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 …
Advances in hydrogen/deuterium exchange mass spectrometry and the pursuit of challenging biological systems
EI James, TA Murphree, C Vorauer, JR Engen… - Chemical …, 2021 - ACS Publications
Solution-phase hydrogen/deuterium exchange (HDX) coupled to mass spectrometry (MS) is
a widespread tool for structural analysis across academia and the biopharmaceutical …
a widespread tool for structural analysis across academia and the biopharmaceutical …
The Hsc70 disaggregation machinery removes monomer units directly from α-synuclein fibril ends
Molecular chaperones contribute to the maintenance of cellular protein homoeostasis
through assisting de novo protein folding and preventing amyloid formation. Chaperones of …
through assisting de novo protein folding and preventing amyloid formation. Chaperones of …
G-quadruplexes rescuing protein folding
Maintaining the health of the proteome is a critical cellular task. Recently, we found G-
quadruplex (G4) nucleic acids are especially potent at preventing protein aggregation in …
quadruplex (G4) nucleic acids are especially potent at preventing protein aggregation in …
Elucidating the novel mechanisms of molecular chaperones by single-molecule technologies
Molecular chaperones play central roles in sustaining protein homeostasis and preventing
protein aggregation. Most studies of these systems have been performed in bulk, providing …
protein aggregation. Most studies of these systems have been performed in bulk, providing …
A proteome-wide map of chaperone-assisted protein refolding in a cytosol-like milieu
The journey by which proteins navigate their energy landscapes to their native structures is
complex, involving (and sometimes requiring) many cellular factors and processes operating …
complex, involving (and sometimes requiring) many cellular factors and processes operating …
A diminished hydrophobic effect inside the GroEL/ES cavity contributes to protein substrate destabilization
I Korobko, RB Eberle, M Roy… - Proceedings of the …, 2022 - National Acad Sciences
Confining compartments are ubiquitous in biology, but there have been few experimental
studies on the thermodynamics of protein folding in such environments. Recently, we …
studies on the thermodynamics of protein folding in such environments. Recently, we …
A temporal gradient of cytonuclear coordination of chaperonins and chaperones during RuBisCo biogenesis in allopolyploid plants
C Li, B Ding, X Ma, X Yang, H Wang… - Proceedings of the …, 2022 - National Acad Sciences
Ribulose-1, 5-bisphosphate carboxylase/oxygenase (RuBisCo) has long been studied from
many perspectives. As a multisubunit (large subunits [LSUs] and small subunits [SSUs]) …
many perspectives. As a multisubunit (large subunits [LSUs] and small subunits [SSUs]) …
Intrinsically disordered regions promote protein refoldability and facilitate retrieval from biomolecular condensates
P To, AM Bhagwat, HE Tarbox, A Ecer, H Wendorff… - bioRxiv, 2023 - biorxiv.org
Many eukaryotic proteins contain intrinsically disordered regions (IDRs) that intersperse
globular folded domains, in contrast with bacterial proteins which are typically highly …
globular folded domains, in contrast with bacterial proteins which are typically highly …
Conserved and divergent chaperoning effects of Hsp60/10 chaperonins on protein folding landscapes
The GroEL/ES chaperonin cavity surface charge properties, especially the negative charges,
play an important role in its capacity to assist intracavity protein folding. Remarkably, the …
play an important role in its capacity to assist intracavity protein folding. Remarkably, the …