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

Cellular and molecular life sciences : CMLS, 2015-02, Vol.72 (3), p.429-451

2015

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The first steps on the journey towards curriculum reconciliation in science, medicine and health education

Higher education research and development, 2021-01, Vol.40 (1), p.194-206

2021

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The chaperone action of bovine milk α S1- and α S2-caseins and their associated form α S-casein

Archives of biochemistry and biophysics, 2011-06, Vol.510 (1), p.42-52

2011

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

Experimental eye research, 2010-11, Vol.91 (5), p.691-699

2010

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Casein Proteins as Molecular Chaperones

Journal of agricultural and food chemistry, 2005-04, Vol.53 (7), p.2670-2683

2005

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

Australian journal of chemistry, 2003, Vol.56 (5), p.357

2003

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

PloS one, 2007-10, Vol.2 (10), p.e1046

2007

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

The FEBS journal, 2008-12, Vol.275 (23), p.5885-5898

2008

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

FEBS letters, 2002-02, Vol.513 (2-3), p.259-266

2002

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

Journal of molecular biology, 2007-09, Vol.372 (2), p.470-484

2007

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

The FEBS journal, 2005-02, Vol.272 (3), p.711-724

2005

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Site-directed mutations in the C-terminal extension of human alphaB-crystallin affect chaperone function and block amyloid fibril formation

PloS one, 2007-10, Vol.2 (10), p.e1046

2007

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Corrigendum to “The chaperone action of bovine milk α S1- and α S2-caseins and their associated form α S-casein” [Arch. Biochem. Biophys. 510 (2011) 42–52]

Archives of biochemistry and biophysics, 2011-09, Vol.513 (1), p.70-70

2011

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

Biochemical journal, 2001-02, Vol.354 (Pt 1), p.79-87

2001

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The small heat-shock chaperone protein, α-crystallin, does not recognise stable molten globule states of cytosolic proteins

Biochimica et biophysica acta, 2000-08, Vol.1481 (1), p.175-188

2000

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

PloS one, 2007-10, Vol.2 (10), p.e1046

2007

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

Journal of molecular biology, 2007-09, Vol.372 (2), p.470-484

2007

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

The FEBS journal, 2005-02, Vol.272 (3), p.711-724

2005

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R120G [alpha]B-crystallin promotes the unfolding of reduced [alpha]-lactalbumin and is inherently unstable

The FEBS journal, 2005-02, Vol.272 (3), p.711

2005

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

Biochemical journal, 2001-02, Vol.354 (1), p.79-87

2001

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

ChemInform, 2003-08, Vol.34 (32), p.no-no

2003

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

The first steps on the journey towards curriculum reconciliation in science, medicine and health education

The chaperone action of bovine milk α S1- and α S2-caseins and their associated form α S-casein

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

Casein Proteins as Molecular Chaperones

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

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

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

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

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

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

Site-directed mutations in the C-terminal extension of human alphaB-crystallin affect chaperone function and block amyloid fibril formation

Corrigendum to “The chaperone action of bovine milk α S1- and α S2-caseins and their associated form α S-casein” [Arch. Biochem. Biophys. 510 (2011) 42–52]

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

The small heat-shock chaperone protein, α-crystallin, does not recognise stable molten globule states of cytosolic proteins

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

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

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

R120G [alpha]B-crystallin promotes the unfolding of reduced [alpha]-lactalbumin and is inherently unstable

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

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

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