Results 21 to 30 of about 57,121 (194)

Recombinant Mammalian Prions: The “Correctly” Misfolded Prion Protein Conformers

Viruses, 2022
Generating a prion with exogenously produced recombinant prion protein is widely accepted as the ultimate proof of the prion hypothesis. Over the years, a plethora of misfolded recPrP conformers have been generated, but despite their seeding capability ...
Jiyan Ma, Jingjing Zhang, Runchuan Yan
doaj   +1 more source

A Cell- and Tissue-Specific Weakness of the Protein Homeostasis System Underlies Brain Vulnerability to Protein Aggregation

iScience, 2020
Summary: The phenomenon of protein misfolding and aggregation is associated with a wide range of neurodegenerative conditions that cause progressive loss of function in specific regions of the human brain.
Rishika Kundra, Christopher M. Dobson, Michele Vendruscolo   +2 more
doaj   +1 more source

Cell Non-autonomous Proteostasis Regulation in Aging and Disease

Frontiers in Neuroscience, 2022
Aging is a risk factor for a number of diseases, being the more notorious ones perhaps neurodegenerative diseases such as Alzheimer’s and Parkinson’s. These and other age-related pathologies are often associated with accumulation of proteotoxic material ...
Joao Vasco Ferreira, Ana da Rosa Soares, Paulo Pereira   +2 more
doaj   +1 more source

A role for eIF5A in translational control of stress‐inducible proteins in multiple myeloma cell lines

Molecular Oncology, EarlyView.
Loss of eIF5A rewires thapsigargin‐mediated endoplasmic reticulum stress responses in multiple myeloma cells by selective translation of mRNA transcripts, consequently dampening thapsigargin‐induced unfolded protein response (UPR) activation and shifting the balance from induction of apoptosis toward cell survival and proliferation.
Demi Both, Ingrid A. M. Derks, Raphaël Vanleyssem, Marine Leclercq, Najla El Hachem, Pierre Close, Eric Eldering, Marco Vincent Haselager   +7 more
wiley   +1 more source

Pharmacological inhibition of α-synuclein aggregation within liquid condensates

Nature Communications
Aggregated forms of α-synuclein constitute the major component of Lewy bodies, the proteinaceous aggregates characteristic of Parkinson’s disease. Emerging evidence suggests that α-synuclein aggregation may occur within liquid condensates formed through ...
Samuel T. Dada, Zenon Toprakcioglu, Mariana P. Cali, Alexander Röntgen, Maarten C. Hardenberg, Owen M. Morris, Lena K. Mrugalla, Tuomas P. J. Knowles, Michele Vendruscolo   +8 more
doaj   +1 more source

Co-Chaperones in Targeting and Delivery of Misfolded Proteins to the 26S Proteasome

Biomolecules, 2020
Protein homeostasis (proteostasis) is essential for the cell and is maintained by a highly conserved protein quality control (PQC) system, which triages newly synthesized, mislocalized and misfolded proteins.
Amanda B. Abildgaard, Sarah K. Gersing, Sven Larsen-Ledet, Sofie V. Nielsen, Amelie Stein, Kresten Lindorff-Larsen, Rasmus Hartmann-Petersen   +6 more
doaj   +1 more source

Comparative Studies in the A30P and A53T α-Synuclein C. elegans Strains to Investigate the Molecular Origins of Parkinson's Disease

Frontiers in Cell and Developmental Biology, 2021
The aggregation of α-synuclein is a hallmark of Parkinson's disease (PD) and a variety of related neurological disorders. A number of mutations in this protein, including A30P and A53T, are associated with familial forms of the disease. Patients carrying
Michele Perni, Annemieke van der Goot, Ryan Limbocker, Ryan Limbocker, Tjakko J. van Ham, Francesco A. Aprile, Catherine K. Xu, Patrick Flagmeier, Karen Thijssen, Pietro Sormanni, Giuliana Fusco, Serene W. Chen, Pavan K. Challa, Julius B. Kirkegaard, Romain F. Laine, Kai Yu Ma, Kai Yu Ma, Martin B. D. Müller, Martin B. D. Müller, Tessa Sinnige, Janet R. Kumita, Samuel I. A. Cohen, Renée Seinstra, Gabriele S. Kaminski Schierle, Clemens F. Kaminski, Denise Barbut, Alfonso De Simone, Tuomas P. J. Knowles, Michael Zasloff, Ellen A. A. Nollen, Michele Vendruscolo, Christopher M. Dobson   +31 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

Chronobiology of Cancer: How Aging Fuels Oncogenesis at the Molecular Level

Aging and Cancer, EarlyView.
This graphical abstract illustrates the key biological pathways linking aging with cancer development and progression. In the upper left, cumulative exposure to ultraviolet radiation, toxins, and reactive oxygen species (ROS) causes DNA damage and genomic instability, whereas age‐related decline in repair mechanisms, such as ATM/ATR, BER, and NER ...
Anu Singh, Aroonima Misra, Sufian Zaheer
wiley   +1 more source

Mitochondrial stress in advanced fibrosis and cirrhosis associated with chronic hepatitis B, chronic hepatitis C, or nonalcoholic steatohepatitis

Hepatology, EarlyView., 2022
Adaptive mitochondrial mechanisms allow mitochondrial resilience and prevent the worsening of fibrosis, while deregulation of these mechanisms promotes the progression from no/minimal‐mild (F0‐F2) fibrosis to advanced fibrosis and cirrhosis (F3‐F4). Abstract Background and Aims Hepatitis B virus (HBV) infection causes oxidative stress (OS) and alters ...
Dimitri Loureiro, Issam Tout, Stéphanie Narguet, Cheikh Mohamed Bed, Morgane Roinard, Ahmad Sleiman, Nathalie Boyer, Nathalie Pons‐Kerjean, Corinne Castelnau, Nathalie Giuly, Dorothy Tonui, Vassili Soumelis, Jamel El Benna, Patrick Soussan, Richard Moreau, Valérie Paradis, Abdellah Mansouri, Tarik Asselah   +17 more
wiley   +1 more source