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Articles by Sofia Bali
The Milk I Was Forced to Drink: How I Learned to Stop Seeking Men’s Approval
The Milk I Was Forced to Drink: How I Learned to Stop Seeking Men’s Approval How a childhood glass of milk became a symbol of obedience, patriarchy, and the journey back to myself. Press enter or click to view image in full size Photo by Eiliv Aceron on Unsplash I hate milk. It’s a strange thing to say because milk is supposed to represent comfort, nourishment, childhood, and care. It’s supposed to be the drink that makes children grow strong.
NLRP3 haploinsufficiency unmasks a compensatory NLRP1-NLRP3 interaction that drives accelerated aging in mice
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Abstract INTRODUCTION RESULTS DISCUSSION MATERIALS AND METHODS Acknowledgments Supplementary Materials REFERENCES Information & Authors Metrics & Citations View Options References Figures Tables Media Share Abstract The NLRP3 inflammasome has been implicated in a wide range of human diseases, including cardiovascular, metabolic, neurodegenerative (such as Alzheimer’s disease), and other age-related conditions. This has positioned NLRP3 as a promising pharmacological target.
By Pascal J. Schmidt, Neha Chetlangia, Pin-Kuan Chiang, Ines Muela-Zarzuela, Elísabet Alcocer-Gómez, Juan M. Suarez-Rivero, Evon Low, Abbas Ishaq, Mikel Azkargorta, Amparo Luque-Sierra, Franz Martín, Felix Elortza, Antonio Astorga-Gamaza, Rosa Anton, Sofia Bali, Joaquín Tamargo-Azpilicueta, Alejandra Guerra-Castellano, Irene Díaz-Moreno, Lukasz A. Joachimiak, Javier Oroz, Jesús Ruiz-Cabello, Thomas von Zglinicki, Alberto Sanz Verified, Mario D. Cordero
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Science Magazine
Verified
Select azo compounds post-translationally modulate HTRA1 abundance and activity potentially through interactions at the trimer interface
Abstract High-temperature requirement protein A1 (HTRA1) is a secreted serine protease with diverse substrates, including extracellular matrix proteins, proteins involved in amyloid deposition, and growth factors. Accordingly, HTRA1 has been implicated in a variety of neurodegenerative diseases including a leading cause of blindness in the elderly, age-related macular degeneration (AMD).
Amyloid-motif-dependent tau self-assembly is modulated by isoform sequence context
Abstract The microtubule-associated protein tau is implicated in neurodegenerative diseases characterized by amyloid formation. Mutations associated with frontotemporal dementia increase tau aggregation propensity and disrupt its endogenous microtubule-binding activity. However, the structural relationship between aggregation propensity and biological activity remains unclear.
Yin Yang 1 and guanine quadruplexes protect dopaminergic neurons from cellular stress via transmissive dormancy - Nature Communications
Abstract Neurons deploy diverse adaptive strategies to ensure survival and neurotransmission amid cellular stress. When these adaptive pathways are overwhelmed, functional impairment or neurodegeneration follows. Here we show that stressed neurons actively induce a state of transmissive dormancy as a protective measure. Extending observations of neurotrauma in C.
Hairpin trimer transition state of amyloid fibril - Nature Communications
Abstract Protein fibril self-assembly is a universal transition implicated in neurodegenerative diseases. Although fibril structure/growth are well characterized, fibril nucleation is poorly understood. Here, we use a computational-experimental approach to resolve fibril nucleation. We show that monomer hairpin content quantified from molecular dynamics simulations is predictive of experimental fibril formation kinetics across a tau motif mutant library.
Ensemble-based design of tau to inhibit aggregation while preserving biological activity.
Abstract The microtubule-associated protein tau is implicated in neurodegenerative diseases characterized by amyloid formation. Mutations associated with frontotemporal dementia increase tau aggregation propensity and disrupt its endogenous microtubule-binding activity. The structural relationship between aggregation propensity and biological activity remains unclear.
FTD-tau S320F mutation stabilizes local structure and allosterically promotes amyloid motif-dependent aggregation - Nature Communications
Abstract Amyloid deposition of the microtubule-associated protein tau is associated with neurodegenerative diseases. In frontotemporal dementia with abnormal tau (FTD-tau), missense mutations in tau enhance its aggregation propensity. Here we describe the structural mechanism for how an FTD-tau S320F mutation drives spontaneous aggregation, integrating data from in vitro, in silico and cellular experiments.
Aβ under stress: the effects of acidosis, Cu2+-binding, and oxidation on amyloid β-peptide dimers
In light of the high affinity of Cu for Alzheimer’s Aβ and its ability to subsequently catalyze the formation of radicals, we examine the effects of Cu binding, Aβ oxidation, and an acidic environment on the conformational dynamics of the smallest Aβ oligomer, the Aβ dimer.
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