Mechanisms and pathology of protein misfolding and aggregation
Despite advances in machine learning-based protein structure prediction, we are still far
from fully understanding how proteins fold into their native conformation. The conventional …
from fully understanding how proteins fold into their native conformation. The conventional …
In vivo aspects of protein folding and quality control
BACKGROUND Proteins are synthesized on ribosomes as linear chains of amino acids and
must fold into unique three-dimensional structures to fulfill their biological functions. Protein …
must fold into unique three-dimensional structures to fulfill their biological functions. Protein …
Molecular chaperones in protein folding and proteostasis
Most proteins must fold into defined three-dimensional structures to gain functional activity.
But in the cellular environment, newly synthesized proteins are at great risk of aberrant …
But in the cellular environment, newly synthesized proteins are at great risk of aberrant …
The GroEL–GroES chaperonin machine: a nano-cage for protein folding
The bacterial chaperonin GroEL and its cofactor GroES constitute the paradigmatic
molecular machine of protein folding. GroEL is a large double-ring cylinder with ATPase …
molecular machine of protein folding. GroEL is a large double-ring cylinder with ATPase …
Molecular chaperone functions in protein folding and proteostasis
The biological functions of proteins are governed by their three-dimensional fold. Protein
folding, maintenance of proteome integrity, and protein homeostasis (proteostasis) critically …
folding, maintenance of proteome integrity, and protein homeostasis (proteostasis) critically …
Recent advances in understanding catalysis of protein folding by molecular chaperones
Molecular chaperones are highly conserved proteins that promote proper folding of other
proteins in vivo. Diverse chaperone systems assist de novo protein folding and trafficking …
proteins in vivo. Diverse chaperone systems assist de novo protein folding and trafficking …
[HTML][HTML] DnaK functions as a central hub in the E. coli chaperone network
G Calloni, T Chen, SM Schermann, H Chang… - Cell reports, 2012 - cell.com
Cellular chaperone networks prevent potentially toxic protein aggregation and ensure
proteome integrity. Here, we used Escherichia coli as a model to understand the …
proteome integrity. Here, we used Escherichia coli as a model to understand the …
Mechanisms of cotranslational maturation of newly synthesized proteins
The timely production of functional proteins is of critical importance for the biological activity
of cells. To reach the functional state, newly synthesized polypeptides have to become …
of cells. To reach the functional state, newly synthesized polypeptides have to become …
Diversity in the origins of proteostasis networks—a driver for protein function in evolution
ET Powers, WE Balch - Nature reviews Molecular cell biology, 2013 - nature.com
Although the sequence of a protein largely determines its function, proteins can adopt
different folding states in response to changes in the environment, some of which may be …
different folding states in response to changes in the environment, some of which may be …
Principles of protein stability and their application in computational design
A Goldenzweig, SJ Fleishman - Annual review of biochemistry, 2018 - annualreviews.org
Proteins are increasingly used in basic and applied biomedical research. Many proteins,
however, are only marginally stable and can be expressed in limited amounts, thus …
however, are only marginally stable and can be expressed in limited amounts, thus …