The crystal structure of amyloidogenic Leu55 --> Pro transthyretin variant reveals a possible pathway for transthyretin polymerization into amyloid fibrils (Q27765294)

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The Crystal Structure of Amyloidogenic Leu55→ Pro Transthyretin Variant Reveals a Possible Pathway for Transthyretin Polymerization into Amyloid Fibrils

Language	Label	Description	Also known as
English	The crystal structure of amyloidogenic Leu55 --> Pro transthyretin variant reveals a possible pathway for transthyretin polymerization into amyloid fibrils	scientific article	The Crystal Structure of Amyloidogenic Leu55→ Pro Transthyretin Variant Reveals a Possible Pathway for Transthyretin Polymerization into Amyloid Fibrils

Statements

scholarly article

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

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The Crystal Structure of Amyloidogenic Leu55→ Pro Transthyretin Variant Reveals a Possible Pathway for Transthyretin Polymerization into Amyloid Fibrils (English)

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crystal structure

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author name string

M P Sebastião

1

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M J Saraiva

2

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A M Damas

3

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Maria Paula Sebastião

1

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Maria João Saraiva

2

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Ana Margarida Damas

3

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language of work or name

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publication date

18 September 1998

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Journal of Biological Chemistry

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273

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38

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24715-22

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24715-24722

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Transthyretin Pro55, a variant associated with early-onset, aggressive, diffuse amyloidosis with cardiac and neurologic involvement

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https://api.crossref.org/works/10.1074%2FJBC.273.38.24715

21 January 2018

Structure of a complex of two plasma proteins: transthyretin and retinol-binding protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.38.24715

21 January 2018

Structure-dependent, competitive interaction of hydroxy-polychlorobiphenyls, -dibenzo-p-dioxins and -dibenzofurans with human transthyretin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.38.24715

21 January 2018

Metabolism of the viatmin A transporting protein complex. I. Turnover studies in normal persons and in patients with chronic renal failure

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.38.24715

21 January 2018

Transthyretin mutations in health and disease.

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https://api.crossref.org/works/10.1074%2FJBC.273.38.24715

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A peculiar form of peripheral neuropathy; familiar atypical generalized amyloidosis with special involvement of the peripheral nerves

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.38.24715

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.38.24715

21 January 2018

Structure of the Val122Ile variant transthyretin - a cardiomyopathic mutant

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.38.24715

21 January 2018

Structural changes in transthyretin produced by the Ile 84 Ser mutation which result in decreased affinity for retinol-binding protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.38.24715

21 January 2018

Crystallization and preliminary X-ray diffraction studies of Leu55Pro variant transthyretin

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https://api.crossref.org/works/10.1074%2FJBC.273.38.24715

21 January 2018

AMoRe: an automated package for molecular replacement

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https://api.crossref.org/works/10.1074%2FJBC.273.38.24715

21 January 2018

The CCP4 suite: programs for protein crystallography

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.38.24715

21 January 2018

Improved methods for building protein models in electron density maps and the location of errors in these models

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.38.24715

21 January 2018

Stereochemical quality of protein structure coordinates

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https://api.crossref.org/works/10.1074%2FJBC.273.38.24715

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.38.24715

21 January 2018

A new isoleucine substitution of Val-20 in transthyretin tetramers selectively impairs dimer-dimer contacts and causes systemic amyloidosis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.38.24715

21 January 2018

A chemical approach to elucidate tin mechanism of transthyretin and β-protein amyloid fibril formation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.38.24715

21 January 2018

‘In vitro’ amyloid fibril formation from transthyretin: the influence of ions and the amyloidogenicity of TTR variants

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.38.24715

21 January 2018

Characterization of two highly amyloidogenic mutants of transthyretin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.38.24715

21 January 2018

Examination of the Structure of the Transthyretin Amyloid Fibril by Image Reconstruction from Electron Micrographs

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.38.24715

21 January 2018

Identifiers

10.1074/JBC.273.38.24715

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