Mitochondrial quality control proteases and their modulation for cancer therapy

J Zhang, W Qiao, Y Luo - Medicinal Research Reviews, 2023 - Wiley Online Library
Mitochondria, the main provider of energy in eukaryotic cells, contains more than 1000
different proteins and is closely related to the development of cells. However, damaged …

Advances in NMR spectroscopy of weakly aligned biomolecular systems

SC Chiliveri, AJ Robertson, Y Shen, DA Torchia… - Chemical …, 2021 - ACS Publications
The measurement and application of residual dipolar couplings (RDCs) in solution NMR
studies of biological macromolecules has become well established over the past quarter of a …

NMR methods for exploring 'dark'states in ligand binding and protein-protein interactions

V Tugarinov, A Ceccon, GM Clore - Progress in nuclear magnetic …, 2022 - Elsevier
A survey, primarily based on work in the authors' laboratory during the last 10 years, is
provided of recent developments in NMR studies of exchange processes involving protein …

Targeting PDZ domains as potential treatment for viral infections, neurodegeneration and cancer

C Nardella, L Visconti, F Malagrinò, L Pagano… - Biology Direct, 2021 - Springer
The interaction between proteins is a fundamental event for cellular life that is generally
mediated by specialized protein domains or modules. PDZ domains are the largest class of …

Competing stress-dependent oligomerization pathways regulate self-assembly of the periplasmic protease-chaperone DegP

RW Harkness, Y Toyama, ZA Ripstein… - Proceedings of the …, 2021 - National Acad Sciences
DegP is an oligomeric protein with dual protease and chaperone activity that regulates
protein homeostasis and virulence factor trafficking in the periplasm of gram-negative …

Dissecting the role of interprotomer cooperativity in the activation of oligomeric high-temperature requirement A2 protein

Y Toyama, RW Harkness… - Proceedings of the …, 2021 - National Acad Sciences
The human high-temperature requirement A2 (HtrA2) mitochondrial protease is critical for
cellular proteostasis, with mutations in this enzyme closely associated with the onset of …

Structural basis of protein substrate processing by human mitochondrial high-temperature requirement A2 protease

Y Toyama, RW Harkness… - Proceedings of the …, 2022 - National Acad Sciences
The human high-temperature requirement A2 (HtrA2) protein is a trimeric protease that
cleaves misfolded proteins to protect cells from stresses caused by toxic, proteinaceous …

Large chaperone complexes through the lens of nuclear magnetic resonance spectroscopy

TK Karamanos, GM Clore - Annual review of biophysics, 2022 - annualreviews.org
Molecular chaperones are the guardians of the proteome inside the cell. Chaperones
recognize and bind unfolded or misfolded substrates, thereby preventing further …

Flexible client-dependent cages in the assembly landscape of the periplasmic protease-chaperone DegP

RW Harkness, ZA Ripstein, JM Di Trani… - Journal of the American …, 2023 - ACS Publications
The periplasmic protein DegP, which is implicated in virulence factor transport leading to
pathogenicity, is a bi-functional protease and chaperone that helps to maintain protein …

Structural basis of substrate recognition and allosteric activation of the proapoptotic mitochondrial HtrA2 protease

EE Aspholm, J Lidman, BM Burmann - Nature Communications, 2024 - nature.com
The mitochondrial serine protease HtrA2 is a human homolog of the Escherichia coli Deg-
proteins exhibiting chaperone and proteolytic roles. HtrA2 is involved in both apoptotic …