] Two amyloid states of the prion protein display significantly different folding patterns
VG Ostapchenko, N Makarava, R Savtchenko… - Journal of Molecular …, 2010 - elibrary.ru
We thank Anne Cohen for assistance in X-ray data collection and Pamela Wright for editing
the manuscript. This work was supported by National Institutes of Health grant NS045585 to …
the manuscript. This work was supported by National Institutes of Health grant NS045585 to …
Two Amyloid States of the Prion Protein Display Significantly Different Folding Patterns
VG Ostapchenko, MR Sawaya, N Makarava… - JOURNAL OF …, 2010 - diva-portal.org
It has been well established that a single amino acid sequence can give rise to several
conformationally distinct amyloid states. The extent to which amyloid structures formed …
conformationally distinct amyloid states. The extent to which amyloid structures formed …
Two Amyloid States of the Prion Protein Display Significantly Different Folding Patterns
VG Ostapchenko, MR Sawaya, N Makarava… - JOURNAL OF …, 2010 - swepub.kb.se
It has been well established that a single amino acid sequence can give rise to several
conformationally distinct amyloid states. The extent to which amyloid structures formed …
conformationally distinct amyloid states. The extent to which amyloid structures formed …
[引用][C] Two Amyloid States of the Prion Protein Display Significantly Different Folding Patterns
VG Ostapchenko, MR Sawaya, N Makarava… - Journal of Molecular …, 2010 - cir.nii.ac.jp