Results 71 to 80 of about 56,657 (298)

Cytosolic Prion Protein Toxicity Is Independent of Cellular Prion Protein Expression and Prion Propagation [PDF]

Journal of Virology, 2007
ABSTRACT Prion diseases are transmissible neurodegenerative diseases caused by a conformational isoform of the prion protein (PrP), a host-encoded cell surface sialoglycoprotein. Recent evidence suggests a cytosolic fraction of PrP (cyPrP) functions either as an initiating factor or toxic element of prion disease.
Eric M, Norstrom, Mark F, Ciaccio, Benjamin, Rassbach, Robert, Wollmann, James A, Mastrianni   +4 more
openaire   +2 more sources

Developing a Functional Polyelectrolyte Hybrid Layer Scaffold Coating and Evaluation of Its Performance for Interaction With Neural Cells

Advanced Materials Interfaces, EarlyView.
Polyelectrolyte scaffold coatings modified with Cu and Fe3O4 nanoparticles regulate neural stem cell behavior in vitro. Increased Fe3O4 content enhances mitochondrial activity and neuronal differentiation, whereas higher Cu levels reduce cell viability.
Anna Grzeczkowicz, Agata Lipko, Angelika Kwiatkowska, Marcin Strawski, Monika Drabik, Ludomira H. Granicka   +5 more
wiley   +1 more source

Unique Properties of the Rabbit Prion Protein Oligomer. [PDF]

PLoS ONE, 2016
Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are a group of fatal neurodegenerative disorders infecting both humans and animals.
Ziyao Yu, Pei Huang, Yuanhui Yu, Zhen Zheng, Zicheng Huang, Chenyun Guo, Donghai Lin   +6 more
doaj   +1 more source

Ecological Adaptation Mechanisms Underlying Successful Plant Reproduction

Advanced Science, EarlyView.
During floral induction, various environmental and endogenous signals converge to regulate the florigen protein, which is transported from leaves to the SAM to initiate flowering. Within the SAM, a complex network of receptor kinases and small peptides orchestrates floral development with high spatiotemporal precision.
Hang Zhao, Shenghui Huo, Yue Xing, Shuxin Zhang, Guilin Li, Yihui Liu, Chongyang Jin, Fuguang Li, Xiaoyang Ge   +8 more
wiley   +1 more source

The Molecular Pathology of Prion Diseases [PDF]

, 2004
Prion diseases, or transmissible spongiform encephalopathies (TSEs), are a group of invariably fatal neurodegenerative disorders. Uniquely, they may present as sporadic, inherited, or infectious forms, all of which involve conversion of the normal ...
Vassallo, Neville, Herms, Jochen, Kretzschmar, Hans A.   +2 more
core  

The crystal structure of the globular domain of sheep prion protein

, 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

Redox‐Dependent Chaperoning of GBF1 Condensates Regulates Seed Germination in Arabidopsis

Advanced Science, EarlyView.
In dormant seeds (low ROS), GBF1 forms liquid condensates to repress the germination gene CathB3, and the chaperone GIP1 maintains condensate liquidity and repressive activity. Upon imbibition (high ROS), ROS oxidize GIP1 during germination, impairing its chaperone function.
Yunying Wang, Xiaofeng Fang
wiley   +1 more source

Astrocyte in prion disease: a double-edged sword

Neural Regeneration Research, 2022
Prion diseases are infectious protein misfolding disorders of the central nervous system that result from misfolding of the cellular prion protein (PrPC) into the pathologic isoform PrPSc.
Waqas Tahir, Simrika Thapa, Hermann M Schatzl   +2 more
doaj   +1 more source

The protean prion protein

PLOS Biology, 2020
The prion protein, PrP, can adopt at least 2 conformations, the overwhelmingly prevalent cellular conformation (PrPC) and the scrapie conformation (PrPSc). PrPC features a globular C-terminal domain containing 3 α-helices and a short β-sheet and a long flexible N-terminal tail whose exact conformation in vivo is not yet known and a metastable subdomain
openaire   +4 more sources