A Single Mutation Promotes Amyloidogenicity through a Highly Promiscuous Dimer Interface (Q27661519)

identical protein binding

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

author name string

Francis C Peterson

1

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Elizabeth M Baden

2

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Barbara A L Owen

3

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Brian F Volkman

4

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Marina Ramirez-Alvarado

Structural Insights into the Role of Mutations in Amyloidogenesis

5

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publication date

12 May 2010

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published in

Structure

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volume

18

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issue

5

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page(s)

563-70

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cites work

1 reference

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Altered Dimer Interface Decreases Stability in an Amyloidogenic Protein

20 March 2017

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Three-dimensional structure of an immunoglobulin light-chain dimer with amyloidogenic properties

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Tertiary structure of human lambda 6 light chains

20 March 2017

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The structure of an entire noncovalent immunoglobulin kappa light-chain dimer (Bence-Jones protein) reveals a weak and unusual constant domains association

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Molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI refined at 2.0-Å resolution

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Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA

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Protein backbone angle restraints from searching a database for chemical shift and sequence homology

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Mutations in specific structural regions of immunoglobulin light chains are associated with free light chain levels in patients with AL amyloidosis

29 September 2017

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Structural relationship of kappa-type light chains with AL amyloidosis: multiple deletions found in a VkappaIV protein

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29 September 2017

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(CAG)(n)-hairpin DNA binds to Msh2-Msh3 and changes properties of mismatch recognition

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27 November 2018

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PubMed

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