Understanding the self-assembly pathways of a single chain variant of monellin: A first step towards the design of sweet nanomaterials-Reference-Cited by-同舟云学术

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Understanding the self-assembly pathways of a single chain variant of monellin: A first step towards the design of sweet nanomaterials

Published:2020-06 Issue: Volume:152 Page:21-29
ISSN:0141-8130
Container-title:International Journal of Biological Macromolecules
language:en
Short-container-title:International Journal of Biological Macromolecules

Author:

Delfi Masoud,Leone Serena,Emendato Alessandro,Ami Diletta,Borriello Margherita,Natalello Antonino,Iannuzzi Clara,Picone Delia

Funder

Italian Ministry of University and Research

Publisher

Elsevier BV

Subject

Molecular Biology,General Medicine,Biochemistry,Structural Biology

Reference82 articles.

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2. Implications of peptide assemblies in amyloid diseases;Ke;Chem. Soc. Rev.,2017

3. Protein misfolding, functional amyloid, and human disease;Chiti;Annu. Rev. Biochem.,2006

4. Amyloid formation by globular proteins under native conditions;Chiti;Nat. Chem. Biol.,2009

5. Amyloid fibrils from muscle myoglobin;Fändrich;Nature,2001

Cited by 3 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. Structural insights and aggregation propensity of a super-stable monellin mutant: A new potential building block for protein-based nanostructured materials;International Journal of Biological Macromolecules;2024-01

2. Investigating the Effect of Substituting a Single Cysteine Residue on the Thermal Stability of an Engineered Sweet Protein, Single-Chain Monellin;The Protein Journal;2023-09-22

3. Understanding the Role of Protein Glycation in the Amyloid Aggregation Process;International Journal of Molecular Sciences;2021-06-21

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