Results 91 to 100 of about 1,598,142 (264)

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

RSF1‐Dependent PAR Turnover Promotes 53BP1 Liquid Condensate Formation at DNA Damage Sites

Advanced Science, EarlyView.
At sites of DNA damage, RSF1 recruits PARG to accelerate PAR turnover, triggering a switch from PAR‐driven condensates to 53BP1 condensates. This condensate transition enables p53‐dependent gene transcription and coordinates the DNA damage response.
Yungyeong Heo, Yonghyeon Kim, Nangyeong Hwang, Gwanho Sung, Sujin Jo, Yeonhu Lee, Ho‐Chul Kang, Jae‐Ho Lee, Yong Won Choi, Hyeseong Cho, Sunwoo Min   +10 more
wiley   +1 more source

Prion Protein Amyloidosis

Brain Pathology, 1996
The prion protein (PrP) plays an essential role in the pathogenesis of a group of sporadic, genetically determined and infectious fatal degenerative diseases, referred to as “prion diseases”, affecting the central nervous system of humans and other mammals. The cellular PrP is encoded by a single copy gene, highly conserved across mammalian species. In
B, Ghetti, P, Piccardo, B, Frangione, O, Bugiani, G, Giaccone, K, Young, F, Prelli, M R, Farlow, S R, Dlouhy, F, Tagliavini   +9 more
openaire   +2 more sources

Prion Protein in Glioblastoma Multiforme [PDF]

International Journal of Molecular Sciences, 2019
The cellular prion protein (PrPc) is an evolutionarily conserved cell surface protein encoded by the PRNP gene. PrPc is ubiquitously expressed within nearly all mammalian cells, though most abundantly within the CNS. Besides being implicated in the pathogenesis and transmission of prion diseases, recent studies have demonstrated that PrPc contributes ...
Larisa Ryskalin, Carla L. Busceti, Francesca Biagioni, Fiona Limanaqi, Pietro Familiari, Alessandro Frati, Francesco Fornai   +6 more
openaire   +2 more sources

Tau Aggregate Imaging and Transcriptomics of Alzheimer's Disease Brain at Different Stages of Disease

Advanced Science, EarlyView.
The protein aggregates and gene expression in the middle temporal gyrus (MTG) and somatosensory cortex (SOM) of the postmortem brains of 13 Alzheimer's disease patients were studied in detail, revealing that small hyperphosphorylated tau aggregates increase with Braak stage driven by microglial inflammation.
Elizabeth A. English, Dorothea Böken, Matthew W. Cotton, Matthew R. Cheetham, Johanna S. Jackson, Georg Meisl, John S. H. Danial, Paul M. Matthews, Nurun N. Fancy, David Klenerman   +9 more
wiley   +1 more source

Prion‐Like Protein LENG8‐Mediated Nucleation Drives Stress Granule Assembly

Advanced Science, EarlyView.
LENG8 is a newly identified stress granule (SG) nucleator required for SG assembly. Following stress, nuclear LENG8 granules disassemble, allowing LENG8 to translocate into the cytoplasm and form independent nucleation foci. These foci fuse with canonical early G3BP1/TIA1 seeds via LENG8‐TIA1 binding to drive SG maturation.
Mingxing Zhang, Xin Wang, Yilan Teng, Zhicheng Wu, Jing Fan, Hongwen Zhu, Peng Dai   +6 more
wiley   +1 more source

Different isoforms of the non-integrin laminin receptor are present in mouse brain and bind PrP [PDF]

, 2003
The prion protein (PrP) plays a central role in prion diseases, and identifying its cellular receptor appears to be of crucial interest. We previously showed in the yeast twohybrid system that PrP interacts with the 37 kDa precursor (LRP) of the high ...
S. Weiss, J.-P. Deslys, Weiss, S., D. Dormont, Simoneau, S., S. Simoneau, Deslys, J.-P., Lasmézas, C., S. Haïk, C. Leucht, Haik, S., Leucht, C., Dormont, D., C. Lasmézas   +13 more
core   +3 more sources

The Yeast Prion [SWI+] Abolishes Multicellular Growth by Triggering Conformational Changes of Multiple Regulators Required for Flocculin Gene Expression

Cell Reports, 2015
Although transcription factors are prevalent among yeast prion proteins, the role of prion-mediated transcriptional regulation remains elusive. Here, we show that the yeast prion [SWI+] abolishes flocculin (FLO) gene expression and results in a complete ...
Zhiqiang Du, Ying Zhang, Liming Li
doaj   +1 more source

Neurotransmitter‐Defined Degeneration Patterns in Sporadic and C9orf72‐Associated Amyotrophic Lateral Sclerosis: Predilection to GABAergic, Serotonergic, Opioid, Glutamatergic, Endocannabinoid, and Microglial Systems—Implications for Therapy Development

Annals of Neurology, EarlyView.
Objective Amyotrophic lateral sclerosis (ALS) has a markedly distinctive clinical and neuroradiological signature, with the preferential involvement of specific brain networks and the apparent sparing of others. The molecular underpinnings of the strikingly selective anatomical vulnerability have not been fully elucidated to date despite the potential ...
Marlene Tahedl, We Fong Siah, Jasmin Lope, Jennifer C. Hengeveld, Mark A. Doherty, Russell L. McLaughlin, Orla Hardiman, Ee Ling Tan, Alison Toomey, Jana Kleinerova, Peter Bede   +10 more
wiley   +1 more source

Characterization of the prion protein in relation to normal cellular function and in disease [PDF]

, 2012
Transmissible spongiform encephalopathies (TSEs), also known as prion diseases, are a group of rare and fatal neurodegenerative disorders that can affect both human and animals.
Wik, Lotta
core   +1 more source