Protein Disorder Prevails under Crowded Conditions-Reference-Cited by-同舟云学术

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Protein Disorder Prevails under Crowded Conditions

Published:2011-06-14 Issue:26 Volume:50 Page:5834-5844
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Szasz Cs.¹,Alexa A.¹²,Toth K.³,Rakacs M.¹²,Langowski J.³,Tompa P.¹⁴⁵

Affiliation:

1. Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary

2. Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary

3. Division Biophysics of Macromolecules, German Cancer Research Center, Heidelberg, Germany

4. VIB Department of Structural Biology, Brussels, Belgium

5. Vrije Universiteit Brussel, Brussels, Belgium

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi200365j

Reference45 articles.

1. Macromolecular crowding: obvious but underappreciated

2. Models for Excluded Volume Interaction between an Unfolded Protein and Rigid Macromolecular Cosolutes: Macromolecular Crowding and Protein Stability Revisited

3. Molecular crowding enhances native state stability and refolding rates of globular proteins

4. Forcing Thermodynamically Unfolded Proteins to Fold

5. Solvent-induced collapse of α-synuclein and acid-denatured cytochrome c

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1. Clustering of RNA Polymerase II C-Terminal Domain Models upon Phosphorylation;2024-07-02

2. Aggregation of an FG nucleoporin under crowded conditions;2024-04-19

3. Trehalose promotes structural disorderness of intrinsically disordered casein proteins with enhanced chaperone function;Journal of Molecular Liquids;2023-09

4. The Action of Chemical Denaturants: From Globular to Intrinsically Disordered Proteins;Biology;2023-05-22

5. Fuzzy Drug Targets: Disordered Proteins in the Drug-Discovery Realm;ACS Omega;2023-03-08

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