In vivo aspects of protein folding and quality control

D Balchin, M Hayer-Hartl, FU Hartl - Science, 2016 - science.org
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 …

Molecular chaperone functions in protein folding and proteostasis

YE Kim, MS Hipp, A Bracher… - Annual review of …, 2013 - annualreviews.org
The biological functions of proteins are governed by their three-dimensional fold. Protein
folding, maintenance of proteome integrity, and protein homeostasis (proteostasis) critically …

Intracellular targeting mechanisms by antimicrobial peptides

CF Le, CM Fang, SD Sekaran - Antimicrobial agents and …, 2017 - Am Soc Microbiol
Antimicrobial peptides (AMPs) are expressed in various living organisms as first-line host
defenses against potential harmful encounters in their surroundings. AMPs are short …

Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones

MP Mayer, LM Gierasch - Journal of Biological Chemistry, 2019 - ASBMB
Hsp70 chaperones are central hubs of the protein quality control network and collaborate
with co-chaperones having a J-domain (an∼ 70-residue–long helical hairpin with a flexible …

The GroEL–GroES chaperonin machine: a nano-cage for protein folding

M Hayer-Hartl, A Bracher, FU Hartl - Trends in biochemical sciences, 2016 - cell.com
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 …

A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways

M Taipale, G Tucker, J Peng, I Krykbaeva, ZY Lin… - Cell, 2014 - cell.com
Chaperones are abundant cellular proteins that promote the folding and function of their
substrate proteins (clients). In vivo, chaperones also associate with a large and diverse set …

Recent advances in understanding catalysis of protein folding by molecular chaperones

D Balchin, M Hayer‐Hartl, FU Hartl - FEBS letters, 2020 - Wiley Online Library
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 …

Functional modules of the proteostasis network

GG Jayaraj, MS Hipp, FU Hartl - Cold Spring Harbor …, 2020 - cshperspectives.cshlp.org
Cells invest in an extensive network of factors to maintain protein homeostasis (proteostasis)
and prevent the accumulation of potentially toxic protein aggregates. This proteostasis …

Protein folding and mechanisms of proteostasis

JF Díaz-Villanueva, R Díaz-Molina… - International journal of …, 2015 - mdpi.com
Highly sophisticated mechanisms that modulate protein structure and function, which involve
synthesis and degradation, have evolved to maintain cellular homeostasis. Perturbations in …

How hsp70 molecular machines interact with their substrates to mediate diverse physiological functions

EM Clerico, JM Tilitsky, W Meng… - Journal of molecular …, 2015 - Elsevier
Hsp70 molecular chaperones are implicated in a wide variety of cellular processes,
including protein biogenesis, protection of the proteome from stress, recovery of proteins …