Temperature induced structural transitions from native to unfolded aggregated states of tobacco etch virus protease-Reference-Cited by-同舟云学术

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Temperature induced structural transitions from native to unfolded aggregated states of tobacco etch virus protease

Published:2015-02 Issue: Volume:1082 Page:80-90
ISSN:0022-2860
Container-title:Journal of Molecular Structure
language:en
Short-container-title:Journal of Molecular Structure

Author:

Zhu Guo-Fei,Ren Si-Yan,Xi Lei,Du Lin-Fang,Zhu Xiao-Feng

Funder

National Key Technology R&D program of China

Science & Technology Foundation of Sichuan Province

Publisher

Elsevier BV

Subject

Inorganic Chemistry,Organic Chemistry,Spectroscopy,Analytical Chemistry

Reference59 articles.

1. Conformational plasticity of cryptolepain: Accumulation of partially unfolded states in denaturants induced equilibrium unfolding

2. Principles of protein folding, misfolding and aggregation

3. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution

4. Protein Folding, Misfolding, Aggregation and Their Implications in Human Diseases: Discovering Therapeutic Ways to Amyloid-Associated Diseases

5. Equilibrium unfolding of A. niger RNase: pH dependence of chemical and thermal denaturation

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2. A probabilistic view of protein stability, conformational specificity, and design;Scientific Reports;2023-09-19

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4. Characterization of structural and functional properties of soybean 11S globulin during the renaturation after the guanidine hydrochloride denaturation;Food Hydrocolloids;2022-09

5. Effects of temperature and pH on the structure of a protease from Lactobacillus brevis R4 isolated from Harbin dry sausage and molecular docking of the protease to the meat proteins;Food Bioscience;2021-08

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