The V30M Amyloidogenic Mutation Decreases the Rate of Refolding Kinetics of the Tetrameric Protein Transthyretin

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Thermodynamic study of transthyretin association (wild-type and senile forms) with heparan sulfate proteoglycan: pH effect and implication of the reactive histidine residue.A New Folding Kinetic Mechanism for Human Transthyretin and the Influence of the Amyloidogenic V30M Mutation.

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The V30M Amyloidogenic Mutation Decreases the Rate of Refolding Kinetics of the Tetrameric Protein Transthyretin

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wetenschappelijk artikel

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наукова стаття, опублікована у 2012

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The V30M Amyloidogenic Mutatio ...... trameric Protein Transthyretin

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The V30M Amyloidogenic Mutatio ...... trameric Protein Transthyretin

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The V30M Amyloidogenic Mutatio ...... trameric Protein Transthyretin

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The V30M Amyloidogenic Mutatio ...... trameric Protein Transthyretin

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The V30M Amyloidogenic Mutatio ...... trameric Protein Transthyretin

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The V30M Amyloidogenic Mutatio ...... trameric Protein Transthyretin

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The V30M Amyloidogenic Mutatio ...... trameric Protein Transthyretin

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Maria J. M. Saraiva

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Amyloid fibrils from the viewpoint of protein folding

Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity.

Quantification of the thermodynamically linked quaternary and tertiary structural stabilities of transthyretin and its disease-associated variants: the relationship between stability and amyloidosis.

Production of recombinant human transthyretin with biological activities toward the understanding of the molecular basis of familial amyloidotic polyneuropathy (FAP).

A perspective on mechanisms of protein tetramer formation.

Partitioning conformational intermediates between competing refolding and aggregation pathways: insights into transthyretin amyloid disease.

Anion shielding of electrostatic repulsions in transthyretin modulates stability and amyloidosis: insight into the chaotrope unfolding dichotomy.

A sensitive assay of transthyretin (prealbumin) in human cerebrospinal fluid in nanogram amounts by ELISA.

Tetramer Dissociation and Monomer Partial Unfolding Precedes Protofibril Formation in Amyloidogenic Transthyretin Variants

Comparative calorimetric study of non-amyloidogenic and amyloidogenic variants of the homotetrameric protein transthyretin

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343-348

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scholarly article

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10.1155/2012/502497

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Rui M. Brito

Daniela C. Vaz

Catarina S.H. Jesus

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2012-01-01T00:00:00Z

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refolding

The V30M Amyloidogenic Mutation Decreases the Rate of Refolding Kinetics of the Tetrameric Protein Transthyretin

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The V30M Amyloidogenic Mutation Decreases the Rate of Refolding Kinetics of the Tetrameric Protein Transthyretin

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P2860

P304

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P1476

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P478

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