scholarly journals Mouse Prion Protein Polymorphism Phe-108/Val-189 Affects the Kinetics of Fibril Formation and the Response to Seeding

2013 ◽  
Vol 288 (7) ◽  
pp. 4772-4781 ◽  
Author(s):  
Leonardo M. Cortez ◽  
Jitendra Kumar ◽  
Ludovic Renault ◽  
Howard S. Young ◽  
Valerie L. Sim
Keyword(s):  
Prion Protein ◽  
Fibril Formation ◽  
Protein Polymorphism ◽  
Kinetics Of ◽  
Kinetics Of Fibril Formation

Kinetics of Fibril Formation of Bovine κ-Casein Indicate a Conformational Rearrangement as a Critical Step in the Process

2008 ◽  
Vol 381 (5) ◽  
pp. 1267-1280 ◽  
Author(s):  
Joelle Leonil ◽  
Gwenaele Henry ◽  
Dianne Jouanneau ◽  
Marie-Madeleine Delage ◽  
Vincent Forge ◽  
...  
Keyword(s):  
Fibril Formation ◽  
Conformational Rearrangement ◽  
Critical Step ◽  
Kinetics Of ◽  
Kinetics Of Fibril Formation

scholarly journals Kinetics of Fibril Formation by Polyalanine Peptides

2005 ◽  
Vol 280 (10) ◽  
pp. 9074-9082 ◽  
Author(s):  
Hung D. Nguyen ◽  
Carol K. Hall
Keyword(s):  
Fibril Formation ◽  
Kinetics Of ◽  
Kinetics Of Fibril Formation

scholarly journals Exploring the potential of deep-blue autofluorescence for monitoring amyloid fibril formation and dissociation

PeerJ ◽  
2019 ◽  
Vol 7 ◽  
pp. e7554
Author(s):  
Mantas Ziaunys ◽  
Tomas Sneideris ◽  
Vytautas Smirnovas
Keyword(s):  
Neurodegenerative Disorders ◽  
Amyloid Fibrils ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Formation ◽  
Amyloid Aggregation ◽  
Deep Blue ◽  
Amyloid Fibril Formation ◽  
Kinetics Of ◽  
Kinetics Of Fibril Formation

Protein aggregation into amyloid fibrils has been linked to multiple neurodegenerative disorders. Determining the kinetics of fibril formation, as well as their structural stability are important for the mechanistic understanding of amyloid aggregation. Tracking both fibril association and dissociation is usually performed by measuring light scattering of the solution or fluorescence of amyloid specific dyes, such as thioflavin-T. A possible addition to these methods is the recently discovered deep-blue autofluorescence (dbAF), which is linked to amyloid formation. In this work we explore the potential of this phenomenon to monitor amyloid fibril formation and dissociation, as well as show its possible relation to fibril size rather than amyloid structure.

Structural mechanisms of oligomer and amyloid fibril formation by the prion protein

2018 ◽  
Vol 54 (49) ◽  
pp. 6230-6242 ◽  
Author(s):  
Ishita Sengupta ◽  
Jayant B. Udgaonkar
Keyword(s):  
Prion Protein ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Aggregation Mechanism ◽  
Amyloid Fibril Formation ◽  
Structural Mechanisms

The aggregation mechanism of the prion protein is highly heterogeneous.

scholarly journals Strain Specific Resistance to Murine Scrapie Associated with a Naturally Occurring Human Prion Protein Polymorphism at Residue 171

2011 ◽  
Vol 7 (9) ◽  
pp. e1002275 ◽  
Author(s):  
James F. Striebel ◽  
Brent Race ◽  
Kimberly D. Meade-White ◽  
Rachel LaCasse ◽  
Bruce Chesebro
Keyword(s):  
Prion Protein ◽  
Specific Resistance ◽  
Protein Polymorphism ◽  
Naturally Occurring ◽  
Human Prion Protein

scholarly journals Effect of Association State and Conformational Stability on the Kinetics of Immunoglobulin Light Chain Amyloid Fibril Formation at Physiological pH

2002 ◽  
Vol 277 (15) ◽  
pp. 12657-12665 ◽  
Author(s):  
Pierre O. Souillac ◽  
Vladimir N. Uversky ◽  
Ian S. Millett ◽  
Ritu Khurana ◽  
Sebastian Doniach ◽  
...  
Keyword(s):  
Light Chain ◽  
Amyloid Fibril ◽  
Conformational Stability ◽  
Fibril Formation ◽  
Immunoglobulin Light Chain ◽  
Amyloid Fibril Formation ◽  
Kinetics Of ◽  
Association State

Prion Protein Aggregation Induced by Copper(II) and Heparan Sulfate. Pressure-dependent Switch of Reaction Pathways

2008 ◽  
Vol 63 (6) ◽  
pp. 747-755 ◽  
Author(s):  
Driss El Moustaine ◽  
Joan Torrent ◽  
Reinhard Lange
Keyword(s):  
Heparan Sulfate ◽  
Prion Protein ◽  
Conformational Changes ◽  
Atmospheric Pressure ◽  
Amyloid Fibrils ◽  
Copper Ions ◽  
Fibril Formation ◽  
Cellular Prion Protein ◽  
Reaction Pathways ◽  
Structural Alterations

Copper ions (Cu2+) and heparan sulfate (HS) are suspected to act as regulatory agents in the conversion of cellular prion protein (PrPC) to its infectious isoform. However, the mechanism of this reaction is still largely unknown. Our previous report suggested multidimensional pathways for structural alterations of PrP, which may be modulated by high pressure (HP). Here we use HP to investigate the effects of Cu2+ and HS binding on PrP conformational changes and assembly. In the presence of Cu2+, amyloid fibrils are formed only under HP. In contrast, in the presence of HS, fibrils are formed at atmospheric pressure, but not under HP. Both compounds appear to compete for the same binding site, since HS-supported fibril formation is quenched by Cu2+. Inversely, Cu2+- mediated fibril formation under HP is inhibited by HS.

Aggregation and Amyloid Fibril Formation of the Prion Protein Is Accelerated in the Presence of Glycogen

2008 ◽  
Vol 11 (2) ◽  
pp. 365-369 ◽  
Author(s):  
Giannantonio Panza ◽  
Jan Stöhr ◽  
Eva Birkmann ◽  
Detlev Riesner ◽  
Dieter Willbold ◽  
...  
Keyword(s):  
Prion Protein ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation
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