Results 131 to 140 of about 16,667 (258)

A Tale of Two Dimers: GFP Proteins under Macromolecular Crowding Studied by Small Angle Neutron Scattering [PDF]

open access: bronze, 2012
Shuo Qian   +4 more
openalex   +1 more source

Human cells for human proteins: Isotope labeling in mammalian cells in suspension for functional NMR studies

open access: yesProtein Science, Volume 35, Issue 4, April 2026.
Abstract In biological and biomedical research, the focus progressively moves towards difficult human proteins, which often can only be expressed in higher eukaryotic cells. Nuclear magnetic resonance (NMR) could contribute significantly to the understanding of important proteins as it is one of the most information‐rich methods.
Philip Rößler   +11 more
wiley   +1 more source

Toxic mechanisms of amyloid oligomers and therapeutic strategies

open access: yesProtein Science, Volume 35, Issue 4, April 2026.
Abstract Amyloid oligomers are increasingly recognized as the major toxic contributors across protein‐misfolding disorders. In this review, we cover mechanistic evidence showing how these transient and structurally heterogeneous oligomers disrupt cellular homeostasis by: (i) permeabilizing lipid membranes and forming ion‐conducting pores; (ii ...
Magdalena I. Ivanova   +2 more
wiley   +1 more source

Sequence‐Modulated Active Tripeptide Condensates for Tandem Catalysis

open access: yesAngewandte Chemie, Volume 138, Issue 13, 23 March 2026.
Sequence‐modulated tripeptide coacervates mimic biomolecular condensates with controllable, enzyme‐regulated phase separation. They co‐sequester hydrophobic active species and hydrophilic enzymes, enabling tandem catalysis in aqueous media. Incorporated into artificial cells, they function as adaptive sub‐organelles, orchestrating compartmentalized ...
Hao Han   +7 more
wiley   +2 more sources

In vitro, cellular and in vivo studies of amyloid oligomers structure and toxicity: Challenges and advances

open access: yesProtein Science, Volume 35, Issue 4, April 2026.
Abstract Oligomeric assemblies of amyloidogenic proteins, such as Aβ, tau, α‐synuclein, amylin, transthyretin, and TDP‐43, are increasingly recognized as key drivers of cellular dysfunction across a range of neurodegenerative and systemic disorders.
Magdalena I. Ivanova   +2 more
wiley   +1 more source

Effects of macromolecular crowding agents on protein folding in vitro and in silico [PDF]

open access: bronze, 2013
Alexander Christiansen   +3 more
openalex   +1 more source

In silico peptide self‐assembly reveals the importance of N‐terminal motifs and the inhibition mechanism of the mutation L38M in α‐synuclein fibrillation

open access: yesProtein Science, Volume 35, Issue 4, April 2026.
Abstract Alpha‐synuclein (αSyn) is a presynaptic protein associated with several neurodegenerative diseases. While the non‐amyloid component (NAC) region of the αSyn sequence (residues 65–90) forms the core of all αSyn fibrils, recent findings suggest that the flanking regions play a key role in initiating or preventing amyloid formation. Two motifs in
Van T. T. Nguyen   +4 more
wiley   +1 more source

Small heat shock proteins HspB1 and HspB5 differentially alter the condensation and aggregation of the TDP‐43 low‐complexity domain

open access: yesProtein Science, Volume 35, Issue 4, April 2026.
Abstract TAR DNA‐binding protein 43 (TDP‐43) is a nucleic acid‐binding protein that regulates processes of mRNA metabolism, during which it undergoes condensation mediated by its C‐terminal low‐complexity domain (TDP‐43LCD). TDP‐43 aggregation and condensation are associated with neurodegenerative disease.
Thomas B. Walker   +7 more
wiley   +1 more source

Design and Properties of Genetically Encoded Probes for Sensing Macromolecular Crowding [PDF]

open access: bronze, 2017
Boqun Liu   +5 more
openalex   +1 more source

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