[HTML][HTML] The role of lysosomal cathepsins in neurodegeneration: Mechanistic insights, diagnostic potential and therapeutic approaches

A Drobny, SP Huarcaya, J Dobert, A Kluge… - … et Biophysica Acta (BBA …, 2022‏ - Elsevier
Lysosomes are ubiquitous organelles with a fundamental role in maintaining cellular
homeostasis by mediating degradation and recycling processes. Cathepsins are the most …

A new kid in the folding funnel: Molecular chaperone activities of the BRICHOS domain

A Leppert, H Poska, M Landreh, A Abelein… - Protein …, 2023‏ - Wiley Online Library
The BRICHOS protein superfamily is a diverse group of proteins associated with a wide
variety of human diseases, including respiratory distress, COVID‐19, dementia, and cancer …

Identification of potential aggregation hotspots on Aβ42 fibrils blocked by the anti-amyloid chaperone-like BRICHOS domain

R Kumar, T Le Marchand, L Adam, R Bobrovs… - Nature …, 2024‏ - nature.com
Protein misfolding can generate toxic intermediates, which underlies several devastating
diseases, such as Alzheimer's disease (AD). The surface of AD-associated amyloid-β …

Doing what spiders cannot—A road map to supreme artificial silk fibers

J Johansson, A Rising - ACS nano, 2021‏ - ACS Publications
Fabricating artificial spider silk fibers in bulk scale has been a major goal in materials
science for centuries. Two main routes have emerged for making such fibers. One method …

Abilities of the BRICHOS domain to prevent neurotoxicity and fibril formation are dependent on a highly conserved Asp residue

G Chen, Y Andrade-Talavera, X Zhong… - RSC chemical …, 2022‏ - pubs.rsc.org
Proteins can self-assemble into amyloid fibrils or amorphous aggregates and thereby cause
disease. Molecular chaperones can prevent both these types of protein aggregation, but to …

Short hydrophobic loop motifs in BRICHOS domains determine chaperone activity against amorphous protein aggregation but not against amyloid formation

G Chen, A Leppert, H Poska, HE Nilsson… - Communications …, 2023‏ - nature.com
ATP-independent molecular chaperones are important for maintaining cellular fitness but
the molecular determinants for preventing aggregation of partly unfolded protein substrates …

[HTML][HTML] Bri2 BRICHOS chaperone rescues impaired fast-spiking interneuron behavior and neuronal network dynamics in an AD mouse model in vitro

Y Andrade-Talavera, G Chen, FR Kurudenkandy… - Neurobiology of …, 2021‏ - Elsevier
Synchronized and properly balanced electrical activity of neurons is the basis for the brain's
ability to process information, to learn, and to remember. In Alzheimer's disease (AD), which …

[HTML][HTML] Identification of cytoskeletal proteins as binding partners of Bri2 BRICHOS domain

M Shimozawa, H Tigro, H Biverstål… - Molecular and Cellular …, 2023‏ - Elsevier
Proteins must fold into three-dimensional structures to execute their biological functions.
Therefore, maintenance of protein homeostasis, proteostasis, including prevention of protein …

Molecular basis for different substrate‐binding sites and chaperone functions of the BRICHOS domain

G Chen, Y Wang, Z Zheng, W Jiang, A Leppert… - Protein …, 2024‏ - Wiley Online Library
Proteins can misfold into fibrillar or amorphous aggregates and molecular chaperones act
as crucial guardians against these undesirable processes. The BRICHOS chaperone …

[HTML][HTML] Exploring the role of British dementia protein-2 (Bri2) and its BRICHOS domain in neurodegenerative disorders

W Ahmad, T Zhao, KF He, SZ Luo - Supramolecular Materials, 2024‏ - Elsevier
Protein functionality hinges on precise three-dimensional structures, while molecular
chaperones orchestrate folding, proteome maintenance, and proteostasis. Recent attention …