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An expanding arsenal of experimental methods yields an explosion of insights into protein folding mechanisms

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TLDR
Improvements in experimental techniques and enhancements in computing power have revolutionized their understanding of the mechanisms of protein folding, and by combining insights gained from theory, experiment and simulation the authors are moving toward an atomistic view of folding landscapes.
Abstract
In recent years, improvements in experimental techniques and enhancements in computing power have revolutionized our understanding of the mechanisms of protein folding. By combining insights gained from theory, experiment and simulation we are moving toward an atomistic view of folding landscapes. Future challenges involve exploiting the knowledge gained and methods developed to enable us to elucidate a molecular description of folding dynamics in the complex environment of the cell.

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Molecular chaperones in protein folding and proteostasis

TL;DR: It is suggested that an age-related decline in proteostasis capacity allows the manifestation of various protein-aggregation diseases, including Alzheimer's disease and Parkinson's disease, which may spring from a detailed understanding of the pathways underlying proteome maintenance.
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Molecular Chaperone Functions in Protein Folding and Proteostasis

TL;DR: This review focuses on recent advances in understanding the mechanisms of chaperone action in promoting and regulating protein folding and on the pathological consequences of protein misfolding and aggregation.
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Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)

Daniel J. Klionsky, +2983 more
- 08 Feb 2021 - 
TL;DR: In this article, the authors present a set of guidelines for investigators to select and interpret methods to examine autophagy and related processes, and for reviewers to provide realistic and reasonable critiques of reports that are focused on these processes.
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Converging concepts of protein folding in vitro and in vivo

TL;DR: Recent concepts emerging from studies of protein folding in vitro and in vivo are reviewed, with a focus on how proteins navigate the complex folding energy landscape inside cells with the aid of molecular chaperones.
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Protein Folding and Modification in the Mammalian Endoplasmic Reticulum

TL;DR: Analysis of the human genome reveals that approximately a third of all open reading frames code for proteins that enter the endoplasmic reticulum (ER), demonstrating the importance of this organelle for global protein maturation.
References
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Journal ArticleDOI

Protein folding and misfolding

TL;DR: The manner in which a newly synthesized chain of amino acids transforms itself into a perfectly folded protein depends both on the intrinsic properties of the amino-acid sequence and on multiple contributing influences from the crowded cellular milieu.
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How to study proteins by circular dichroism

TL;DR: The basis of the CD approach and its application to the study of proteins, and clear guidelines on how reliable data can be obtained and analysed are presented.
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Funnels, pathways, and the energy landscape of protein folding: A synthesis

TL;DR: The work unifies several previously proposed ideas concerning the mechanism protein folding and delimits the regions of validity of these ideas under different thermodynamic conditions.
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Adapting proteostasis for disease intervention.

TL;DR: The proteostasis network is described, a set of interacting activities that maintain the health of proteome and the organism that has the potential to ameliorate some of the most challenging diseases of this era.
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Macromolecular crowding: obvious but underappreciated.

TL;DR: Positive results of crowding include enhancing the collapse of polypeptide chains into functional proteins, the assembly of oligomeric structures and the efficiency of action of some molecular chaperones and metabolic pathways.
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