(Q57665571)

5

0 references

Alexandre Quintas

object named as

Alexandre Quintas

1

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Isabel Cardoso

object named as

Isabel Cardoso

3

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author name string

Maria João M. Saraiva

Journal of Biological Chemistry

4

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language of work or name

English

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publication date

16 April 2001

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published in

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volume

276

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issue

29

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page(s)

27207-27213

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cites work

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Protein misfolding, evolution and disease

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Alternative conformations of amyloidogenic proteins govern their behavior

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The amyloidogenic potential of transthyretin variants correlates with their tendency to aggregate in solution

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The Tetrameric Protein Transthyretin Dissociates to a Non-native Monomer in Solution

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

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Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1.

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Determination and analysis of urea and guanidine hydrochloride denaturation curves

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Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants

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Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding

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Amyloid beta-protein fibrillogenesis. Detection of a protofibrillar intermediate.

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Assembly of A beta amyloid protofibrils: an in vitro model for a possible early event in Alzheimer's disease

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Physicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains

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A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro

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Sequence Communication: Tabulation of transthyretin (TTR) variants as of 1/1/2000

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Analysis of x-ray diffraction patterns from amyloid of biopsied vitreous humor and kidney of transthyretin (TTR) Met30 familial amyloidotic polyneuropathy (FAP) patients: axially arrayed TTR monomers constitute the protofilament

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The crystal structure of amyloidogenic Leu55 --> Pro transthyretin variant reveals a possible pathway for transthyretin polymerization into amyloid fibrils

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Search for intermediate structures in transthyretin fibrillogenesis: soluble tetrameric Tyr78Phe TTR expresses a specific epitope present only in amyloid fibrils

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