Results 201 to 210 of about 56,365 (241)

Disarming the Hsp70–Bim Alliance: Small‐Molecule and Peptidic Disruptors of a Chaperone‐Apoptotic Switch in Cancer

open access: yesChemistryOpen, Volume 15, Issue 4, April 2026.
Targeting a nucleotide‐sensitive groove on Hsp70 that binds the Bim BH3 helix, we integrate structures, biophysics, and SAR from peptides, fragments, and phenalene‐dicarbonitrile “wedges.” These disrupt the Hsp70–Bim complex with sub‐µM cellular engagement and in vivo activity while sparing Hsp90/mortalin.
Emadeldin M. Kamel   +5 more
wiley   +1 more source

Coupling CZE, Liquid‐Phase Ion Mobility, to MS/MS for Quantitative Top‐Down Proteomics: Revealing Significant Proteoform Differences Between Healthy and Alzheimer's Disease Brains

open access: yesPROTEOMICS, Volume 26, Issue 4, Page 23-35, April 2026.
ABSTRACT Alzheimer's disease (AD) is a neurodegenerative disorder characterized by cognitive decline and pathological protein aggregation. Comprehensive quantitative proteomics of brain tissues from AD patients is critical for pursuing a better understanding of the molecular mechanisms that drive AD progression.
Mehrdad Falamarzi Askarani   +3 more
wiley   +1 more source

Functions of J‐domain proteins in mitochondrial protein biogenesis

open access: yesProtein Science, Volume 35, Issue 4, April 2026.
Abstract Mitochondrial biogenesis and functions depend on the import and assembly of more than 1000 proteins that are made as precursors on cytosolic ribosomes. The majority of these precursor proteins are transported from the ribosome to the translocase of the outer membrane (TOM complex), which constitutes the main entry site for mitochondrial ...
Vitasta Tiku   +3 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

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

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