scholarly journals Sedimentation Velocity Analysis with Fluorescence Detection of Mutant Huntingtin Exon 1 Aggregation inDrosophila melanogasterandCaenorhabditis elegans

Biochemistry ◽  
2017 ◽  
Vol 56 (35) ◽  
pp. 4676-4688 ◽  
Author(s):  
Surin A. Kim ◽  
Victoria F. D’Acunto ◽  
Bashkim Kokona ◽  
Jennifer Hofmann ◽  
Nicole R. Cunningham ◽  
...  
Keyword(s):  
Fluorescence Detection ◽  
Sedimentation Velocity ◽  
Velocity Analysis ◽  
Mutant Huntingtin ◽  
Exon 1

scholarly journals Sedimentation Velocity Analysis of Polyglutamine Assembly in C. elegans using a Fluorescence Detection System

2013 ◽  
Vol 104 (2) ◽  
pp. 566a
Author(s):  
Bashkim Kokona ◽  
Zachary P. Smith ◽  
Robert Fairman ◽  
Thomas Laue ◽  
Chris Link ◽  
...  
Keyword(s):  
Fluorescence Detection ◽  
Detection System ◽  
Sedimentation Velocity ◽  
Velocity Analysis ◽  
C Elegans ◽  
Fluorescence Detection System

Sedimentation velocity analysis of amyloid oligomers and fibrils using fluorescence detection

Methods ◽  
2011 ◽  
Vol 54 (1) ◽  
pp. 67-75 ◽  
Author(s):  
Yee-Foong Mok ◽  
Timothy M. Ryan ◽  
Shuo Yang ◽  
Danny M. Hatters ◽  
Geoffrey J. Howlett ◽  
...  
Keyword(s):  
Fluorescence Detection ◽  
Sedimentation Velocity ◽  
Velocity Analysis ◽  
Amyloid Oligomers

scholarly journals The Nt17 domain and its helical conformation regulate the aggregation, cellular properties and neurotoxicity of mutant huntingtin exon 1

2021 ◽  
pp. 167222
Author(s):  
Sophie Vieweg ◽  
Anne-Laure Mahul-Mellier ◽  
Francesco S. Ruggeri ◽  
Nathan Riguet ◽  
Sean M. DeGuire ◽  
...  
Keyword(s):  
Helical Conformation ◽  
Mutant Huntingtin ◽  
Exon 1

scholarly journals The structure of L-lactate oxidase from Mycobacterium smegmatis

1977 ◽  
Vol 165 (2) ◽  
pp. 375-383 ◽  
Author(s):  
P A Sullivan ◽  
C Y Soon ◽  
W J Schreurs ◽  
J F Cutfield ◽  
M G Shepherd
Keyword(s):  
Electron Microscopy ◽  
Mycobacterium Smegmatis ◽  
Sedimentation Velocity ◽  
Equilibrium Analysis ◽  
Sedimentation Equilibrium ◽  
Cross Linking ◽  
Velocity Analysis ◽  
Approach To Equilibrium ◽  
Lactate Oxidase ◽  
Dimethyl Suberimidate

1. An improved purification was developed for L-lactate oxidase from Mycobacterium smegmatis. 2. The mol.wt. of the native enzyme by a sedimentation-equilibrium analysis was 345 000, and other ultracentrifuge methods gave values in the range 345 000-350 000. 3. An amino acid analysis, determinations of protein and flavin, a sedimentation-velocity analysis and an approach to equilibrium analysis gave values for the subunit mol.wt. in the range 43 500-47 000. 4. It was concluded that L-lactate oxidase contains eight subunits of mol.wt. 43 500. 5. Cross-linking of the subunits with dimethyl suberimidate and electron-microscopy studies were consistent with an octameric structure.

scholarly journals Self-assembly of Mutant Huntingtin Exon-1 Fragments into Large Complex Fibrillar Structures Involves Nucleated Branching

2018 ◽  
Vol 430 (12) ◽  
pp. 1725-1744 ◽  
Author(s):  
Anne S. Wagner ◽  
Antonio Z. Politi ◽  
Anne Ast ◽  
Kenny Bravo-Rodriguez ◽  
Katharina Baum ◽  
...  
Keyword(s):  
Self Assembly ◽  
Mutant Huntingtin ◽  
Large Complex ◽  
Exon 1

scholarly journals Sedimentation velocity analysis of TMPyP4-induced dimer formation of human telomeric G-quadruplex

RSC Advances ◽  
2017 ◽  
Vol 7 (87) ◽  
pp. 55098-55105 ◽  
Author(s):  
Yating Gao ◽  
Tianlei Guang ◽  
Xiaodong Ye
Keyword(s):  
Analytical Ultracentrifugation ◽  
Sedimentation Velocity ◽  
Velocity Analysis ◽  
Dimer Formation ◽  
G Quadruplex

Analytical ultracentrifugation sedimentation velocity (AUC-SV) was used to study the interactions between TMPyP4 and AGGG(TTAGGG)3 (Tel22) and the TMPyP4-induced dimer formation of G-quadruplex.

scholarly journals Topological Insights into Mutant Huntingtin Exon 1 and PolyQ Aggregates by Cryo-Electron Tomography

2020 ◽  
Author(s):  
Jesús G. Galaz-Montoya ◽  
Sarah H. Shahmoradian ◽  
Koning Shen ◽  
Judith Frydman ◽  
Wah Chiu
Keyword(s):  
Trinucleotide Repeat ◽  
Electron Tomography ◽  
Mutant Huntingtin ◽  
And Topology ◽  
Cryo Electron Tomography ◽  
Exon 1 ◽  
Subtomogram Averaging ◽  
The Brain ◽  
Polyq Tract

ABSTRACTHuntington disease (HD) is a neurodegenerative trinucleotide repeat disorder caused by an expanded poly-glutamine (polyQ) tract in the mutant huntingtin (mHTT) protein. The formation and topology of filamentous mHTT inclusions in the brain (hallmarks of HD implicated in neurotoxicity) remain elusive. Using cryo-electron tomography and subtomogram averaging, here we show that mHTT exon 1 and polyQ-only aggregates in vitro are structurally heterogenous and filamentous, similar to prior observations with other methods. Yet, we observed some filaments in both types of aggregates under ∼2 nm in width, thinner than previously reported, while other regions form large sheets. In addition, our data show a prevalent subpopulation of filaments exhibiting a lumpy, slab-shaped morphology in both aggregates, supportive of the “polyQ core” model. This provides a basis for future cryoET studies of various aggregated mHTT and polyQ constructs to improve their structure-based modeling and their identification in cells without fusion tags.

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