The Tetrameric Protein Transthyretin Dissociates to a Non-native Monomer in Solution (Q57665576)

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1 November 2019

title

The tetrameric protein transthyretin dissociates to a non-native monomer in solution. A novel model for amyloidogenesis (English)

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1 November 2019

1

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1 November 2019

Maria João Saraiva

2

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1 November 2019

Rui M. Brito

3

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1 November 2019

author name string

Alexandre Quintas

1

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Maria João M. Saraiva

2

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Rui M. M. Brito

3

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language of work or name

English

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publication date

1 November 1999

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Journal of Biological Chemistry

1 November 2019

published in

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1 November 2019

volume

274

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issue

46

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page(s)

32943-32949

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Amyloid fibril protein in familial amyloidotic polyneuropathy, Portuguese type. Definition of molecular abnormality in transthyretin (prealbumin).

1 November 2019

cites work

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

21 January 2018

1 reference

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Structure of prealbumin: secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 A

21 January 2018

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Normal transthyretin and synthetic transthyretin fragments form amyloid-like fibrils in vitro

21 January 2018

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Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro

21 January 2018

1 reference

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The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid

21 January 2018

1 reference

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

21 January 2018

1 reference

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Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

21 January 2018

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

21 January 2018

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Comparison of Lethal and Nonlethal Transthyretin Variants and Their Relationship to Amyloid Disease

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.46.32943

Characterization of two highly amyloidogenic mutants of transthyretin

21 January 2018

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Characterization of the transthyretin acid denaturation pathways by analytical ultracentrifugation: implications for wild-type, V30M, and L55P amyloid fibril formation

21 January 2018

1 reference

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Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies

21 January 2018

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Solute quenching of protein fluorescence

21 January 2018

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Collapse and cooperativity in protein folding

21 January 2018

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Analysis of thyroid hormone binding to human serum prealbumin by 8-anilinonaphthalene-1-sulfonate fluorescence

21 January 2018

1 reference

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Transthyretin mutation Leu-55-Pro significantly alters tetramer stability and increases amyloidogenicity

21 January 2018

1 reference

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Comparative stability and clearance of [Met30]transthyretin and [Met119]transthyretin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.46.32943

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

21 January 2018

1 reference

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21 January 2018

Identifiers

DOI

10.1074/JBC.274.46.32943

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10551861%20AND%20SRC:MED&resulttype=core&format=json

1 November 2019

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