scholarly journals Characterization of Oligomers of Heterogeneous Size as Precursors of Amyloid Fibril Nucleation of an SH3 Domain: An Experimental Kinetics Study

PLoS ONE ◽  
2012 ◽  
Vol 7 (11) ◽  
pp. e49690 ◽  
Author(s):  
David Ruzafa ◽  
Bertrand Morel ◽  
Lorena Varela ◽  
Ana I. Azuaga ◽  
Francisco Conejero-Lara
Keyword(s):  
Amyloid Fibril ◽  
Sh3 Domain ◽  
Kinetics Study ◽  
Experimental Kinetics ◽  
Heterogeneous Size

scholarly journals Amyloid fibril formation by an SH3 domain

1998 ◽  
Vol 95 (8) ◽  
pp. 4224-4228 ◽  
Author(s):  
J. I. Guijarro ◽  
M. Sunde ◽  
J. A. Jones ◽  
I. D. Campbell ◽  
C. M. Dobson
Keyword(s):  
Amyloid Fibril ◽  
Sh3 Domain ◽  
Fibril Formation ◽  
Amyloid Fibril Formation

scholarly journals Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation

2015 ◽  
Vol 112 (16) ◽  
pp. E1994-E2003 ◽  
Author(s):  
Serene W. Chen ◽  
Srdja Drakulic ◽  
Emma Deas ◽  
Myriam Ouberai ◽  
Francesco A. Aprile ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Self Assembly ◽  
Protein Misfolding ◽  
Amyloid Fibril ◽  
Amyloid Formation ◽  
Image Reconstruction Techniques ◽  
Cryo Electron Microscopy ◽  
Amyloid Oligomers ◽  
Β Sheet

We describe the isolation and detailed structural characterization of stable toxic oligomers of α-synuclein that have accumulated during the process of amyloid formation. Our approach has allowed us to identify distinct subgroups of oligomers and to probe their molecular architectures by using cryo-electron microscopy (cryoEM) image reconstruction techniques. Although the oligomers exist in a range of sizes, with different extents and nature of β-sheet content and exposed hydrophobicity, they all possess a hollow cylindrical architecture with similarities to certain types of amyloid fibril, suggesting that the accumulation of at least some forms of amyloid oligomers is likely to be a consequence of very slow rates of rearrangement of their β-sheet structures. Our findings reveal the inherent multiplicity of the process of protein misfolding and the key role the β-sheet geometry acquired in the early stages of the self-assembly process plays in dictating the kinetic stability and the pathological nature of individual oligomeric species.

Localized laryngeal amyloidosis: Partial characterization of an amyloid fibril protein al

1982 ◽  
Vol 19 (3) ◽  
pp. 447-450 ◽  
Author(s):  
Per Westermark ◽  
Knut Sletten ◽  
Peter Pitkänen ◽  
Jacob B. Natvig ◽  
Carl-Eric Lindholm
Keyword(s):  
Amyloid Fibril ◽  
Partial Characterization ◽  
Laryngeal Amyloidosis ◽  
Amyloid Fibril Protein ◽  
Localized Laryngeal Amyloidosis

scholarly journals Detection and Characterization of Partially Unfolded Oligomers of the SH3 Domain of α-Spectrin

2004 ◽  
Vol 86 (4) ◽  
pp. 2403-2413 ◽  
Author(s):  
Salvador Casares ◽  
Mourad Sadqi ◽  
Obdulio López-Mayorga ◽  
Francisco Conejero-Lara ◽  
Nico A.J. van Nuland
Keyword(s):  
Sh3 Domain ◽  
Partially Unfolded

scholarly journals Isolation and characterization of a novel HS1 SH3 domain binding protein, HS1BP3

1999 ◽  
Vol 11 (12) ◽  
pp. 1957-1964 ◽  
Author(s):  
Yoshihiro Takemoto ◽  
Masaaki Furuta ◽  
Mitsuru Sato ◽  
Masato Kubo ◽  
Yasuhiro Hashimoto
Keyword(s):  
Binding Protein ◽  
Sh3 Domain ◽  
Isolation And Characterization

scholarly journals Structural and Functional Characterization of an Unusual SH3 Domain from the Fungal Adaptor Protein Bem1

2010 ◽  
Vol 98 (3) ◽  
pp. 249a
Author(s):  
Maryna Gorelik ◽  
Ranjith Muhandiram ◽  
Alan Davidson
Keyword(s):  
Functional Characterization ◽  
Adaptor Protein ◽  
Sh3 Domain
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