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Articles by Dezerae Cox
Direct single-molecule visualization of Hsp90-mediated relief of an Hsp70-folding block
Abstract INTRODUCTION RESULTS DISCUSSION METHODS Acknowledgments Supplementary Materials REFERENCES Information & Authors Metrics & Citations View Options References Figures Tables Media Share Abstract Heat shock protein 70 (Hsp70) and Hsp90 are essential molecular chaperones that cooperate to fold diverse client proteins, yet how their activities are coordinated to remodel clients remains unclear.
Fingerprinting disease-derived protein aggregates reveals unique signature of Motor Neuron Disease
Abstract Inappropriate aggregation of TAR DNA-binding protein 43 (TDP-43) is a hallmark of motor neuron disease (MND). Current methods for quantifying heterogeneous aggregate populations in biofluids are limited, precluding their routine use in diagnosis and disease monitoring. Single molecule microscopy methods overcome these limitations to deliver quantitative morphological and compositional fingerprinting of molecular assemblies containing TDP-43.
Single‐Molecule Characterization and Super‐Resolution Imaging of Alzheimer's Disease‐Relevant Tau Aggregates in Human Samples
Introduction Hyperphosphorylation and aggregation of tau is a defining characteristic of a range of neurodegenerative diseases collectively known as tauopathies, including Alzheimer's disease (AD), progressive supranuclear palsy, and multiple forms of frontotemporal dementia, including Pick's disease.1-5 Tau is an essential protein involved in the stabilization of microtubules.6, 7 However, hyperphosphorylation of tau causes it to dissociate from microtubules leading to its aggregation.8...
Single-molecule observations of human small heat shock proteins in complex with aggregation-prone client proteins
Abstract Small heat shock proteins (sHsps) are molecular chaperones that act to prevent the aberrant aggregation of misfolded proteins. Whilst it is widely suggested that sHsps prevent aggregation by binding to misfolded client proteins, the dynamic and heterogeneous nature of sHsps has hindered attempts to establish the mechanistic details of how sHsp-client protein complexes form.
Characterization and super-resolution imaging of small tau aggregates in human samples.
Abstract Hyperphosphorylation and aggregation of the microtubule binding protein tau plays a key role in the development of Alzheimer's disease. While the structure of the filamentous aggregates formed in humans has recently been determined to atomic resolution, there is far less information available about the smaller aggregate precursors, thought to be the most neurotoxic.
Characterization and super-resolution imaging of small tau aggregates in human samples.
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Replicative aging impedes stress-induced assembly of a key human protein disaggregase
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Sequence grammar underlying the unfolding and phase separation of globular proteins
Method details Cell imaging For all imaging experiments, cells were plated at 3×104 cells per well in 8-well μ-slides (Ibidi) and transfected using Lipofectamine 3000 (Thermo Fisher Scientific) as per the manufacturer’s protocol. In the case of HEK293T cells, plates were pre-coated with poly-L-lysine to aid adhesion. Imaging was conducted on a Leica TCS SP5 Confocal microscope using a HCX APO CS 63 × 1.40 Oil objective lens unless stated otherwise.
Hidden information on protein function in censuses of proteome foldedness - Nature Communications
Abstract Methods that assay protein foldedness with proteomics have generated censuses of apparent protein folding stabilities in biological milieu. However, different censuses poorly correlate with each other. Here, we show that the reason for this is that methods targeting foldedness through monitoring amino acid sidechain reactivity also detect changes in conformation and ligand binding, which can be a substantial fraction of the data.
Nascent mutant Huntingtin exon 1 chains do not stall on ribosomes during translation but aggregates do recruit machinery involved in ribosome quality control and RNA
Loading metrics Open Access Peer-reviewed Research Article Angelique R. Ormsby, Dezerae Cox, James Daly, David Priest, Elizabeth Hinde, Danny M. Hatters Angelique R. Ormsby, Dezerae Cox, James Daly, David Priest, Elizabeth Hinde, Danny M. Hatters Published: July 31, 2020 https://doi.org/10.1371/journal.pone.0233583 Figures Abstract Mutations that cause Huntington’s Disease involve a polyglutamine (polyQ) sequence expansion beyond 35 repeats in exon 1 of Huntingtin.
N- and C-terminal regions of αB-crystallin and Hsp27 mediate inhibition of amyloid nucleation, fibril binding, and fibril disaggregation
Emily E. Selig1,2, Courtney O. Zlatic1,2, Dezerae Cox1,2, Yee-Foong Mok1,2, Paul R. Gooley1,2, Heath Ecroyd3,4 and Michael D. W.
N- and C-terminal regions of αB-crystallin and Hsp27 mediate inhibition of amyloid nucleation, fibril binding, and fibril disaggregation
Emily E. Selig1, Courtney O. Zlatic2, Dezerae Cox2, Yee-Foong Mok3, Paul R.
Single-Molecule Characterization of the Interactions between Extracellular Chaperones and Toxic α-Synuclein Oligomers
We first performed TCCD measurements to explore the interaction of the ECs with αS during the aggregation process. To achieve this, we made use of the A90C mutational variant αS, which allows the conjugation of a fluorophore through a single thiol group; previous studies have shown that the conjugation does not significantly change the behavior of the protein from that of wild-type αS (Cremades et al., 2012xDirect observation of the interconversion of normal and toxic forms of α-synuclein.
The small heat shock protein Hsp27 binds α-synuclein fibrils, preventing elongation and cytotoxicity
Proteostasis, or protein homeostasis, encompasses the maintenance of the conformational and functional integrity of the proteome and involves an integrated network of cellular pathways. Molecular chaperones, such as the small heat shock proteins (sHsps), are key elements of the proteostasis network that have crucial roles in inhibiting the aggregation of misfolded proteins.
The small heat shock protein Hsp27 binds α-synuclein fibrils, preventing elongation and cytotoxicity
Author contributions: H.E. and D.C. conceived the experiments and coordinated the study. H.E., D.C., D. R.W., J.B. and M.H.H. designed the experiments. D.C., D.R.W., M.H.H. and R.S.G. performed the experiments. C.M.D, D.K. and A.O helped in the design of experiments, and acquisition and interpretation of data. All authors analysed and reviewed the data. D.C. and H.E. wrote the paper. All authors read and approved the final manuscript.
A biosensor-based framework to measure latent proteostasis capacity
A toolkit for FRET biosensor comprising a combinatorial library of circularly permuted mTFP1 and Venus fluorescent proteins (cpFRET library in pTriEx4 expression vector) was used34. Barnase mutants were synthesized (Thermo Fisher Scientific) and inserted via PCR-mediated cloning with XmaI and NotI flanking restriction sites between BspEI (complementary to XmaI) and NotI sites of the cpFRET library such that barnase was fused to mTFP1 and Venus at the amino and carboxy termini, respectively.
Small Heat-shock Proteins Prevent α-Synuclein Aggregation via Transient Interactions and Their Efficacy Is Affected by the Rate of Aggregation
The aggregation of ?-synuclein (?-syn) into amyloid fibrils is associated with neurodegenerative diseases, collectively referred to as the ?-synucleinopathies. In vivo, molecular chaperones, such as the small heat-shock proteins (sHsps), normally act to prevent protein aggregation; however, it remains to be determined how aggregation-prone ?-syn evades sHsp chaperone action leading to its disease-associated deposition.
Small Heat Shock Proteins Prevent Alpha-Synuclein Aggregation via Transient Interactions and their Efficacy is Affected by the Rate of Aggregation
The aggregation of α-synuclein (α-syn) into amyloid fibrils is associated with neurodegenerative diseases, collectively referred to as the α-synucleinopathies. In vivo, molecular chaperones, such as the small heat-shock proteins (sHsps), normally act to prevent protein aggregation; however, it remains to be determined how aggregation-prone α-syn evades sHsp chaperone action leading to its disease-associated deposition.
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