The seesaw between normal function and protein aggregation: How functional interactions may increase protein solubility-Reference-Cited by-同舟云学术

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The seesaw between normal function and protein aggregation: How functional interactions may increase protein solubility

Published:2021-03-29 Issue:6 Volume:43 Page:2100031
ISSN:0265-9247
Container-title:BioEssays
language:en
Short-container-title:BioEssays

Author:

Temussi Piero Andrea¹,Tartaglia Gian Gaetano²³,Pastore Annalisa¹^ORCID

Affiliation:

1. UK Dementia Research Institute at King's College London The Maurice Wohl Institute London UK

2. Center for Human Technologies Central RNA laboratory Istituto Italiano di Tecnologia Genova Italy

3. Charles Darwin Department of Biology and Biotechnology Sapienza University of Rome Rome Italy

Publisher

Wiley

Subject

General Biochemistry, Genetics and Molecular Biology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/bies.202100031

Reference84 articles.

1. Protein misfolding and disease: from the test tube to the organism

2. Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world

3. A century-old debate on protein aggregation and neurodegeneration enters the clinic

4. Shifts and drifts in prion science

5. The two faces of protein misfolding: gain- and loss-of-function in neurodegenerative diseases

Cited by 4 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Amyloid fibrils act as a reservoir of soluble oligomers, the main culprits in protein deposition diseases;BioEssays;2022-09-14

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

3. Aggregation is a Context-Dependent Constraint on Protein Evolution;Frontiers in Molecular Biosciences;2021-06-18

4. Cryptic amyloidogenic regions in intrinsically disordered proteins: Function and disease association;Computational and Structural Biotechnology Journal;2021

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