Results 61 to 70 of about 4,011,919 (357)

Protein Quality Control by Molecular Chaperones in Neurodegeneration

Frontiers in Neuroscience, 2017
Protein homeostasis (proteostasis) requires the timely degradation of misfolded proteins and their aggregates by protein quality control (PQC), of which molecular chaperones are an essential component.
A. Ciechanover, Y. Kwon
semanticscholar   +1 more source

Hematopoietic (stem) cells—The elixir of life?

FEBS Letters, EarlyView.
The aging of HSCs (hematopoietic stem cells) and the blood system leads to the decline of other organs. Rejuvenating aged HSCs improves the function of the blood system, slowing the aging of the heart, kidney, brain, and liver, and the occurrence of age‐related diseases.
Emilie L. Cerezo, Jonah Anderson, Emilie Dinh Vedrenne, Noël Yeh Martín, Jette Lengefeld   +4 more
wiley   +1 more source

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

Journal of Biological Chemistry, 2018
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 loop and a conserved His–Pro–Asp motif required for ATP hydrolysis by ...
M. Mayer, L. Gierasch
semanticscholar   +1 more source

The role of histone modifications in transcription regulation upon DNA damage

FEBS Letters, EarlyView.
This review discusses the critical role of histone modifications in regulating gene expression during the DNA damage response (DDR). By modulating chromatin structure and recruiting repair factors, these post‐translational modifications fine‐tune transcriptional programmes to maintain genomic stability.
Angelina Job Kolady, Siyao Wang
wiley   +1 more source

Chaperones as integrators of cellular networks: Changes of cellular integrity in stress and diseases

, 2008
Cellular networks undergo rearrangements during stress and diseases. In un-stressed state the yeast protein-protein interaction network (interactome) is highly compact, and the centrally organized modules have a large overlap.
Albanese, Albert, Almaas, Arita, Barabasi, Barabasi, Batada, Batada, Batagelj, Bertin, Bobula, Colizza, Csermely, Csermely, Csermely, Csermely, Derenyi, Ekman, Gasch, Goldberger, Guimerá, Han, Kim, Komurov, Korcsmaros, Korcsmáros, Lewandowska, Linding, Luscombe, Macario, Maslov, McAuley, McClellan, Ng, Palla, Papp, Pál, Ravasz, Rutherford, Sales-Pardo, Shorter, Song, Soti, Soti, Soti, Szabadkai, Szalay, Tanaka, Taxis, Vigh, Wang, Watts, Xu, Yu, Zhu   +54 more
core   +2 more sources

Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators.

Genes & Development, 1998
Our cells and tissues are challenged constantly by exposure to extreme conditions that cause acute and chronic stress. Consequently, survival has necessitated the evolution of stress response networks to detect, monitor, and respond to environmental ...
R. Morimoto
semanticscholar   +1 more source

Structural instability impairs function of the UDP‐xylose synthase 1 Ile181Asn variant associated with short‐stature genetic syndrome in humans

FEBS Letters, EarlyView.
The Ile181Asn variant of human UDP‐xylose synthase (hUXS1), associated with a short‐stature genetic syndrome, has previously been reported as inactive. Our findings demonstrate that Ile181Asn‐hUXS1 retains catalytic activity similar to the wild‐type but exhibits reduced stability, a looser oligomeric state, and an increased tendency to precipitate ...
Tuo Li, Pedro A. Sánchez‐Murcia, Bernd Nidetzky   +2 more
wiley   +1 more source

How do Chaperones Bind (Partly) Unfolded Client Proteins?

Frontiers in Molecular Biosciences, 2021
Molecular chaperones are central to cellular protein homeostasis. Dynamic disorder is a key feature of the complexes of molecular chaperones and their client proteins, and it facilitates the client release towards a folded state or the handover to ...
Iva Sučec, Beate Bersch, Paul Schanda, Paul Schanda   +3 more
doaj   +1 more source

COA6 facilitates cytochrome c oxidase biogenesis as thiol-reductase for copper metallochaperones in mitochondria.

, 2020
The mitochondrial cytochrome c oxidase, the terminal enzyme of the respiratory chain, contains heme and copper centers for electron transfer. The conserved COX2 subunit contains the CuA site, a binuclear copper center.
Aich, A., Bogeski, I., Chacinska, A., Chudenkova, M., Deckers, M., Dennerlein, S., Gibhardt, C., Oeljeklaus, S., Pacheu-Grau, D., Rehling, P., Warscheid, B., Wasilewski, M.   +11 more
core   +2 more sources

Cell density–dependent nuclear‐cytoplasmic shuttling of SETDB1 integrates with Hippo signaling to regulate YAP1‐mediated transcription

FEBS Letters, EarlyView.
At low cell density, SETDB1 and YAP1 accumulate in the nucleus. As cell density increases, the Hippo pathway is gradually activated, and SETDB1 is associated with increased YAP1 phosphorylation. At high cell density, phosphorylated YAP1 is sequestered in the cytoplasm, while SETDB1 becomes polyubiquitinated and degraded by the ubiquitin–proteasome ...
Jaemin Eom, Jaewoong Jang, Jung Sun Park, Yong‐Kook Kang   +3 more
wiley   +1 more source