Results 71 to 80 of about 183,487 (307)

Disruption of the Ubiquitin-Proteasome System and Elevated Endoplasmic Reticulum Stress in Epilepsy

Biomedicines, 2022
The epilepsies are a broad group of conditions characterized by repeated seizures, and together are one of the most common neurological disorders. Additionally, epilepsy is comorbid with many neurological disorders, including lysosomal storage diseases ...
Sarah Poliquin, Jing-Qiong Kang
doaj   +1 more source

Proteostasis collapse is a driver of cell aging and death. [PDF]

, 2019
What molecular processes drive cell aging and death? Here, we model how proteostasis-i.e., the folding, chaperoning, and maintenance of protein function-collapses with age from slowed translation and cumulative oxidative damage.
de Graff, Adam MR, Dill, Ken A, Santra, Mantu   +2 more
core  

Chaperone-assisted translocation of a polymer through a nanopore

, 2011
Using Langevin dynamics simulations, we investigate the dynamics of chaperone-assisted translocation of a flexible polymer through a nanopore. We find that increasing the binding energy $\epsilon$ between the chaperone and the chain and the chaperone ...
Abdolvahab R. H., Abdolvahab R. H., Alberts B., Allen M. P., Ambjörnsson T., Ambjörnsson T., Branton D., Chuang C., de Gennes P.-G., D’Orsogna M. R., Elston T. C., Ermak D. L., Farkas K., Han J., Hanss B., Holowka E. P., Huopaniemi I., Kaifu Luo, Kantor Y., Kasianowicz J. J., Krapivsky P. L., Liebermeister W., Luo K., Luo K., Luo K., Luo K., Matlack K. E. S., Matlack K. E. S., Meller A., Meller A., Meller A., Metzler R., Muthukumar M., Neupert W., Salman H., Simon S. M., Sung W., Wancheng Yu, Zandi R.   +38 more
core   +1 more source

Small heat-shock proteins: important players in regulating cellular proteostasis [PDF]

, 2015
Small heat-shock proteins (sHsps) are a diverse family of intra-cellular molecular chaperone proteins that play a critical role in mitigating and preventing protein aggregation under stress conditions such as elevated temperature, oxidation and infection.
Carver, John A., Ecroyd, Heath, Meehan, Sarah, Treweek, Teresa M.   +3 more
core   +1 more source

Promiscuous stimulation of HSP70 ATPase activity by parasite‐derived J‐domains

FEBS Open Bio, EarlyView.
The malaria parasite Plasmodium falciparum exports three highly homologous yet functionally divergent J‐domain proteins into human erythrocytes. Here, we show that J‐domains isolated from all three proteins effectively stimulate the ATPase activity of both endogenous host and exported parasite HSP70 chaperones.
Julian Barth, Moritz Koch, Le‐Han Rössner, Johanna Eichhorn, Denys Pogoryelov, Matthias P. Mayer, Jude M. Przyborski   +6 more
wiley   +1 more source

Hsp90 Inhibitors and the Reduction of Anti-Cancer Drug Resistance by Non-Genetic and Genetic Mechanisms

Pharmaceuticals, 2012
In this review, we focus on how inhibitors of Hsp90 can help prevent the resistance to anti-cancer drugs by synergistically increasing their cancer killing abilities and thereby allowing them to function at much lower concentrations than normally used ...
Douglas M. Ruden, Xiangyi Lu, Luan Wang
doaj   +1 more source

YlmG1 is localized exclusively to the chloroplast envelope membrane and is involved in preprotein translocation in Arabidopsis thaliana

FEBS Open Bio, EarlyView.
Cytosolically synthesized chloroplast preproteins are translocated across the outer and inner envelope membranes through translocons called TOC and TIC, respectively. In green algae and plants, the TIC core is composed of essential membrane proteins, Tic12, Tic20, and Tic214.
Mengyi Li, Xueyang Zhao, Masato Nakai
wiley   +1 more source

Abnormal Copper Homeostasis: Mechanisms and Roles in Neurodegeneration

Toxics, 2014
As a cofactor of proteins and enzymes involved in critical molecular pathways in mammals and low eukaryotes, copper is a transition metal essential for life.
Mario Manto
doaj   +1 more source

Directed motion emerging from two coupled random processes: Translocation of a chain through a membrane nanopore driven by binding proteins

, 2005
We investigate the translocation of a stiff polymer consisting of M monomers through a nanopore in a membrane, in the presence of binding particles (chaperones) that bind onto the polymer, and partially prevent backsliding of the polymer through the pore.
Alberts B, Ambjörnsson T, Ambjörnsson T, Bates M, Chauwin J-F, Elston T C, Elston T C, Farkas Z, Gardiner C W, Gerland U, Harada Y, Lubensky D K, McQuistan R B, Meller A, Metzler R, Metzler R, Michael A Lomholt, Peskin C S, Press W H, Ralf Metzler, Risken H, Simon S F, Tobias Ambjörnsson, van Kampen N G   +23 more
core   +2 more sources

Evolutionarily divergent DUF4465 domains have a common vitamin B12‐binding function

FEBS Open Bio, EarlyView.
We show that DUF4465 family proteins, widespread across bacteria from gut microbiomes, hydrothermal vents, and soil, share a common vitamin B12‐binding function. These augmented β‐jellyroll proteins bind vitamin B12 via extended loops. Our findings establish sequence‐diverse DUF4465 proteins as a widespread class of B12‐binding proteins, highlighting ...
Charlea Clarke, Michal Banasik, Rokas Juodeikis, Martin J. Warren, Richard W. Pickersgill   +4 more
wiley   +1 more source