Site-Specific Interactions with Copper Promote Amyloid Fibril Formation for λ6aJL2-R24G-Reference-Cited by-同舟云学术

Site-Specific Interactions with Copper Promote Amyloid Fibril Formation for λ6aJL2-R24G

Published:2020-03-23 Issue:13 Volume:5 Page:7085-7095
ISSN:2470-1343
Container-title:ACS Omega
language:en
Short-container-title:ACS Omega

Author:

Pelaez-Aguilar Angel E.¹,Valdés-García Gilberto²,French-Pacheco Leidys³,Pastor Nina¹²^ORCID,Amero Carlos³^ORCID,Rivillas-Acevedo Lina¹^ORCID

Affiliation:

1. Centro de Investigación en Dinámica Celular-IICBA, Universidad Autónoma del Estado de Morelos, Cuernavaca, Morelos 62209, Mexico

2. Department of Molecular Medicine and Bioprocesses, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Cuernavaca, Morelos 62210, Mexico

3. Centro de Investigaciones Químicas-IICBA, Universidad Autónoma del Estado de Morelos, Cuernavaca, Morelos 62209, Mexico

Funder

Consejo Nacional de Ciencia y Tecnolog?a

Publisher

American Chemical Society (ACS)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.acs.org/doi/pdf/10.1021/acsomega.9b03220

Reference77 articles.

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1. Cu(II) binding to the λ6aJL2-R24G antibody light chain protein associated with light chain amyloidosis disease: The role of histidines;International Journal of Biological Macromolecules;2024-06

2. Unveiling the Effects of Copper Ions in the Aggregation of Amyloidogenic Proteins;Molecules;2023-09-05

3. Unfolding and Aggregation Pathways of Variable Domains from Immunoglobulin Light Chains;Biochemistry;2023-02-21

4. From the Light Chain Sequence to the Tissue Microenvironment: Contribution of the Mesangial Cells to Glomerular Amyloidosis;Hemato;2022-03-17

5. Cu(II) Binding Increases the Soluble Toxicity of Amyloidogenic Light Chains;International Journal of Molecular Sciences;2022-01-16