Results 91 to 100 of about 3,400,014 (272)

A Unifying Thermodynamic Model for Phase Separation and Aging of Biopolymers

Advanced Science, EarlyView.
Phase separation and aging of intrinsically disordered proteins are placed in a unifying framework. A thermodynamically consistent time‐dependent version of associating‐polymer theory shows how the processes are intricately coupled. Assuming aging to occur through interacting sites resulting from reversible conformational transitions, the model ...
Jasper J. Michels, Joana Caria, Edward A. Lemke   +2 more
wiley   +1 more source

Gene expression profiling en association with prion-related lesions in the medulla oblongata of symptomatic natural scrapie animals. [PDF]

, 2011
The pathogenesis of natural scrapie and other prion diseases remains unclear. Examining transcriptome variations in infected versus control animals may highlight new genes potentially involved in some of the molecular mechanisms of prion-induced ...
Bossers, A., Rosa Bolea, Hicham Filali, Varona, L., Filalil, Hicham, Harders, F., Inmaculada Martin-Burriel, Alex Bossers, Zaragoza, P., Badiola, J.J., Juan J. Badiola, Bossers, Alex, Pumarola i Batlle, Martí, Lyahyai, Jaber, Lyahyai, J., Martín Burriel, Inmaculada, Pilar Zaragoza, Juan J Badiola, Bolea, Rosa, Filali, H., Bolea, R., Acín, Cristina, Luis Varona, Frank Harders, Filali, Hicham, Pumarola, M., Harders, Frank, Zaragoza, Pilar, Badiola, Juan J, Varona, Luis, Martí Pumarola, Jaber Lyahyai, Martin-Burriel, I., Badiola, Juan José, Pumarola, Martí   +34 more
core   +2 more sources

To develop with or without the prion protein [PDF]

Frontiers in Cell and Developmental Biology, 2014
The deletion of the cellular form of the prion protein (PrP(C)) in mouse, goat, and cattle has no drastic phenotypic consequence. This stands in apparent contradiction with PrP(C) quasi-ubiquitous expression and conserved primary and tertiary structures in mammals, and its pivotal role in neurodegenerative diseases such as prion and Alzheimer's ...
Sophie eHalliez, Bruno ePasset, Séverine eMartin-Lannerée, Séverine eMartin-Lannerée, Julia eHernandez-Rapp, Julia eHernandez-Rapp, Hubert eLaude, Sophie eMouillet-Richard, Sophie eMouillet-Richard, Jean-Luc eVilotte, Vincent eBéringue   +10 more
openaire   +5 more sources

Differential interactome mapping of aggregation prone/prion-like proteins under stress: novel links to stress granule biology

Cell & Bioscience, 2023
Background Aberrant stress granules (SGs) are emerging as prime suspects in the nucleation of toxic protein aggregates. Understanding the molecular networks linked with aggregation-prone proteins (prion protein, synuclein, and tau) under stressful ...
Neelam Younas, Saima Zafar, Tayyaba Saleem, Leticia Camila Fernandez Flores, Abrar Younas, Matthias Schmitz, Inga Zerr   +6 more
doaj   +1 more source

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

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

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

Cystatin F is a biomarker of prion pathogenesis in mice.

PLoS ONE, 2017
Misfolding of the cellular prion protein (PrPC) into the scrapie prion protein (PrPSc) results in progressive, fatal, transmissible neurodegenerative conditions termed prion diseases.
Mario Nuvolone, Nicolas Schmid, Gino Miele, Silvia Sorce, Rita Moos, Christian Schori, Roger R Beerli, Monika Bauer, Philippe Saudan, Klaus Dietmeier, Ingolf Lachmann, Michael Linnebank, Roland Martin, Ulf Kallweit, Veronika Kana, Elisabeth J Rushing, Herbert Budka, Adriano Aguzzi   +17 more
doaj   +1 more source

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 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
McKinnon, C, Tabrizi, SJ, Goold, R
core