J. Carver

发表

The structure of melittin. A 1H-NMR study in methanol.

I. Campbell, A. Pastore, R. Bazzo, 1988, European journal of biochemistry.

Protein nanostructures in food – Should we be worried?

J. Carver, J. Gerrard, S. Gras, 2014 .

Artificial Nanostructures in Food

J. Carver, J. Gerrard, S. Gras, 2017 .

Casein proteins as molecular chaperones.

J. Carver, W. Price, P. E. Morgan, 2005, Journal of agricultural and food chemistry.

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 antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2.

J. Carver, J. Wallace, T. Rozek, 2000, European journal of biochemistry.

Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance

L. Llewellyn, G. Booker, J. Carver, 2004, Peptides.

Investigating the importance of the flexible hinge in caerin 1.1: solution structures and activity of two synthetically modified caerin peptides.

J. Carver, T. Pukala, J. Bowie, 2004, Biochemistry.

Amyloid aggregation and membrane activity of the antimicrobial peptide uperin 3.5

Lisandra L. Martin, Yuning Hong, R. Hoffmann, 2018 .

A novel protein distance matrix based on the minimum arc-length between two amino-acid residues on the surface of a globular protein.

Ryuzo Azuma, Damien Hall, Kazuo Yamashita, 2014, Biophysical chemistry.

Assignments of meso 1H NMR resonances in haem proteins by selective deuteriation

M. Parker, J. Carver, J. Howard Bradbury, 1982 .

The quaternary organization and dynamics of the molecular chaperone HSP26 are thermally regulated.

Florian Stengel, Eman Basha, Elizabeth Vierling, 2010, Chemistry & biology.

The chaperone activity of α‐synuclein: Utilizing deletion mutants to map its interaction with target proteins

J. Carver, A. Rekas, Jongsun Kim, 2012, Proteins.

Measurement of amyloid formation by turbidity assay—seeing through the cloud

J. Carver, F. Arisaka, D. Hall, 2016, Biophysical Reviews.

Small Heat-shock Proteins Prevent α-Synuclein Aggregation via Transient Interactions and Their Efficacy Is Affected by the Rate of Aggregation*

J. Carver, D. Cox, H. Ecroyd, 2016, The Journal of Biological Chemistry.

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.

Metabolic effects of interleukin 3 on 32D cl23 cells analyzed by NMR

I. Campbell, J. Carver, D. Rees, 1987, Journal of cellular physiology.

The multifaceted nature of αB-crystallin

J. Carver, Junna Hayashi, 2020, Cell Stress and Chaperones.

The Molecular Chaperone, α-Crystallin, Inhibits Amyloid Formation by Apolipoprotein C-II*

J. Carver, G. Howlett, D. Hatters, 2001, The Journal of Biological Chemistry.

Mimicking phosphorylation of alphaB-crystallin affects its chaperone activity.

C. Robinson, C. MacPhee, J. Carver, 2007, The Biochemical journal.

α-Crystallin: molecular chaperone and protein surfactant

J. Carver, J. Aquilina, R. Truscott, 1994 .

Amyloid Fibril Formation by Lens Crystallin Proteins and Its Implications for Cataract Formation*

C. Dobson, C. MacPhee, B. Luisi, 2004, Journal of Biological Chemistry.

Decreased heat stability and increased chaperone requirement of modified human betaB1-crystallins.

T. Shearer, J. Carver, K. Lampi, 2002, Molecular vision.

Supramolecular order within the lens: 1H NMR spectroscopic evidence for specific crystallin-crystallin interactions.

J. Carver, J. Aquilina, R. Truscott, 1994, Experimental eye research.

Functional and dysfunctional folding, association and aggregation of caseins.

J. Carver, C. Holt, 2019, Advances in protein chemistry and structural biology.

Identification of Glutathionyl-3-hydroxykynurenine Glucoside as a Novel Fluorophore Associated with Aging of the Human Lens*

J. Carver, R. Truscott, R. Lindner, 1999, The Journal of Biological Chemistry.

A quantitative NMR spectroscopic examination of the flexibility of the C-terminal extensions of the molecular chaperones, αA- and αB-crystallin.

J. Carver, T. Treweek, A. Rekas, 2010, Experimental eye research.

J. Carver, R. Truscott, A. Aquilina, 1996 .

The Interaction of the Molecular Chaperone, α-Crystallin, with Molten Globule States of Bovine α-Lactalbumin*

J. Carver, A. Kapur, R. Lindner, 1997, The Journal of Biological Chemistry.

On the interaction of α-crystallin with unfolded proteins

J. Carver, R. Truscott, N. Guerreiro, 1995 .

The molecular chaperone β-casein prevents amorphous and fibrillar aggregation of α-lactalbumin by stabilisation of dynamic disorder

J. Carver, Blagojce Jovcevski, T. Pukala, 2020, The Biochemical journal.

Clusterin is an ATP-independent chaperone with very broad substrate specificity that stabilizes stressed proteins in a folding-competent state.

J. Carver, M. Rybchyn, M. Wilson, 2000, Biochemistry.

Clusterin Has Chaperone-like Activity Similar to That of Small Heat Shock Proteins*

J. Carver, Mark R. Wilson, S. Easterbrook-Smith, 1999, The Journal of Biological Chemistry.

Loss of the C-terminal serine residue from bovine βB2-crystallin

J. Carver, R. Truscott, M. Sheil, 1995 .

FACILE DETECTION OF ORGANOMETALLIC DERIVATIVES OF PEPTIDES USING ELECTROSPRAY MASS SPECTROMETRY

K. Bennett, L. Kane-Maguire, J. Carver, 1995 .

Ion Mobility Mass Spectrometry Studies of the Inhibition of Alpha Synuclein Amyloid Fibril Formation by (–)-Epigallocatechin-3-Gallate

J. Carver, T. Pukala, Yanqin Liu, 2011 .

Sequence characteristics responsible for protein-protein interactions in the intrinsically disordered regions of caseins, amelogenins, and small heat-shock proteins.

J. Carver, C. Holt, J. Raynes, 2019, Biopolymers.

The Effect of Oxidized Dopamine on the Structure and Molecular Chaperone Function of the Small Heat-Shock Proteins, αB-Crystallin and Hsp27

T. Preiss, J. Carver, D. Pountney, 2021, International journal of molecular sciences.

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

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

R120G αB‐crystallin promotes the unfolding of reduced α‐lactalbumin and is inherently unstable

C. Robinson, J. Carver, J. Aquilina, 2005 .

On the interaction of alpha-crystallin with unfolded proteins.

J. Carver, R. Truscott, N. Guerreiro, 1995, Biochimica et biophysica acta.

Monitoring the prevention of amyloid fibril formation by α‐crystallin

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

Interaction of the molecular chaperone alphaB-crystallin with alpha-synuclein: effects on amyloid fibril formation and chaperone activity.

Christopher G. Adda, C. Masters, C. Robinson, 2004, Journal of molecular biology.

Monitoring the Interaction between beta(2)-Microglobulin and the Molecular Chaperone alpha B-crystallin by NMR and Mass Spectrometry alpha B-CRYSTALLIN DISSOCIATES beta(2)-MICROGLOBULIN OLIGOMERS

Bellotti, J. Carver, F. Fogolari, 2013 .

The interaction of unfolding α-lactalbumin and malate dehydrogenase with the molecular chaperone αB-crystallin: a light and X-ray scattering investigation

J. Carver, K. Bremmell, J. Regini, 2010, Molecular vision.

Are casein micelles extracellular condensates formed by liquid‐liquid phase separation?

M. Vendruscolo, J. Carver, M. Fuxreiter, 2022, FEBS letters.

The Extracellular Molecular Chaperone Clusterin Inhibits Amyloid Fibril Formation and Suppresses Cytotoxicity Associated with Semen-Derived Enhancer of Virus Infection (SEVI)

J. Carver, Mark R. Wilson, I. Musgrave, 2022, Cells.

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.

Structural alterations of alpha-crystallin during its chaperone action.

J. Carver, M. Mariani, A. Kapur, 1998, European journal of biochemistry.

Primary structure of trypsin inhibitors from Sicyos australis.

J. Carver, D. Shaw, M. Sheil, 1996, Phytochemistry.

Carboxymethylated-kappa-casein: a convenient tool for the identification of polyphenolic inhibitors of amyloid fibril formation.

J. Carver, H. Ecroyd, Yanqin Liu, 2010, Bioorganic & medicinal chemistry.

NMR studies of the Na+, Mg2+ and Ca2+ complexes of cyclosporin A

J. Carver, B. Chowdhry, N. Rees, 1992 .

A structural and functional study of Gln147 deamidation in &agr;A‐crystallin, a site of modification in human cataract

J. Carver, D. Hall, Nicholas J. Ray, 2017, Experimental eye research.

Real-time monitoring of amyloid growth in a rigid gel matrix.

J. Carver, D. Hall, Hendrik Maat, 2016, Analytical biochemistry.

Characterisation of amyloid fibril formation by small heat-shock chaperone proteins human alphaA-, alphaB- and R120G alphaB-crystallins.

C. Dobson, M. Vendruscolo, C. MacPhee, 2007, Journal of molecular biology.

Polypeptide modification and cross-linking by oxidized 3-hydroxykynurenine.

J. Carver, J. Aquilina, R. Truscott, 2000, Biochemistry.

Host defence antibacterial peptides from skin secretions of Australian amphibians. The relationship between structure and activity

J. Carver, J. Wallace, K. Wegener, 1999 .

Investigation of gammaE-crystallin target protein binding to bovine lens alpha-crystallin by small-angle neutron scattering.

J. Carver, P. Griffiths, P. Callow, 2010, Biochimica et biophysica acta.

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.

The molecular chaperone alpha-crystallin is in kinetic competition with aggregation to stabilize a monomeric molten-globule form of alpha-lactalbumin.

J. Carver, T. Treweek, R. Lindner, 2001, The Biochemical journal.

The mammalian small heat-shock protein Hsp20 forms dimers and is a poor chaperone.

W. D. de Jong, R. Jaenicke, J. Carver, 1998, European journal of biochemistry.

RNA-LIM: a novel procedure for analyzing protein/single-stranded RNA propensity data with concomitant estimation of interface structure.

D. Standley, R. Azuma, J. Carver, 2015, Analytical biochemistry.

A spectroscopic study of glycated bovine alpha-crystallin: investigation of flexibility of the C-terminal extension, chaperone activity and evidence for diglycation.

J. Carver, M. Sheil, R. Blakytny, 1997, Biochimica et biophysica acta.

Casein structures in the context of unfolded proteins

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

A high resolution 1H NMR study of the solution structure of human epidermal growth factor

I. Campbell, R. Cooke, J. Carver, 1986, FEBS letters.

Structural characterization of piperidine alkaloids from Pandanus amaryllifolius by inverse-detected 2D NMR techniques

M. Garson, J. Carver, R. Truscott, 1993 .

Inactivation of chicken liver pyruvate carboxylase by 1,10-phenanthroline.

J. Carver, G. Baldwin, J. Wallace, 1988, The Biochemical journal.

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 .

AlphaB-crystallin inhibits the cell toxicity associated with amyloid fibril formation by kappa-casein and the amyloid-beta peptide

J. Carver, I. Musgrave, H. Ecroyd, 2014 .

Methionine oxidation enhances κ-casein amyloid fibril formation.

Peter Hoffmann, P. Hoffmann, J. Carver, 2012, Journal of agricultural and food chemistry.

αB-Crystallin inhibits the cell toxicity associated with amyloid fibril formation by κ-casein and the amyloid-β peptide

J. Carver, I. Musgrave, H. Ecroyd, 2010, Cell Stress and Chaperones.

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.

Darwinian transformation of a ‘scarcely nutritious fluid’ into milk

J. Carver, C. Holt, Carl Holt, 2012, Journal of evolutionary biology.

Oxidation products of 3-hydroxykynurenine bind to lens proteins: relevance for nuclear cataract.

J. Carver, J. Aquilina, R. Truscott, 1997, Experimental eye research.

Non-oxidative modification of lens crystallins by kynurenine: a novel post-translational protein modification with possible relevance to ageing and cataract.

J. Carver, R. Truscott, R. Lindner, 2000, Biochimica et biophysica acta.

A new UV‐filter compound in human lenses

J. Carver, M. Sheil, G. Kilby, 1994, FEBS letters.

Identification of 3-hydroxykynurenine as the lens pigment in the gourami Trichogaster trichopterus.

R. Douglas, J. Carver, R. Truscott, 1992, Experimental eye research.

Elucidation of a novel polypeptide cross-link involving 3-hydroxykynurenine.

J. Carver, J. Aquilina, R. Truscott, 1999, Biochemistry.

Alpha-crystallin: molecular chaperone and protein surfactant.

J. Carver, J. Aquilina, R. Truscott, 1994, Biochimica et Biophysica Acta.

Preparation, processing and applications of protein nanofibers

J. Carver, J. Gerrard, M. Garvey, 2013 .

Immobilization of the C-terminal Extension of Bovine αA-Crystallin Reduces Chaperone-like Activity*

W. D. de Jong, J. Carver, M. V. van Boekel, 1996, The Journal of Biological Chemistry.

Monitoring the Interaction between β2-Microglobulin and the Molecular Chaperone αB-crystallin by NMR and Mass Spectrometry

A. Heck, V. Alverdi, J. Carver, 2013, The Journal of Biological Chemistry.

Coaggregation of κ-Casein and β-Lactoglobulin Produces Morphologically Distinct Amyloid Fibrils.

M. Horrocks, J. Carver, L. Day, 2017, Small.

Solution conformation of bovine lens α‐and βB2‐crystallin terminal extensions

J. Carver, E. L. Breton, 2009 .

Probing the structure and interactions of crystallin proteins by NMR spectroscopy

J. Carver, 1999, Progress in Retinal and Eye Research.

NMR spectroscopy of α-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins

J. Carver, R. Lindner, 1998 .

1H NMR spectroscopy reveals that mouse Hsp25 has a flexible C‐terminal extension of 18 amino acids

M. Gaestel, J. Carver, G. Esposito, 1995, FEBS letters.

A possible chaperone-like quaternary structure for alpha-crystallin.

J. Carver, J. Aquilina, R. Truscott, 1994, Experimental eye research.

Functional Amyloid Protection in the Eye Lens: Retention of α-Crystallin Molecular Chaperone Activity after Modification into Amyloid Fibrils

J. Carver, J. Gerrard, M. Garvey, 2017, Biomolecules.

Site-Directed Mutations in the C-Terminal Extension of Human αB-Crystallin Affect Chaperone Function and Block Amyloid Fibril Formation

Danielle M. Williams, J. Carver, H. Ecroyd, 2007, PloS one.

An investigation into the stability of alpha-crystallin by NMR spectroscopy; evidence for a two-domain structure.

J. Carver, J. Aquilina, R. Truscott, 1993, Biochimica et biophysica acta.

NMR spectroscopy of large proteins

J. Carver, M. Keniry, 2002 .

Small heat-shock proteins: important players in regulating cellular proteostasis

J. Carver, H. Ecroyd, T. Treweek, 2015, Cellular and Molecular Life Sciences.

The growing world of small heat shock proteins: from structure to functions

B. Brundel, H. Kampinga, C. Emanuelsson, 2017, Cell Stress and Chaperones.

Mouse Hsp25, a small heat shock protein

M. Gaestel, J. Carver, J. Buchner, 2000 .

Mouse Hsp25, a small shock protein. The role of its C-terminal extension in oligomerization and chaperone action.

M. Gaestel, J. Carver, J. Buchner, 2000, European journal of biochemistry.

NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins.

J. Carver, R. Lindner, 1998, International journal of biological macromolecules.

Structural investigation of the hedamycin:d(ACCGGT)2 complex by NMR and restrained molecular dynamics.

J. Carver, G. Burley, E. A. Owen, 2002, Biochemical and biophysical research communications.

Preliminary communication: The use of [(C6H7)Fe(CO)3]+ as a recoverable protecting group in peptide synthesis

L. Kane-Maguire, J. Carver, Shanlin Fu, 1993 .

Selective labelling of peptides using (dienyl) iron tricarbonyl cations

L. Kane-Maguire, J. Carver, Betty Fates, 1993 .

Research The effect of dextran on subunit exchange of α A-crystallin The effect of dextran on subunit exchange of A-crystallin

J. Carver, W. Price, A. Rekas, 2017 .

The effect of dextran on subunit exchange of αAcrystallin

J. Carver, A. Rekas, W. E. Price, 2014 .

The effect of dextran on subunit exchange of the molecular chaperone alphaA-crystallin.

J. Carver, W. Price, A. Rekas, 2007, Biochimica et biophysica acta.

Identification by 1H NMR spectroscopy of flexible C‐terminal extensions in bovine lens α‐crystallin

J. Carver, J. Aquilina, R. Truscott, 1992, FEBS letters.

Structural differences between bovine A(1) and A(2) β-casein alter micelle self-assembly and influence molecular chaperone activity.

J. Carver, L. Day, M. Augustin, 2015, Journal of dairy science.

Clusterin is an extracellular chaperone that specifically interacts with slowly aggregating proteins on their off‐folding pathway

J. Carver, Mark R. Wilson, T. Treweek, 2002, FEBS letters.

Probing the disulfide folding pathway of insulin-like growth factor-I.

J. Carver, F. Ballard, G. Francis, 1999, Biotechnology and bioengineering.

Glucoindole alkaloids from Ophiorrhiza acuminata.

M. Hemling, J. Carver, R. Truscott, 1995, Planta medica.

The thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compounds

Tak W. Kee, J. Carver, S. Hudson, 2009, The FEBS journal.

Evidence that clusterin has discrete chaperone and ligand binding sites.

J. Lakins, J. Carver, Mark R. Wilson, 2002, Biochemistry.

Eye Lens Crystallins: Remarkable Long‐Lived Proteins

J. Carver, Aidan B. Grosas, 2021 .

Hemin as a generic and potent protein misfolding inhibitor.

J. Carver, T. Pukala, I. Musgrave, 2014, Biochemical and biophysical research communications.

Preventing α-synuclein aggregation: the role of the small heat-shock molecular chaperone proteins.

J. Carver, D. Cox, H. Ecroyd, 2014, Biochimica et biophysica acta.

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.

Binding of the molecular chaperone alphaB-crystallin to Abeta amyloid fibrils inhibits fibril elongation

Alexander K. Buell, C. Dobson, M. Welland, 2020 .

Binding of the molecular chaperone αB-crystallin to Aβ amyloid fibrils inhibits fibril elongation.

Alexander K. Buell, C. Dobson, M. Welland, 2011, Biophysical journal.

Recognizing and analyzing variability in amyloid formation kinetics: Simulation and statistical methods.

G. Rivas, J. Carver, D. Hall, 2016, Analytical biochemistry.

A multi‐pathway perspective on protein aggregation: Implications for control of the rate and extent of amyloid formation

J. Carver, J. Kardos, D. Hall, 2015, FEBS letters.

Structure/function studies of dogfish α-crystallin, comparison with bovine α-crystallin

J. Carver, A. Rekas, R. Augusteyn, 2009, Molecular vision.

Deamidation of N76 in human γS-crystallin promotes dimer formation.

J. Carver, D. Hall, Nicholas J. Ray, 2016, Biochimica et biophysica acta.

The Interaction of the Molecular Chaperone α-Crystallin with Unfolding α-Lactalbumin: A Structural and Kinetic Spectroscopic Study

C. Dobson, J. Carver, D. Canet, 2002 .

Assignment of 1H NMR resonances of histidine and other aromatic residues in met-, cyano-, oxy-, and (carbon monoxy)myoglobins.

J. Carver, J. Bradbury, 1984, Biochemistry.

Dephosphorylation of alpha(s)- and beta-caseins and its effect on chaperone activity: a structural and functional investigation.

P. Hoffmann, J. Carver, T. Koudelka, 2009, Journal of agricultural and food chemistry.

Gallic acid is the major component of grape seed extract that inhibits amyloid fibril formation.

Danielle M. Williams, J. Carver, T. Pukala, 2013, Bioorganic & medicinal chemistry letters.

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.

The functional roles of the unstructured N- and C-terminal regions in αB-crystallin and other mammalian small heat-shock proteins

J. Carver, H. Ecroyd, R. Quinlan, 2017, Cell Stress and Chaperones.

The multifaceted nature of αB-crystallin

J. Carver, Junna Hayashi, 2020, Cell Stress and Chaperones.

Characterisation of Amyloid Fibril Formation by Small Heat-shock Chaperone Proteins Human αA-, αB- and R120G αB-Crystallins

C. Dobson, M. Vendruscolo, C. MacPhee, 2007 .

R120G alphaB-crystallin promotes the unfolding of reduced alpha-lactalbumin and is inherently unstable.

C. Robinson, J. Carver, J. Aquilina, 2005, The FEBS journal.

Host defence peptides from the skin glands of the Australian blue mountains tree-frog Litoria citropa. Solution structure of the antibacterial peptide citropin 1.1.

J. Carver, J. Wallace, K. Wegener, 1999, European journal of biochemistry.

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.

Small heat-shock proteins interact with a flanking domain to suppress polyglutamine aggregation

Martin J. Scanlon, Amy L. Robertson, Stephen P. Bottomley, 2010, Proceedings of the National Academy of Sciences.

Solution Structure and Backbone Dynamics of Long-[Arg3]insulin-like Growth Factor-I*

J. Carver, J. Wallace, G. Francis, 2000, The Journal of Biological Chemistry.

Small heat shock proteins: multifaceted proteins with important implications for life

Tangchun Wu, R. Klevit, J. Carver, 2019, Cell Stress and Chaperones.

(-)-epigallocatechin-3-gallate (EGCG) maintains kappa-casein in its pre-fibrillar state without redirecting its aggregation pathway.

J. Carver, S. Hudson, I. Musgrave, 2009, Journal of molecular biology.

The eye lens protein alphaA-crystallin of the blind mole rat Spalax ehrenbergi: effects of altered functional constraints.

W. D. de Jong, J. Carver, R. Lindner, 2002, Experimental eye research.

The molecular basis of kirromycin (mocimycin) action; a 1H NMR study using deuterated elongation factor Tu.

J. Barber, J. Carver, R. Leberman, 1988, The Journal of antibiotics.

Amyloid-β oligomers are sequestered by both intracellular and extracellular chaperones.

C. Dobson, D. Klenerman, J. Carver, 2012, Biochemistry.

Analysis of Glaucoma-related Mortality in the United States Using Death Certificate Data

J. Carver, M. Wise, F. Sorvillo, 2008, Journal of glaucoma.

Mildly Acidic pH Activates the Extracellular Molecular Chaperone Clusterin*

J. Carver, M. Rybchyn, Mark R. Wilson, 2002, The Journal of Biological Chemistry.

Hardware Validation of the Advanced Plant Habitat on ISS: Canopy Photosynthesis in Reduced Gravity

Nicole F. Dufour, J. Carver, O. Monje, 2020, Frontiers in Plant Science.

The two-faced nature of small heat shock proteins: amyloid assembly and the inhibition of fibril formation. Relevance to disease states

J. Carver, H. Ecroyd, Sarah Meehan, 2010 .

Mimicking phosphorylation of αB-crystallin affects its chaperone activity

Cait E. MacPhee, Carol V. Robinson, Justin L. P. Benesch, 2007 .

Enhanced molecular chaperone activity of the small heat-shock protein alphaB-cystallin following covalent immobilization onto a solid-phase support.

H. Griesser, J. Shapter, J. Carver, 2011, Biopolymers.

Terminal Regions Confer Plasticity to the Tetrameric Assembly of Human HspB2 and HspB3

Alice R. Clark, A. R. Clark, J. Carver, 2018, Journal of molecular biology.

A radish seed antifungal peptide with a high amyloid fibril-forming propensity.

D. Craik, H. Schirra, J. Carver, 2013, Biochimica et biophysica acta.

Unraveling the mysteries of protein folding and misfolding

J. Carver, H. Ecroyd, 2008, IUBMB life.

Crystallin proteins and amyloid fibrils

J. Carver, H. Ecroyd, John A. Carver, 2008, Cellular and Molecular Life Sciences.

The solution structure and activity of caerin 1.1, an antimicrobial peptide from the Australian green tree frog, Litoria splendida.

J. Carver, J. Bowie, H. Wong, 1997, European journal of biochemistry.

β-Synuclein: An Enigmatic Protein with Diverse Functionality

J. Carver, Junna Hayashi, 2022, Biomolecules.

Small heat shock proteins: multifaceted proteins with important implications for life

Tangchun Wu, R. Klevit, J. Carver, 2019, Cell Stress and Chaperones.

Glutamic acid residues in the C‐terminal extension of small heat shock protein 25 are critical for structural and functional integrity

J. Carver, Amie M. Morris, J. Aquilina, 2008, The FEBS journal.

The interaction of the molecular chaperone alpha-crystallin with unfolding alpha-lactalbumin: a structural and kinetic spectroscopic study.

C. Dobson, J. Carver, D. Canet, 2002, Journal of molecular biology.

The structured core domain of αB-crystallin can prevent amyloid fibrillation and associated toxicity

Georg K. A. Hochberg, D. Eisenberg, J. Stroud, 2014, Proceedings of the National Academy of Sciences.

SEVI, the semen enhancer of HIV infection along with fragments from its central region, form amyloid fibrils that are toxic to neuronal cells.

J. Carver, I. Musgrave, D. Scanlon, 2014, Biochimica et biophysica acta.

1H‐NMR spectroscopy of βB2‐crystallin from bovine eye lens

J. Carver, R. Truscott, P. G. Cooper, 1993 .

VEG-01: Veggie Hardware Validation Testing on the International Space Station

Raymond M. Wheeler, Robert Morrow, Mary Hummerick, 2017 .

Glutamic Acid Residues in the C-Terminal Extension of Hsp25 are Critical for Structural and Functional Integrity

J. Carver, Amie M. Morris, J. Aquilina, 2014 .

The molecular chaperone α-crystallin is in kinetic competition with aggregation to stabilize a monomeric molten-globule form of α-lactalbumin

J. Carver, T. Treweek, R. Lindner, 2022 .

1H nuclear magnetic resonance studies of an integral membrane protein: subunit c of the F1F0 ATP synthase.

I. Campbell, J. Carver, J. Boyd, 1987, Journal of molecular biology.

High-resolution 1H NMR study of the solution structure of alamethicin.

I. Campbell, J. Carver, G. Esposito, 1987, Biochemistry.

The Selective Inhibition of Serpin Aggregation by the Molecular Chaperone, α-Crystallin, Indicates a Nucleation-dependent Specificity*

Glyn L. Devlin, S. Bottomley, J. Carver, 2003, Journal of Biological Chemistry.

Model for amorphous aggregation processes.

J. Carver, E. Waters, S. Stranks, 2009, Physical review. E, Statistical, nonlinear, and soft matter physics.

Interaction of the Molecular Chaperone αB-Crystallin with α-Synuclein: Effects on Amyloid Fibril Formation and Chaperone Activity

Christopher G. Adda, C. Masters, C. Robinson, 2004 .

The small heat-shock chaperone protein, alpha-crystallin, does not recognize stable molten globule states of cytosolic proteins.

J. Carver, M. Mariani, T. Treweek, 2000, Biochimica et biophysica acta.

The solution structure of frenatin 3, a neuronal nitric oxide synthase inhibitor from the giant tree frog, Litoria infrafrenata.

L. Llewellyn, J. Carver, K. Wegener, 2003, Biopolymers.

nNOS inhibition, antimicrobial and anticancer activity of the amphibian skin peptide, citropin 1.1 and synthetic modifications. The solution structure of a modified citropin 1.1.

L. Llewellyn, J. Carver, K. Wegener, 2003, European journal of biochemistry.

Maculatin 1.1, an anti-microbial peptide from the Australian tree frog, Litoria genimaculata solution structure and biological activity.

J. Carver, T. Mulhern, J. Bowie, 2000, European journal of biochemistry.

The solution structure of uperin 3.6, an antibiotic peptide from the granular dorsal glands of the Australian toadlet, Uperoleia mjobergii.

J. Carver, T. Mulhern, J. Bowie, 1999, The journal of peptide research : official journal of the American Peptide Society.

The membrane-active amphibian peptide caerin 1.8 inhibits fibril formation of amyloid β1-42

J. Carver, Tianfang Wang, S. Cummins, 2015, Peptides.

Secondary structure determination of 15N‐labelled human Long‐[Arg‐3]‐insulin‐like growth factor 1 by multidimensional NMR spectroscopy

J. Carver, J. Wallace, G. Francis, 1997, FEBS letters.

A two dimensional 1H NMR study of the solution conformation of gastrin releasing peptide.

J. Carver, 1988, Biochemical and biophysical research communications.

The conformation of bombesin in solution as determined by two-dimensional 1H-NMR techniques.

J. Carver, 1987, European journal of biochemistry.

The Interaction of αB-Crystallin with Mature α-Synuclein Amyloid Fibrils Inhibits Their Elongation

C. Dobson, J. Skepper, M. Welland, 2010, Biophysical journal.

Application of the Double-Mutant Cycle Strategy to Protein Aggregation Reveals Transient Interactions in Amyloid-β Oligomers.

Adam J. Carroll, Adam J Carroll, J. Carver, 2021, The journal of physical chemistry. B.

Single Molecule Characterization of the Interactions between Amyloid-β Peptides and the Membranes of Hippocampal Cells

C. Dobson, D. Klenerman, P. S. St George-Hyslop, 2013, Journal of the American Chemical Society.

1H‐NMR spectroscopy of bovine lens β‐crystallin

J. Carver, R. Truscott, P. G. Cooper, 1993 .

1H-NMR spectroscopy of bovine lens beta-crystallin. The role of the beta B2-crystallin C-terminal extension in aggregation.

J. Carver, R. Truscott, P. G. Cooper, 1993, European journal of biochemistry.

Protein aggregate turbidity: Simulation of turbidity profiles for mixed-aggregation reactions.

Nathaniel J. Bloomfield, Steven R. Williams, J. Carver, 2016, Analytical biochemistry.

Gallic acid interacts with α-synuclein to prevent the structural collapse necessary for its aggregation.

J. Carver, T. Pukala, Yanqin Liu, 2014, Biochimica et biophysica acta.

The interaction of the molecular chaperone, alpha-crystallin, with molten globule states of bovine alpha-lactalbumin.

J. Carver, A. Kapur, R. Lindner, 1997, The Journal of biological chemistry.

Avoiding the oligomeric state: αB‐crystallin inhibits fragmentation and induces dissociation of apolipoprotein C‐II amyloid fibrils

J. Carver, H. Ecroyd, M. Griffin, 2013, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

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.

A Spectroscopic Marker for Structural Transitions Associated with Amyloid-β Aggregation.

Yuning Hong, J. Carver, Anirban Das, 2020, Biochemistry.

Formation of βA3/βB2-crystallin mixed complexes: involvement of N- and C-terminal extensions

W. W. Jong, J. Carver, R. Lindner, 1999 .

The elusive role of the N-terminal extension of beta A3- and beta A1-crystallin.

W. D. de Jong, R. Jaenicke, J. Carver, 1996, Protein engineering.

A 1H NMR Spectroscopic Comparison of γs- and γB-crystallins

J. Carver, J. Aquilina, R. Truscott, 1994 .

NMR identification of a partial helical conformation for bombesin in solution.

J. Collins, J. Carver, 1990, European journal of biochemistry.

Host defense peptides from the secretion of the skin glands of frogs: membrane-active peptides from the genera Litoria, Uperoleia and Crinia

Frances Separovic, J. Carver, F. Separovic, 2009 .

Kinetics of Amyloid Fibrillar Aggregation of Uperin 3.5 is Directed by the Peptide's Secondary Structure.

Yuning Hong, J. Carver, T. John, 2019, Biochemistry.

Structural comparison between retro-inverso and parent peptides: molecular basis for the biological activity of a retro-inverso analogue of the immunodominant fragment of VP1 coat protein from foot-and-mouth disease virus.

F. Brown, J. Carver, F. Fogolari, 1997, Biopolymers.

NMR spectroscopy of 14-3-3ζ reveals a flexible C-terminal extension: differentiation of the chaperone and phosphoserine-binding activities of 14-3-3ζ.

Danielle M. Williams, H. Fu, J. Carver, 2011, The Biochemical journal.

The effect of small molecules in modulating the chaperone activity of αB‐crystallin against ordered and disordered protein aggregation

J. Carver, H. Ecroyd, Heath Ecroyd, 2008, The FEBS journal.

The Amyloid Fibril‐Forming Properties of the Amphibian Antimicrobial Peptide Uperin 3.5

Antonio N Calabrese, J. Carver, T. Pukala, 2016, Chembiochem : a European journal of chemical biology.

Intracellular Protein Unfolding and Aggregation: The Role of Small Heat-Shock Chaperone Proteins

J. Carver, Amie M. Morris, T. Treweek, 2003 .

The thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compounds

Tak W. Kee, J. Carver, S. Hudson, 2009, The FEBS journal.

SEVI, the semen enhancer of HIV infection along with fragments from its central region, form amyloid fibrils that are toxic to neuronal cells.

J. Carver, I. Musgrave, D. Scanlon, 2014, Biochimica et biophysica acta.

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

Danielle M. Williams, Glyn L. Devlin, P. Hoffmann, 2008, Journal of Biological Chemistry.

Amyloid fibril formation, structure and domain swapping of acyl‐coenzyme A thioesterase‐7

J. Carver, M. Sunde, J. Forwood, 2023, The FEBS journal.

Crystallin proteins and amyloid fibrils

J. Carver, H. Ecroyd, 2008, Cellular and Molecular Life Sciences.

Mimicking phosphorylation of αB-crystallin affects its chaperone activity

C. Robinson, C. MacPhee, J. Carver, 2007 .

Protein nanofibres of defined morphology prepared from mixtures of crude crystallins

J. Carver, J. Gerrard, S. Gras, 2009 .

The molecular chaperone alpha-crystallin is in kinetic competition with aggregation to stabilize a monomeric molten-globule form of alpha-lactalbumin.

J. Carver, T. Treweek, R. Lindner, 2001, The Biochemical journal.

The interaction of unfolding α-lactalbumin and malate dehydrogenase with the molecular chaperone αB-crystallin: a light and X-ray scattering investigation

J. Carver, K. Bremmell, J. Regini, 2010, Molecular vision.

The Amyloid Fibril‐Forming Properties of the Amphibian Antimicrobial Peptide Uperin 3.5

J. Carver, T. Pukala, Tianfang Wang, 2016, Chembiochem : a European journal of chemical biology.

Role of salt bridges in the dimer interface of 14-3-3ζ in dimer dynamics, N-terminal α-helical order, and molecular chaperone activity

J. Sandow, Angel F. Lopez, J. Carver, 2017, The Journal of Biological Chemistry.

The solution structures and activity of caerin 1.1 and caerin 1.4 in aqueous trifluoroethanol and dodecylphosphocholine micelles

J. Carver, K. Wegener, J. Bowie, 2003, Biopolymers.