Results 71 to 80 of about 3,689,678 (299)

Transmission electron microscopy characterization of fluorescently labelled amyloid β 1-40 and α-synuclein aggregates

open access: yesBMC Biotechnology, 2011
Background Fluorescent tags, including small organic molecules and fluorescent proteins, enable the localization of protein molecules in biomedical research experiments.
Anderson Valerie L, Webb Watt W
doaj   +1 more source

Going viral − Virus‐targeting nanobodies for research, diagnostics and therapy

open access: yesFEBS Letters, EarlyView.
The increasing prevalence of viral diseases represents a major threat for global human health. Nanobodies, small binding fragments derived from camelid heavy‐chain antibodies, offer versatile tools for viral research, diagnostics, and antiviral therapy.
Domenic Ebert, Ulrich Rothbauer
wiley   +1 more source

Deposition of amyloid fibrils promotes cell-surface accumulation of amyloid β precursor protein

open access: yesNeurobiology of Disease, 2004
Amyloid β protein (Aβ) deposition and neuronal degeneration are characteristic pathological features of Alzheimer's disease (AD). In vitro, Aβ fibrils (fAβ) induce neuronal degeneration reminiscent to AD, but the mechanism of neurotoxicity is unknown ...
Lorena Heredia   +5 more
doaj   +1 more source

Developmental programmes drive cellular plasticity, disease progression and therapy resistance in lung adenocarcinoma

open access: yesMolecular Oncology, EarlyView.
This study shows that lung adenocarcinomas exploit developmental branching morphogenesis to acquire a therapy resistant basal‐like tumour cell state. This process was found to be regulated by combined TP53 loss‐of‐function and type‐I interferon signalling, identifying a novel axis for biomarker and therapeutic target discovery.
Kamila J Bienkowska   +13 more
wiley   +1 more source

The Kinetics of Amyloid Fibril Formation by de Novo Protein Albebetin and Its Mutant Variants

open access: yesBiomolecules, 2020
Engineering of amyloid structures is one of the new perspective areas of protein engineering. Studying the process of amyloid formation can help find ways to manage it in the interests of medicine and biotechnology.
Vitalii Balobanov   +5 more
doaj   +1 more source

Co-factor-free aggregation of tau into seeding-competent RNA-sequestering amyloid fibrils

open access: yesNature Communications, 2021
The authors present a method for the conversion of full-length tau protein into seeding-competent amyloid fibrils without heparin or other negatively charged co-factors, which could be useful for studying the effects of post-translational modifications ...
Pijush Chakraborty   +8 more
doaj   +1 more source

Finding novel vulnerabilities of hypomorphic BRCA1 alleles

open access: yesMolecular Oncology, EarlyView.
Synthetic lethality screens performed to identify novel vulnerabilities often model complete gene loss, thereby overlooking patient‐derived hypomorphic mutations. In this study, we have performed genome‐wide CRISPR screens on BRCA1 hypomorphic mutations, showing BRCA1I26A behaves like wild‐type, while BRCA1R1699Q mimics deficiency. Furthermore, we have
Anne Schreuder   +10 more
wiley   +1 more source

Overview of engineering and functionalizing cross-β fibrils from β-solenoid protein monomers.

open access: yes, 2020
Fibrils formed from the engineered protein are micrometers long. These fibrils were readily conjugated to 5 nm gold nanoparticles to give densely modified structures.
Maria D. R. Peralta (4568749)   +3 more
core   +1 more source

The VHL tumor suppressor at the crossroad of protein folding, aggregation, and cancer

open access: yesMolecular Oncology, EarlyView.
Mutations, environmental stress, and chaperone dysfunction can destabilize pVHL, promoting its conversion from the native folded state into amyloid‐like assemblies. This transition may contribute to protein storage, cell dormancy, survival, and drug resistance.
Lara Abad   +2 more
wiley   +1 more source

Arginine π-stacking drives binding to fibrils of the Alzheimer protein Tau

open access: yes, 2020
Aggregation of the Tau protein into fibrils defines progression of neurodegenerative diseases, including Alzheimer's Disease. The molecular basis for potentially toxic reactions of Tau aggregates is poorly understood.
Ferrari, Luca   +18 more
core  

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