Results 71 to 80 of about 5,604,422 (355)

Autophagy in cancer and protein conformational disorders

FEBS Letters, EarlyView.
Autophagy plays a crucial role in numerous biological processes, including protein and organelle quality control, development, immunity, and metabolism. Hence, dysregulation or mutations in autophagy‐related genes have been implicated in a wide range of human diseases.
Sergio Attanasio
wiley   +1 more source

Prion-Like Proteins in Phase Separation and Their Link to Disease

Biomolecules, 2021
Aberrant protein folding underpins many neurodegenerative diseases as well as certain myopathies and cancers. Protein misfolding can be driven by the presence of distinctive prion and prion-like regions within certain proteins. These prion and prion-like
Macy L. Sprunger, Meredith E. Jackrel
doaj   +1 more source

Pathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding [PDF]

, 2010
Transmissible spongiform encephalopathies, or prion diseases, are caused by misfolding and aggregation of the prion protein PrP. These diseases can be hereditary in humans and four of the many disease-associated missense mutants of PrP are in the ...
Daggett, Valerie, van der Kamp, Marc W
core   +1 more source

Neuronal death induced by misfolded prion protein is due to NAD+ depletion and can be relieved in vitro and in vivo by NAD+ replenishment.

Brain : a journal of neurology, 2015
The mechanisms of neuronal death in protein misfolding neurodegenerative diseases such as Alzheimer's, Parkinson's and prion diseases are poorly understood.
Minghai Zhou, Gregory K. Ottenberg, G. F. Sferrazza, Christopher Hubbs, M. Fallahi, Gavin Rumbaugh, A. F. Brantley, C. Lasmézas   +7 more
semanticscholar   +1 more source

Purification tags markedly affect self‐aggregation of CPEB3

FEBS Letters, EarlyView.
Although recombinant proteins are used to study protein aggregation in vitro, uncleaved tags can interfere with accurate interpretation. Our findings demonstrate that His₆‐GFP and His₁₂ tags significantly affect liquid droplet and amyloid fibril formation in the intrinsically disordered region (IDR) of mouse cytoplasmic polyadenylation element‐binding ...
Harunobu Saito, Yujin Lee, Motoharu Ueno, Naotaka Sekiyama, Masatomo So, Ayako Furukawa, Kenji Sugase   +6 more
wiley   +1 more source

Use of bovine recombinant prion protein and real-time quaking-induced conversion to detect cattle transmissible mink encephalopathy prions and discriminate classical and atypical L- and H-Type bovine spongiform encephalopathy. [PDF]

PLoS ONE, 2017
Prions are amyloid-forming proteins that cause transmissible spongiform encephalopathies through a process involving conversion from the normal cellular prion protein to the pathogenic misfolded conformation (PrPSc).
Soyoun Hwang, Justin J Greenlee, Eric M Nicholson   +2 more
doaj   +1 more source

Evolutionary descent of prion genes from a ZIP metal ion transport ancestor [PDF]

, 2009
In the more than 20 years since its discovery, both the phylogenetic origin and cellular function of the prion protein (PrP) have remained enigmatic.
David Westaway, Gerold Schmitt-Ulms, Holger Wille, Joel C. Watts, Sepehr Ehsani   +4 more
core   +1 more source

Molecular dynamics studies on the NMR and X-ray structures of rabbit prion protein wild-type and mutants

, 2013
Prion diseases are invariably fatal and highly infectious neurodegenerative diseases that affect a wide variety of mammalian species such as sheep, goats, mice, humans, chimpanzees, hamsters, cattle, elks, deer, minks, cats, chicken, pigs, turtles, etc ...
Barlow, Baron, Barry, Barry, Barry, Bastian, Bencsik, Bendheim, Bett, Biswas, Bitel, Bjorndahl, Bockman, Bode, Brun, Caughey, Chianini, Cho, Chou, Chou, Chou, Chou, Chou, Chou, Chou, Christen, Christen, Christen, Christen, Cong, Courageot, Damberger, Di Martino, Dong, Dupiereux, Farquhar, Fernandez-Funez, Fernandez-Funez, Fernandez-Funez, Fernández-Borges, Friedman-Levi, Gabizon, Gabizon, Gao, Garrec, Garssen, Gerber, Gilch, Golanska, Gossert, Groschup, Groschup, Groschup, Guiroy, Handisurya, Hanoux, Hashimoto, Hay, Huang, Ikegami, Ishiguro, Ishikawa, Jackman, Jiapu Zhang, Julien, Kabsch, Kascsak, Kascsak, Kelker, Khan, Kim, Kirby, Kirkwood, Kitamoto, Kocisko, Komar, Korth, Laude, Lawson, Li, Li, Loftus, Lopez, Lührs, Ma, Madec, Mays, Meli, Merz, Miller, Nisbet, Oboznaya, Onodera, Polymenidou, Pérez, Riek, Robakis, Roberts, Rossetti, Sachsamanoglou, Sakudo, Schmerr, Senator, Shin, Shinagawa, Sigurdson, Sigurdson, Sigurdson, Stanker, Sweeting, Takahashi, Takahashi, Takekida, Tang, Timmes, Vidal, Vilette, Vol'pina, Vorberg, Wade, Wang, Wen, Wen, Wiley, Xi, Xiao, Yokoyama, Yokoyama, Yost, Yuanli Zhang, Zahn, Zhang, Zhang, Zhang, Zhang, Zhang, Zhao, Zhou, Zhou, Zhou, Zhou, Zhou, Zocche Soprana   +142 more
core   +1 more source

Prion degradation pathways: Potential for therapeutic intervention [PDF]

, 2015
Prion diseases are fatal neurodegenerative disorders. Pathology is closely linked to the misfolding of native cellular PrP(C) into the disease-associated form PrP(Sc) that accumulates in the brain as disease progresses. Although treatments have yet to be
Goold, R, McKinnon, C, Tabrizi, SJ
core   +1 more source

Glycosylation and prion protein

Current Opinion in Structural Biology, 2002
Recent advances have elucidated the detailed glycosylation of the prion protein and highlighted the size of the sugars, which shield large areas of the protein and confer some conformational stability on the normal cellular form. The reliability of SDS-PAGE banding patterns of different "glycoforms" as a diagnostics tool has been discussed.
Rudd, P, Merry, A, Wormald, M, Dwek, R
openaire   +3 more sources