(Q54477460)

30 May 2018

title

L55P transthyretin accelerates subunit exchange and leads to rapid formation of hybrid tetramers. (English)

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30 May 2018

6

Carol V Robinson

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30 May 2018

author name string

Catherine A Keetch

1

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30 May 2018

Elizabeth H C Bromley

2

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30 May 2018

Margaret G McCammon

3

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30 May 2018

Nan Wang

4

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30 May 2018

John Christodoulou

5

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30 May 2018

language of work or name

English

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publication date

11 October 2005

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30 May 2018

Journal of Biological Chemistry

published in

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30 May 2018

volume

280

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30 May 2018

page(s)

41667-41674

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issue

50

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30 May 2018

Folding proteins in fatal ways

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

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An engineered transthyretin monomer that is nonamyloidogenic, unless it is partially denatured

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

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A comparative analysis of 23 structures of the amyloidogenic protein transthyretin

21 January 2018

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Identification of a subunit interface in transthyretin amyloid fibrils: evidence for self-assembly from oligomeric building blocks

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Familial amyloidotic polyneuropathy: report of patients heterozygous for the transthyretin Gly42 gene

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Transthyretin slowly exchanges subunits under physiological conditions: A convenient chromatographic method to study subunit exchange in oligomeric proteins.

21 January 2018

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Kinetic stabilization of an oligomeric protein under physiological conditions demonstrated by a lack of subunit exchange: implications for transthyretin amyloidosis.

21 January 2018

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The most pathogenic transthyretin variant, L55P, forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions

21 January 2018

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Inhibiting transthyretin amyloid fibril formation via protein stabilization

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Protein subunit interactions and structural integrity of amyloidogenic transthyretins: evidence from electrospray mass spectrometry.

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Prevention of transthyretin amyloid disease by changing protein misfolding energetics.

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Parameters affecting the restoration of activity to inactive mutants of thymidylate synthase via subunit exchange: further evidence that thymidylate synthase is a half-of-the-sites activity enzyme

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

21 January 2018

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D18G transthyretin is monomeric, aggregation prone, and not detectable in plasma and cerebrospinal fluid: a prescription for central nervous system amyloidosis?

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

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21 January 2018

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The beta-strand D of transthyretin trapped in two discrete conformations.

21 January 2018

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Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M508753200

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30 May 2018

PubMed ID

16219761

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30 May 2018