J. Kumita

发表

Disulfide Bonds Reduce the Toxicity of the Amyloid Fibrils Formed by an Extracellular Protein**

C. Dobson, X. Salvatella, Anne Dhulesia, 2011, Angewandte Chemie.

The kinetics of helix unfolding of an azobenzene cross-linked peptide probed by nanosecond time-resolved optical rotatory dispersion.

D. Kliger, G. A. Woolley, E. Chen, 2003, Journal of the American Chemical Society.

Hypochlorite-induced structural modifications enhance the chaperone activity of human α2-macroglobulin

C. Dobson, Mark R. Wilson, J. Kumita, 2014, Proceedings of the National Academy of Sciences.

Intercellular propagated misfolding of wild-type Cu/Zn superoxide dismutase occurs via exosome-dependent and -independent mechanisms

A. Hill, I. Mackenzie, S. Plotkin, 2014, Proceedings of the National Academy of Sciences.

Engineering mono- and multi-valent inhibitors on a modular scaffold† †Electronic supplementary information (ESI) available. See DOI: 10.1039/d0sc03175e

L. Itzhaki, Albert Perez-Riba, S. McLaughlin, 2020, Chemical science.

Probing the unfolded protein response in long-lived naked mole-rats

C. Dobson, L. Itzhaki, E. Smith, 2020, Biochemical and biophysical research communications.

Structural Characterization of Covalently Stabilized Human Cystatin C Oligomers

Adam K. Sieradzan, C. Dobson, M. Chrabąszczewska, 2020, International journal of molecular sciences.

The Influence of Pathogenic Mutations in α-Synuclein on Biophysical and Structural Characteristics of Amyloid Fibrils.

C. Dobson, D. Chirgadze, T. Knowles, 2020, ACS nano.

Defining α-synuclein species responsible for Parkinson's disease phenotypes in mice

C. Dobson, José D. Camino, L. Volpicelli-Daley, 2019, The Journal of Biological Chemistry.

The influence of novel gemini surfactants containing cycloalkyl side-chains on the structural phases of DNA in solution.

C. Dobson, M. Kozak, J. Kumita, 2015, Colloids and surfaces. B, Biointerfaces.

NMR characterization of the conformational fluctuations of the human lymphocyte function‐associated antigen‐1 I‐domain

M. Vendruscolo, C. Camilloni, F. Bemporad, 2014, Protein science : a publication of the Protein Society.

Human pregnancy zone protein stabilizes misfolded proteins including preeclampsia- and Alzheimer’s-associated amyloid beta peptide

C. Dobson, D. Charnock-Jones, M. Ranson, 2019, Proceedings of the National Academy of Sciences.

Human zone protein stabilises misfolded proteins including preeclampsia- and Alzheimer’s-associated amyloid beta peptide

C. Dobson, D. Charnock-Jones, M. Ranson, 2019 .

Fabrication and Characterization of Reconstituted Silk Microgels for the Storage and Release of Small Molecules.

C. Dobson, Ulyana Shimanovich, T. Knowles, 2019, Macromolecular rapid communications.

The relevance of contact-independent cell-to-cell transfer of TDP-43 and SOD1 in amyotrophic lateral sclerosis

C. Dobson, J. Kumita, J. Yerbury, 2017, Biochimica et biophysica acta. Molecular basis of disease.

Flow cytometric measurement of the cellular propagation of TDP-43 aggregation

Mark R. Wilson, J. Kumita, J. Yerbury, 2017, Prion.

The Significance of the Location of Mutations for the Native-State Dynamics of Human Lysozyme

Francisco N. Newby, C. Dobson, C. Robinson, 2016, Biophysical journal.

Protease-activated alpha-2-macroglobulin can inhibit amyloid formation via two distinct mechanisms

C. Dobson, Mark R. Wilson, H. Ecroyd, 2013, FEBS letters.

α2-Macroglobulin and Haptoglobin Suppress Amyloid Formation by Interacting with Prefibrillar Protein Species*

C. Dobson, Mark R. Wilson, Sarah Meehan, 2009, Journal of Biological Chemistry.

Microsoft Word-conformer for resubmission 052219

José D. Camino, L. Volpicelli-Daley, N. Cremades, 2019 .

Effects of N-terminal acetylation on the aggregation of disease-related α-synuclein variants.

M. Vendruscolo, Rosie Bell, Catherine K. Xu, 2022, Journal of molecular biology.

N-Terminal Acetylation of α-Synuclein Slows down Its Aggregation Process and Alters the Morphology of the Resulting Aggregates

C. Dobson, M. Vendruscolo, Rosie Bell, 2022, Biochemistry.

Nature and significance of the interactions between amyloid fibrils and biological polyelectrolytes.

C. Dobson, F. Chiti, N. Taddei, 2006, Biochemistry.

A water-soluble azobenzene cross-linker for photocontrol of peptide conformation.

O. Smart, D. Burns, J. Kumita, 2003, Bioconjugate chemistry.

Normal and aberrant biological self-assembly: Insights from studies of human lysozyme and its amyloidogenic variants.

C. Dobson, M. Dumoulin, J. Kumita, 2006, Accounts of chemical research.

A prion-like domain in ELF3 functions as a thermosensor in Arabidopsis

Katja E. Jaeger, X. Lai, C. Zubieta, 2020, Nature.

Photo-control of helix content in a short peptide.

O. Smart, J R Kumita, O S Smart, 2000, Proceedings of the National Academy of Sciences of the United States of America.

Photo-control of peptide helix content by an azobenzene cross-linker: steric interactions with underlying residues are not critical.

O. Smart, J. Kumita, G. Woolley, 2002, Protein engineering.

Alpha-helix formation in a photoswitchable peptide tracked from picoseconds to microseconds by time-resolved IR spectroscopy.

P. Hamm, J. Helbing, J. Kumita, 2005, Proceedings of the National Academy of Sciences of the United States of America.

Protein amyloids develop an intrinsic fluorescence signature during aggregation.

C. Dobson, C. Kaminski, C. Bertoncini, 2013, The Analyst.

Using an azobenzene cross-linker to either increase or decrease peptide helix content upon trans-to-cis photoisomerization.

G Andrew Woolley, O. Smart, Daniel G Flint, 2002, Chemistry & biology.

Cholesterol catalyses Aβ42 aggregation through a heterogeneous nucleation pathway in the presence of lipid membranes

C. Dobson, M. Vendruscolo, S. Linse, 2018, Nature Chemistry.

Clusterin protects neurons against intracellular proteotoxicity

C. Dobson, Colin Smith, Mark R. Wilson, 2017, Acta Neuropathologica Communications.

Native-State Stability Determines the Extent of Degradation Relative to Secretion of Protein Variants from Pichia pastoris

C. Dobson, M. Alcocer, D. Archer, 2011, PloS one.

Exogenous misfolded protein oligomers can cross the intestinal barrier and cause a disease phenotype in C. elegans

C. Dobson, M. Vendruscolo, F. Chiti, 2021, Scientific Reports.

Comparative Studies in the A30P and A53T α-Synuclein C. elegans Strains to Investigate the Molecular Origins of Parkinson's Disease

Romain F. Laine, J. B. Kirkegaard, C. Dobson, 2021, Frontiers in Cell and Developmental Biology.

Multistep Inhibition of a-synuclein aggregation and toxicity in vitro 1 and in vivo by trodusquemine 2 3

J. B. Kirkegaard, C. Dobson, M. Vendruscolo, 2019 .

Multistep Inhibition of α-Synuclein Aggregation and Toxicity in Vitro and in Vivo by Trodusquemine.

J. B. Kirkegaard, C. Dobson, M. Vendruscolo, 2018, ACS chemical biology.

Secondary nucleation and elongation occur at different sites on Alzheimer’s amyloid-β aggregates

C. Dobson, D. Klenerman, M. Vendruscolo, 2019, Science Advances.

Single-Molecule Characterization of the Interactions between Extracellular Chaperones and Toxic a-Synuclein Oligomers Graphical

C. Dobson, D. Klenerman, M. Horrocks, 2018 .

Alpha-2-Macroglobulin Is Acutely Sensitive to Freezing and Lyophilization: Implications for Structural and Functional Studies

Christopher M. Dobson, C. Dobson, Mark R. Wilson, 2015, PloS one.

Systematic development of small molecules to inhibit specific microscopic steps of Aβ42 aggregation in Alzheimer’s disease

Tuomas P. J. Knowles, Michele Vendruscolo, Christopher M. Dobson, 2016, Proceedings of the National Academy of Sciences.

The Non-Core Regions of Human Lysozyme Amyloid Fibrils Influence Cytotoxicity

Christopher M. Dobson, Mireille Dumoulin, Xavier Salvatella, 2010, Journal of molecular biology.

Towards multiparametric fluorescent imaging of amyloid formation: studies of a YFP model of alpha-synuclein aggregation.

C. Dobson, C. Kaminski, C. Bertoncini, 2010, Journal of molecular biology.

Mapping pathogenic processes contributing to neurodegeneration in Drosophila models of Alzheimer's disease

L. Itzhaki, Hanna Appelqvist, K. Kågedal, 2019, FEBS open bio.

The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures

C. Dobson, Mark R. Wilson, Sarah Meehan, 2007, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Molecular determinants of the aggregation behavior of α‐ and β‐synuclein

C. Dobson, M. Vendruscolo, J. Christodoulou, 2008, Protein science : a publication of the Protein Society.

Amyloid-like Fibrils from an α-Helical Transmembrane Protein

C. Dobson, M. Vendruscolo, P. Booth, 2017, Biochemistry.

ANS binding reveals common features of cytotoxic amyloid species.

C. Dobson, G. Favrin, Mark R. Wilson, 2010, ACS chemical biology.

C. Dobson, D. Lomas, D. Crowther, 2012, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Methods and models in neurodegenerative and systemic protein aggregation diseases.

C. Dobson, E. Speretta, T. Knowles, 2010, Frontiers in bioscience.

Rationalising lysozyme amyloidosis: insights from the structure and solution dynamics of T70N lysozyme.

Mireille Dumoulin, Christopher M Dobson, Carol V Robinson, 2005, Journal of molecular biology.

Rapid Structural, Kinetic, and Immunochemical Analysis of Alpha-Synuclein Oligomers in Solution.

William E. Arter, C. Dobson, T. Knowles, 2020, Nano letters.

Rapid Fractionation and Characterisation of Alpha-Synuclein Oligomers in Solution

William E. Arter, C. Dobson, T. Knowles, 2020, bioRxiv.

Single-Molecule Characterization of the Interactions between Extracellular Chaperones and Toxic α-Synuclein Oligomers

C. Dobson, D. Klenerman, M. Horrocks, 2018, Cell reports.

The Pathological G51D Mutation in Alpha-Synuclein Oligomers Confers Distinct Structural Attributes and Cellular Toxicity

C. Dobson, L. Itzhaki, T. Knowles, 2022, Molecules.

A nanobody binding to non-amyloidogenic regions of the protein human lysozyme enhances partial unfolding but inhibits amyloid fibril formation.

C. Dobson, L. Wyns, S. Muyldermans, 2013, The journal of physical chemistry. B.

Analysis of the Native Structure, Stability and Aggregation of Biotinylated Human Lysozyme

C. Dobson, C. Kaminski, M. Erdélyi, 2012, PloS one.

Local Cooperativity in an Amyloidogenic State of Human Lysozyme Observed at Atomic Resolution

Christopher M. Dobson, Mireille Dumoulin, Xavier Salvatella, 2010, Journal of the American Chemical Society.

Protein Chemistry of Amyloid Fibrils and Chaperones: Implications for Amyloid Formation and Disease

J. Kumita, J. Yerbury, 2010 .

Structure and Dynamics of the Integrin LFA-1 I-Domain in the Inactive State Underlie its Inside-Out/Outside-In Signaling and Allosteric Mechanisms

Carlo Camilloni, Michele Vendruscolo, Predrag Kukic, 2015, Structure.

Inhibition of α-Synuclein Fibril Elongation by Hsp70 Is Governed by a Kinetic Binding Competition between α-Synuclein Species.

C. Dobson, M. Vendruscolo, Anne Dhulesia, 2017, Biochemistry.

Reversible photocontrol of DNA binding by a designed GCN4-bZIP protein.

M. Berezovski, O. Smart, J. P. Calarco, 2006, Biochemistry.

A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers

C. Dobson, M. Vendruscolo, S. Linse, 2021, Communications biology.

α-Synuclein Oligomers Displace Monomeric α-Synuclein from Lipid Membranes

William E. Arter, S. Devenish, A. Levin, 2024, bioRxiv.

Squalamine and Its Derivatives Modulate the Aggregation of Amyloid-β and α-Synuclein and Suppress the Toxicity of Their Oligomers

C. Dobson, M. Vendruscolo, F. Chiti, 2021, Frontiers in Neuroscience.

Trodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism

C. Dobson, M. Vendruscolo, F. Chiti, 2020, Communications Biology.

Trodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism

C. Dobson, M. Vendruscolo, F. Chiti, 2020, Communications Biology.

Structural Characterization of Covalently Stabilized Human Cystatin C Oligomers

Adam K. Sieradzan, C. Dobson, M. Chrabąszczewska, 2019, bioRxiv.

Rationally Designed Antibodies as Research Tools to Study the Structure–Toxicity Relationship of Amyloid-β Oligomers

C. Dobson, M. Vendruscolo, F. Chiti, 2020, International journal of molecular sciences.

Trodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes

C. Dobson, M. Vendruscolo, F. Chiti, 2019, Nature Communications.

Achieving photo-control of protein conformation and activity: producing a photo-controlled leucine zipper.

G Andrew Woolley, O. Smart, Daniel G Flint, 2003, Faraday discussions.

Origins of helix-coil switching in a light-sensitive peptide.

Darcy C Burns, Luis Serrano, G Andrew Woolley, 2004, Biochemistry.

Impact of the native‐state stability of human lysozyme variants on protein secretion by Pichia pastoris

C. Dobson, C. Robinson, M. Alcocer, 2006, The FEBS journal.

Application of Lysine-specific Labeling to Detect Transient Interactions Present During Human Lysozyme Amyloid Fibril Formation

C. Dobson, X. Salvatella, J. Christodoulou, 2017, Scientific Reports.

Hypochlorite-induced oxidation promotes aggregation and reduces toxicity of amyloid beta 1-42

J. Kumita, N. Mañucat-Tan, A. Wyatt, 2023, Redox biology.

Lipid membranes from naked mole-rat brain lipids are cholesterol-rich, highly phase-separated, and sensitive to amyloid-induced damage

Melissa R. Pergande, B. Bhushan, M. Vendruscolo, 2020, bioRxiv.

Cholesterol rich, highly phase separated, naked mole-rat brain lipids are exquisitely sensitive to amyloid induced membrane damage

B. Bhushan, M. Vendruscolo, E. Smith, 2020 .

Cholesterol-rich naked mole-rat brain lipid membranes are susceptible to amyloid beta-induced damage in vitro

Melissa R. Pergande, B. Bhushan, M. Vendruscolo, 2020, Aging.

Solvent exposure of Tyr10 as a probe of structural differences between monomeric and aggregated forms of the amyloid-β peptide

C. Dobson, J. Kumita, E. K. Esbjörner, 2015, Biochemical and biophysical research communications.

Using Tetracysteine-Tagged TDP-43 with a Biarsenical Dye To Monitor Real-Time Trafficking in a Cell Model of Amyotrophic Lateral Sclerosis

C. Dobson, Mark R. Wilson, J. Kumita, 2019, Biochemistry.

A FRET sensor for non-invasive imaging of amyloid formation in vivo.

Clemens F Kaminski, Christopher M Dobson, Alessandro Esposito, 2011, Chemphyschem : a European journal of chemical physics and physical chemistry.

Chemical and mechanistic analysis of photodynamic inhibition of Alzheimer's β-amyloid aggregation.

C. Dobson, M. Vendruscolo, J. Habchi, 2019, Chemical communications.

Population of nonnative states of lysozyme variants drives amyloid fibril formation.

Alexander K. Buell, C. Dobson, X. Salvatella, 2011, Journal of the American Chemical Society.

Phase separation and molecular ordering of the prion-like domain of the thermosensory protein EARLY FLOWERING 3

M. Blackledge, C. Zubieta, M. Nanao, 2023, bioRxiv.

Different Folding States from the Same Protein Sequence Determine Reversible vs Irreversible Amyloid Fate.

R. Mezzenga, Yiping Cao, M. Diener, 2021, Journal of the American Chemical Society.

Characterisation of the structural, dynamic and aggregation properties of the W64R amyloidogenic variant of human lysozyme.

C. Dobson, P. Charlier, A. Brans, 2021, Biophysical chemistry.

The extracellular chaperone clusterin potently inhibits human lysozyme amyloid formation by interacting with prefibrillar species.

Mireille Dumoulin, Christopher M Dobson, Elise M. Stewart, 2007, Journal of molecular biology.

Serum amyloid P component promotes formation of distinct aggregated lysozyme morphologies and reduces toxicity in Drosophila flies expressing F57I lysozyme

Daniel R. Richards, D. Richards, J. Kumita, 2020, PloS one.

A non-natural variant of human lysozyme (I59T) mimics the in vitro behaviour of the I56T variant that is responsible for a form of familial amyloidosis.

C. Dobson, C. Robinson, J. Christodoulou, 2010, Protein engineering, design & selection : PEDS.

Engineering a camelid antibody fragment that binds to the active site of human lysozyme and inhibits its conversion into amyloid fibrils.

C. Dobson, L. Wyns, S. Muyldermans, 2008, Biochemistry.

Explorer Single-Molecule Characterization of the Interactions between Extracellular Chaperones and Toxic -Synuclein Oligomers

D. Klenerman, M. Horrocks, H. Ecroyd, 2018 .

Explorer Single-Molecule Characterization of the Interactions between Extracellular Chaperones and Toxic -Synuclein Oligomers

D. Klenerman, M. Horrocks, H. Ecroyd, 2018 .

Systematic development of small molecules to inhibit specific microscopic steps of Aβ42 aggregation in Alzheimer’s disease

C. Dobson, M. Vendruscolo, O. Hansson, 2016, Proceedings of the National Academy of Sciences.

Cholesterol catalyses Aβ42 aggregation through a heterogeneous nucleation pathway in the presence of lipid membranes

C. Dobson, M. Vendruscolo, S. Linse, 2018, Nature Chemistry.

α2-Macroglobulin and Haptoglobin Suppress Amyloid Formation by Interacting with Prefibrillar Protein Species*

C. Dobson, Mark R. Wilson, Sarah Meehan, 2009, Journal of Biological Chemistry.

Inhibition of α-Synuclein Fibril Elongation by Hsp70 Is Governed by a Kinetic Binding Competition between α-Synuclein Species.

C. Dobson, M. Vendruscolo, Anne Dhulesia, 2017, Biochemistry.

Source Data: A prion-like domain in ELF3 functions as a thermosensor in Arabidopsis

X. Lai, Jae-Hoon Jung, Catarina S. Silva, 2020 .

Prevention of peptide fibril formation in an aqueous environment by mutation of a single residue to Aib.

C. Weston, L. Choo-Smith, O. Smart, 2003, Biochemistry.

The influence of novel gemini surfactants containing cycloalkyl side-chains on the structural phases of DNA in solution.

C. Dobson, M. Kozak, J. Kumita, 2015, Colloids and surfaces. B, Biointerfaces.

A cysteine-free firefly luciferase retains luminescence activity.

J. Kumita, E. Safroneeva, G. Woolley, 2000, Biochemical and biophysical research communications.

Phase separation and molecular ordering of the prion-like domain of the Arabidopsis thermosensory protein EARLY FLOWERING 3

M. Blackledge, C. Zubieta, M. Nanao, 2023, Proceedings of the National Academy of Sciences of the United States of America.

Tandem-repeat proteins introduce tuneable properties to engineered biomolecular condensates

Jerelle A. Joseph, L. Itzhaki, R. Collepardo-Guevara, 2024, bioRxiv.

Publisher Correction: A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers

C. Dobson, M. Vendruscolo, S. Linse, 2021, Communications biology.