L55P transthyretin accelerates subunit exchange and leads to rapid formation of hybrid tetramers. (Q54477460)

30 May 2018

title

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

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6

Carol V Robinson

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author name string

Catherine A Keetch

1

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Elizabeth H C Bromley

2

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Margaret G McCammon

3

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Nan Wang

4

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John Christodoulou

5

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language of work or name

English

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publication date

11 October 2005

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Journal of Biological Chemistry

published in

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volume

280

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issue

50

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page(s)

41667-41674

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Folding proteins in fatal ways

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

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Subunit Exchange of αA-Crystallin

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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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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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21 January 2018

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21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M508753200

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30 May 2018

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30 May 2018