Results 41 to 50 of about 4,254,953 (206)

Hsp90-Associated Immunophilin Homolog Cpr7 Is Required for the Mitotic Stability of [URE3] Prion in Saccharomyces cerevisiae.

PLoS Genetics, 2015
The role of Hsp70 chaperones in yeast prion propagation is well established. Highly conserved Hsp90 chaperones participate in a number of cellular processes, such as client protein maturation, protein degradation, cellular signalling and apoptosis, but ...
Navinder Kumar, Deepika Gaur, Arpit Gupta, Anuradhika Puri, Deepak Sharma   +4 more
doaj   +1 more source

Anti-Prion Systems in Saccharomyces cerevisiae Turn an Avalanche of Prions into a Flurry

Viruses, 2022
Prions are infectious proteins, mostly having a self-propagating amyloid (filamentous protein polymer) structure consisting of an abnormal form of a normally soluble protein.
Moonil Son, Reed B. Wickner
doaj   +1 more source

From energy provision to protein synthesis: Tunnelling nanotubes as mediators of intercellular metabolic cooperation in cancer

FEBS Open Bio, EarlyView.
The cytoskeleton‐mediated transport of mitochondria via tunnelling nanotubes restores respiration, increases ATP production, rescues cells from apoptosis, activates the AKT/mTOR signalling pathway, promotes cell migration and invasiveness, contributes to cancer progression and treatment resistance.
Stanislava Martínková, Jan Trnka
wiley   +1 more source

The crystal structure of the globular domain of sheep prion protein [PDF]

, 2004
The prion protein PrP is a naturally occurring polypeptide that becomes transformed from a normal conformation to that of an aggregated form, characteristic of pathological states in fatal transmissible spongiform conditions such as Creutzfeld–Jacob ...
Vasisht N, Whyte, SM, Dodson EJ, Vasisht, N, Gill, A.C., Whyte, S.M., Dodson, G.G., Whyte, S M, Vasisht, N., Bayley, P M, Verma, C., Verma C, Gill, A C, Bayley, PM, Bayley, P.M., Whyte SM, Haire LF, Gill AC, Gill, AC, Bayley PM, Dodson, EJ, Haire, L.F., Dodson, GG, Dodson, E.J., Haire, L F, Verma, C, Haire, LF, Dodson, E J, Dodson, G G   +28 more
core   +1 more source

Thermodynamic Stabilization of the Folded Domain of Prion Protein Inhibits Prion Infection in Vivo

Cell Reports, 2013
Prion diseases, or transmissible spongiform encephalopathies (TSEs), are associated with the conformational conversion of the cellular prion protein, PrPC, into a protease-resistant form, PrPSc.
Qingzhong Kong, Jeffrey L. Mills, Bishwajit Kundu, Xinyi Li, Liuting Qing, Krystyna Surewicz, Ignazio Cali, Shenghai Huang, Mengjie Zheng, Wieslaw Swietnicki, Frank D. Sönnichsen, Pierluigi Gambetti, Witold K. Surewicz   +12 more
doaj   +1 more source

Treatment with KCL‐286, a first‐in‐class retinoic acid receptor‐β (RARβ) agonist, ameliorates neuronal DNA damage and inflammation in a mouse model of Alzheimer's disease

FEBS Open Bio, EarlyView.
Repair of neuronal DNA damage in Alzheimer's disease by KCL‐286. (A) Amyloid‐β oligomers and plaques impair neuronal DNA repair pathways, leading to DNA double‐strand breaks and glial activation. (B) KCL‐286 activates RARβ/RXR signalling via retinoic acid response elements (RAREs), associated with increased BRCA1 expression, enhanced DNA repair and ...
Natasha Hill, Hassan Yousef Othman AlMuallim, Elouisa Maddock, Carl Hobbs, Earl Clarke, Maria B. Goncalves, Jonathan P. T. Corcoran   +6 more
wiley   +1 more source

Synthesis and anti-prion aggregation activity of acylthiosemicarbazide analogues

Journal of Enzyme Inhibition and Medicinal Chemistry, 2023
Prions are infectious protein particles known to cause prion diseases. The biochemical entity of the pathogen is the misfolded prion protein (PrPSc) that forms insoluble amyloids to impair brain function. PrPSc interacts with the non-pathogenic, cellular
Dong Hwan Kim, Jaehyeon Kim, Hakmin Lee, Dongyun Lee, So Myoung Im, Ye Eun Kim, Miryeong Yoo, Yong-Pil Cheon, Jason C. Bartz, Young-Jin Son, Eun-Kyoung Choi, Yong-Sun Kim, Jae-Ho Jeon, Hyo Shin Kim, Sungeun Lee, Chongsuk Ryou, Tae-gyu Nam   +16 more
doaj   +1 more source

Adenosine triphosphate as a modulator of protein interactions and stability

FEBS Open Bio, EarlyView.
ATP is best known as the cell's energy currency, but it also shapes how proteins fold, interact, aggregate and form biomolecular condensates. This review explains the emerging physical principles behind these effects, including weak binding to charged protein regions, magnesium‐dependent behaviour and concentration‐dependent control of protein ...
Shuyuan Tan, Robin Curtis
wiley   +1 more source

Pros and cons of a prion-like pathogenesis in Parkinson's disease [PDF]

, 2011
Background: Parkinson's disease (PD) is a slowly progressive neurodegenerative disorder which affects widespread areas of the brainstem, basal ganglia and cerebral cortex.
Chapman Joab, Hilker, Ruediger, Brotchie, Jonathan M, Hilker, Rüdiger, Hilker Ruediger, Brotchie, Jonathan M., Joab Chapman, Ruediger Hilker, Chapman, Joab, Jonathan M Brotchie, Brotchie Jonathan M   +10 more
core   +2 more sources

A Sequence-Dependent DNA Condensation Induced by Prion Protein

Journal of Nucleic Acids, 2018
Different studies indicated that the prion protein induces hybridization of complementary DNA strands. Cell culture studies showed that the scrapie isoform of prion protein remained bound with the chromosome. In present work, we used an oxazole dye, YOYO,
Alakesh Bera, Sajal Biring
doaj   +1 more source