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 …
[HTML][HTML] Bridging structural and cell biology with cryo-electron microscopy
E Nogales, J Mahamid - Nature, 2024 - nature.com
Most life scientists would agree that understanding how cellular processes work requires
structural knowledge about the macromolecules involved. For example, deciphering the …
structural knowledge about the macromolecules involved. For example, deciphering the …
Aggrephagy at a glance
Cells keep their proteome functional by the action of the proteostasis network, composed of
the chaperones, the ubiquitin-proteasome system and autophagy. The decline of this …
the chaperones, the ubiquitin-proteasome system and autophagy. The decline of this …
Structural basis of plp2-mediated cytoskeletal protein folding by TRiC/CCT
The cytoskeletal proteins tubulin and actin are the obligate substrates of TCP-1 ring
complex/Chaperonin containing TCP-1 (TRiC/CCT), and their folding involves co …
complex/Chaperonin containing TCP-1 (TRiC/CCT), and their folding involves co …
STYXL1 regulates CCT complex assembly and flagellar tubulin folding in sperm formation
Y Chen, M Luo, H Tu, Y Qi, Y Guo, X Zhang… - Nature …, 2024 - nature.com
Tubulin-based microtubule is a core component of flagella axoneme and essential for sperm
motility and male fertility. Structural components of the axoneme have been well explored …
motility and male fertility. Structural components of the axoneme have been well explored …
Brain malformations and seizures by impaired chaperonin function of TRiC
F Kraft, P Rodriguez-Aliaga, W Yuan, L Franken, K Zajt… - Science, 2024 - science.org
Malformations of the brain are common and vary in severity, from negligible to potentially
fatal. Their causes have not been fully elucidated. Here, we report pathogenic variants in the …
fatal. Their causes have not been fully elucidated. Here, we report pathogenic variants in the …
Pathway and mechanism of tubulin folding mediated by TRiC/CCT along its ATPase cycle revealed using cryo-EM
The eukaryotic chaperonin TRiC/CCT assists the folding of about 10% of cytosolic proteins
through an ATP-driven conformational cycle, and the essential cytoskeleton protein tubulin …
through an ATP-driven conformational cycle, and the essential cytoskeleton protein tubulin …
A hierarchical assembly pathway directs the unique subunit arrangement of TRiC/CCT
KB Moreira, MP Collier, A Leitner, KH Li, ILS Lachapel… - Molecular Cell, 2023 - cell.com
How the essential eukaryotic chaperonin TRiC/CCT assembles from eight distinct subunits
into a unique double-ring architecture remains undefined. We show TRiC assembly involves …
into a unique double-ring architecture remains undefined. We show TRiC assembly involves …
In silico protein dynamics in the human cytoplasm: Partial folding, misfolding, fold switching, and non‐native interactions
We examine the influence of cellular interactions in all‐atom models of a section of the
Homo sapiens cytoplasm on the early folding events of the three‐helix bundle protein B …
Homo sapiens cytoplasm on the early folding events of the three‐helix bundle protein B …
Mechanistic insights into protein folding by the eukaryotic chaperonin complex CCT
TM Smith, BM Willardson - Biochemical Society Transactions, 2022 - portlandpress.com
The cytosolic chaperonin CCT is indispensable to eukaryotic life, folding the cytoskeletal
proteins actin and tubulin along with an estimated 10% of the remaining proteome …
proteins actin and tubulin along with an estimated 10% of the remaining proteome …