D. C. Thorn

发表

Amyloid fibril formation by bovine milk kappa-casein and its inhibition by the molecular chaperones alphaS- and beta-casein.

C. Dobson, C. MacPhee, J. Carver, 2005, Biochemistry.

Amyloid fibril formation by bovine milk alpha s2-casein occurs under physiological conditions yet is prevented by its natural counterpart, alpha s1-casein.

J. Carver, M. Sunde, H. Ecroyd, 2008, Biochemistry.

The two-faced nature of milk casein proteins: amyloid fibril formation and chaperone-like activity

J. Carver, H. Ecroyd, D. C. Thorn, 2009 .

The chaperone action of bovine milk αS1- and αS2-caseins and their associated form αS-casein.

J. Carver, W. Price, T. Treweek, 2011, Archives of biochemistry and biophysics.

The Aggregation of αB-Crystallin under Crowding Conditions Is Prevented by αA-Crystallin: Implications for α-Crystallin Stability and Lens Transparency.

J. Carver, D. C. Thorn, A. Rekas, 2020, Journal of molecular biology.

Cumulative deamidations of the major lens protein γS‐crystallin increase its aggregation during unfolding and oxidation

J. Carver, K. Lampi, T. Wales, 2020, Protein science : a publication of the Protein Society.

Amyloid fibrils from readily available sources: milk casein and lens crystallin proteins.

J. Carver, J. Gerrard, M. Garvey, 2013, Methods in molecular biology.

Monitoring the prevention of amyloid fibril formation by α‐crystallin

R. Cappai, J. Carver, D. C. Thorn, 2007 .

Amyloid fibril formation by αS1- and β-casein implies that fibril formation is a general property of all casein proteins.

J. Carver, M. Sunde, C. Holt, 2022, Biochimica et biophysica acta. Proteins and proteomics.

Proteostasis and the Regulation of Intra- and Extracellular Protein Aggregation by ATP-Independent Molecular Chaperones: Lens α-Crystallins and Milk Caseins.

J. Carver, R. Truscott, C. Holt, 2018, Accounts of chemical research.

Monitoring the prevention of amyloid fibril formation by alpha-crystallin. Temperature dependence and the nature of the aggregating species.

R. Cappai, J. Carver, D. C. Thorn, 2007, The FEBS journal.

Casein structures in the context of unfolded proteins

J. Carver, C. Holt, H. Ecroyd, 2015 .

Invited review: Caseins and the casein micelle: their biological functions, structures, and behavior in foods.

J. Carver, C. Holt, H. Ecroyd, 2013, Journal of dairy science.

The Effect of Milk Constituents and Crowding Agents on Amyloid Fibril Formation by κ-Casein.

J. Carver, Jihua Liu, H. Ecroyd, 2016, Journal of agricultural and food chemistry.

Polymorphism in Casein Protein Aggregation and Amyloid Fibril Formation

J. Carver, H. Ecroyd, D. C. Thorn, 2014 .

Dissociation from the Oligomeric State Is the Rate-limiting Step in Fibril Formation by κ-Casein*

Danielle M. Williams, P. Hoffmann, J. Carver, 2008, Journal of Biological Chemistry.

Native disulphide-linked dimers facilitate amyloid fibril formation by bovine milk αS2-casein.

Glyn L. Devlin, P. Hoffmann, J. Carver, 2020, Biophysical chemistry.

The dissociated form of kappa-casein is the precursor to its amyloid fibril formation.

J. Carver, H. Ecroyd, D. C. Thorn, 2010, The Biochemical journal.

A native chemical chaperone in the human eye lens

E. Shakhnovich, R. Klevit, Sourav Chowdhury, 2020, bioRxiv.

Monitoring Early-Stage Protein Aggregation by an Aggregation-Induced Emission Fluorogen.

Yuning Hong, J. Carver, H. Ecroyd, 2017, Analytical chemistry.

The Amyloid Fibril-Forming β-Sheet Regions of Amyloid β and α-Synuclein Preferentially Interact with the Molecular Chaperone 14-3-3ζ

Danielle M. Williams, C. Dobson, J. Carver, 2021, Molecules.

Role of Oxidative Stress in Ocular Diseases: A Balancing Act

D. C. Thorn, Kin-Sang Cho, Daisy Y. Shu, 2023, Metabolites.

The Structure and Stability of the Disulfide-Linked γS-Crystallin Dimer Provide Insight into Oxidation Products Associated with Lens Cataract Formation.

J. Carver, C. Jackson, D. C. Thorn, 2019, Journal of molecular biology.

Small Heat‐shock Proteins and Clusterin: Intra‐ and Extracellular Molecular Chaperones with a Common Mechanism of Action and Function?

J. Carver, Mark R. Wilson, D. C. Thorn, 2003, IUBMB life.

Accumulative deamidation of human lens protein γS-crystallin leads to partially unfolded intermediates with enhanced aggregation propensity

J. Carver, K. Lampi, L. David, 2020, bioRxiv.

Redox chemistry of lens crystallins: A system of cysteines.

D. C. Thorn, L. Quintanar, E. Serebryany, 2021, Experimental Eye Research.