Results 41 to 50 of about 184,458 (283)

Non-Equilibrium Protein Folding and Activation by ATP-Driven Chaperones

Biomolecules, 2022
Recent experimental studies suggest that ATP-driven molecular chaperones can stabilize protein substrates in their native structures out of thermal equilibrium. The mechanism of such non-equilibrium protein folding is an open question. Based on available
Huafeng Xu
doaj   +1 more source

β-secretase 1´s Targeting Reduces Hyperphosphorilated Tau, Implying Autophagy Actors in 3xTg-AD Mice

Frontiers in Cellular Neuroscience, 2016
β-site APP cleaving enzyme 1 (BACE1) initiates APP cleavage, which has been reported to be an inducer of tau pathology by altering proteasome functions in Alzheimer’s disease (AD).
Diego ePiedrahita, John Fredy Castro-Alvarez, Ryan eBoudreau, Carlos Andrés Villegas, Kenneth eKosik, Juan Carlos eGallego-Gomez, Gloria Patricia eCardona-Gomez   +6 more
doaj   +1 more source

Heat shock proteins and viral infection

Frontiers in Immunology, 2022
Heat shock proteins (HSPs) are a kind of proteins which mostly found in bacterial, plant and animal cells, in which they are involved in the monitoring and regulation of cellular life activities.
Xizhen Zhang, Xizhen Zhang, Wei Yu, Wei Yu   +3 more
doaj   +1 more source

Chaperoning erythropoiesis

Blood, 2009
AbstractMultisubunit complexes containing molecular chaperones regulate protein production, stability, and degradation in virtually every cell type. We are beginning to recognize how generalized and tissue-specific chaperones regulate specialized aspects of erythropoiesis.
Mitchell J, Weiss, Camila O, dos Santos
openaire   +3 more sources

Chaperone driven polymer translocation through Nanopore: spatial distribution and binding energy

, 2016
Chaperones are binding proteins which work as a driving force to bias the biopolymer translocation by binding to it near the pore and preventing its backsliding. Chaperones may have different spatial distribution. Recently we show the importance of their
Abdolvahab, Rouhollah Haji
core   +1 more source

The Role of the Heat Shock Protein B8 (HSPB8) in Motoneuron Diseases

Frontiers in Molecular Neuroscience, 2017
Amyotrophic lateral sclerosis (ALS) and spinal and bulbar muscular atrophy (SBMA) are two motoneuron diseases (MNDs) characterized by aberrant protein behavior in affected cells.
Paola Rusmini, Riccardo Cristofani, Mariarita Galbiati, Maria E. Cicardi, Marco Meroni, Veronica Ferrari, Giulia Vezzoli, Barbara Tedesco, Elio Messi, Margherita Piccolella, Serena Carra, Valeria Crippa, Valeria Crippa, Angelo Poletti, Angelo Poletti   +14 more
doaj   +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
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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

Select pyrimidinones inhibit the propagation of the malarial parasite, Plasmodium falciparum [PDF]

, 2009
Plasmodium falciparum, the Apicomplexan parasite that is responsible for the most lethal forms of human malaria, is exposed to radically different environments and stress factors during its complex lifecycle.
Annette N. Chiang, Banumathy, Billy W. Day, Botha, Brian P. Mead, Chiu, Corinne Schneider, Craig, David A. Fidock, Donna M. Huryn, Ekland, Fernandez-Saiz, Fewell, Fewell, Fewell, Fidock, Frydman, Hartl, Hunt, Jeffrey L. Brodsky, Jiang, Juan-Carlos Valderramos, Maier, Matambo, Mayer, McClellan, McKerrow, Michael G. Klein, Midorikawa, Nadeau, Noedl, Pavithra, Pecoul, Peter Wipf, Raghavan Balachandran, Raj J. Chovatiya, Ramya, Rodina, Samantha L. Bell, Shonhai, Shonhai, Sidhu, Tang, Tonkin, Wellems, Werner, Wright, Xiaojiang S. Chen, Youker   +48 more
core   +1 more source

The Crimson Conundrum: Heme Toxicity and Tolerance in GAS

Frontiers in Cellular and Infection Microbiology, 2014
The massive erythrocyte lysis caused by the Group A Streptococcus (GAS) suggests that the β-hemolytic pathogen is likely to encounter free heme during the course of infection.
ANKITA JAGDISH SACHLA, Yoann Stephane Le Breton, Fahmina eAkhter, Kevin S McIver, Zehava eEichenbaum   +4 more
doaj   +1 more source