Literature DB >> 10507026

In vitro immunoglobulin light chain fibrillogenesis.

J Wall1, C L Murphy, A Solomon.   

Abstract

These techniques permit the production of bulk quantities of fibrils and provide methods for monitoring the kinetics of fibrillogenesis. Experiments performed in the fluorimeter require low protein concentrations, sampling is not necessary (with ThT in situ), and the measured fluorescence signal is indicative of fibril content and is not complicated by the presence of amorphous aggregates. However, ASF using the orbital shaker is a simple, rapid, initial procedure, adequate for screening for fibrillogenic potential, in which multiple experiments can be performed simultaneously and over long periods of incubation. These methods may be used to investigate the fibrillogenesis of VL proteins and BJps as a means of predicting pathogenicity, as well as providing information on the basic biophysical principles underlying light chain aggregation.

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Year:  1999        PMID: 10507026     DOI: 10.1016/s0076-6879(99)09016-3

Source DB:  PubMed          Journal:  Methods Enzymol        ISSN: 0076-6879            Impact factor:   1.600


  26 in total

1.  Analysis of somatic hypermutation and antigenic selection in the clonal B cell in immunoglobulin light chain amyloidosis (AL).

Authors:  Roshini S Abraham; Susan M Geyer; Marina Ramírez-Alvarado; Tammy L Price-Troska; Morie A Gertz; Rafael Fonseca
Journal:  J Clin Immunol       Date:  2004-07       Impact factor: 8.317

Review 2.  Plasticity of amyloid fibrils.

Authors:  Ronald Wetzel; Shankaramma Shivaprasad; Angela D Williams
Journal:  Biochemistry       Date:  2007-01-09       Impact factor: 3.162

3.  Site-directed mutagenesis reveals regions implicated in the stability and fiber formation of human λ3r light chains.

Authors:  Miryam I Villalba; Juan C Canul-Tec; Oscar D Luna-Martínez; Rosalba Sánchez-Alcalá; Timoteo Olamendi-Portugal; Enrique Rudiño-Piñera; Sonia Rojas; Rosana Sánchez-López; Daniel A Fernández-Velasco; Baltazar Becerril
Journal:  J Biol Chem       Date:  2014-12-11       Impact factor: 5.157

4.  Identification of two principal amyloid-driving segments in variable domains of Ig light chains in systemic light-chain amyloidosis.

Authors:  Boris Brumshtein; Shannon R Esswein; Michael R Sawaya; Gregory Rosenberg; Alan T Ly; Meytal Landau; David S Eisenberg
Journal:  J Biol Chem       Date:  2018-10-24       Impact factor: 5.157

5.  Formation of amyloid fibers by monomeric light chain variable domains.

Authors:  Boris Brumshtein; Shannon R Esswein; Meytal Landau; Christopher M Ryan; Julian P Whitelegge; Martin L Phillips; Duilio Cascio; Michael R Sawaya; David S Eisenberg
Journal:  J Biol Chem       Date:  2014-08-19       Impact factor: 5.157

6.  Recruitment of Light Chains by Homologous and Heterologous Fibrils Shows Distinctive Kinetic and Conformational Specificity.

Authors:  Luis M Blancas-Mejía; Marina Ramirez-Alvarado
Journal:  Biochemistry       Date:  2016-05-16       Impact factor: 3.162

7.  Four crystal forms of a Bence-Jones protein.

Authors:  Debora L Makino; Agnes H Henschen-Edman; Alexander McPherson
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2004-12-02

8.  SLLISWD sequence in the 10FNIII domain initiates fibronectin fibrillogenesis.

Authors:  Elaine P S Gee; Deniz Yüksel; Collin M Stultz; Donald E Ingber
Journal:  J Biol Chem       Date:  2013-06-05       Impact factor: 5.157

9.  The Kinetic Stability of a Full-Length Antibody Light Chain Dimer Determines whether Endoproteolysis Can Release Amyloidogenic Variable Domains.

Authors:  Gareth J Morgan; Jeffery W Kelly
Journal:  J Mol Biol       Date:  2016-08-26       Impact factor: 5.469

10.  Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils-current status.

Authors:  Minna Groenning
Journal:  J Chem Biol       Date:  2009-08-20
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