X-ray absorption spectroscopy reveals a substantial increase of sulfur oxidation in transthyretin (TTR) upon fibrillization (Q44285399)

1 December 2017

title

X-ray absorption spectroscopy reveals a substantial increase of sulfur oxidation in transthyretin (TTR) upon fibrillization (English)

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Luís Miguel Gales Pereira Pinto

1 December 2017

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series ordinal

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Alexandre Quintanilha

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1 December 2017

Isabel Cardoso

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Barbara Fayard

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1 December 2017

Ana M Damas

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1 December 2017

language of work or name

English

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publication date

21 January 2003

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Journal of Biological Chemistry

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inferred from page(s)

published in

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1 December 2017

volume

278

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1 December 2017

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1 December 2017

page(s)

11654-11660

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Transthyretin mutations in hyperthyroxinemia and amyloid diseases

1 December 2017

cites work

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21 January 2018

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21 January 2018

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Characterization of transthyretin mutants from serum using immunoprecipitation, HPLC/electrospray ionization and matrix-assisted laser desorption/ionization mass spectrometry.

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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Characterization of sulfur in asphaltenes by sulfur K- and L-edge XANES spectroscopy

21 January 2018

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

21 January 2018

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Intermolecular disulfide linkages are not required for transthyretin amyloid fibril formation in vitro

21 January 2018

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Potential treatment of transthyretin-type amyloidoses by sulfite

21 January 2018

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Detection by mass spectrometry of highly increased amount of S-sulfonated transthyretin in serum from a patient with molybdenum cofactor deficiency

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M210798200

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1 December 2017

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