Results 101 to 110 of about 69,622 (226)

The prevalence and distribution of the amyloidogenic transthyretin (TTR) V122I allele in Africa [PDF]

, 2016
Transthyretin (TTR) pV142I (rs76992529-A) is one of the 113 variants in the human TTR gene associated with systemic amyloidosis. It results from a G to A transition at a CG dinucleotide in the codon for amino acid 122 of the mature protein (TTR V122I ...
Alexander, Alice A, Buxbaum, Joel N., Garvey, W. T, Jacobson, Daniel R, Kalidi, Issa, Modiano, David, Sirima, Sodiomon B, Tagoe, Clement, Tishkoff, Sara, Toure, Amadou, Williams, Scott M   +10 more
core   +1 more source

Toxic mechanisms of amyloid oligomers and therapeutic strategies

Protein 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, Carmelo La Rosa, Ayyalusamy Ramamoorthy   +2 more
wiley   +1 more source

Hypoxic regulation of ion channel function and expression [PDF]

, 2002
Acute hypoxia regulates the activity of specific ion channels in a rapid and reversible manner. Such effects underlie appropriate cellular responses to hypoxia which are designed to initiate cardiorespiratory reflexes and contribute importantly to other ...
Peers, C.
core   +1 more source

Altered Dimer Interface Decreases Stability in an Amyloidogenic Protein [PDF]

Journal of Biological Chemistry, 2008
Amyloidoses are devastating and currently incurable diseases in which the process of amyloid formation causes fatal cellular and organ damage. The molecular mechanisms underlying amyloidoses are not well known. In this study, we address the structural basis of immunoglobulin light chain amyloidosis, which results from deposition of light chains ...
Elizabeth M, Baden, Barbara A L, Owen, Francis C, Peterson, Brian F, Volkman, Marina, Ramirez-Alvarado, James R, Thompson   +5 more
openaire   +2 more sources

Structural and morphological dynamics of “on‐path” and “off‐path” oligomers of human islet amyloid polypeptide

Protein Science, Volume 35, Issue 4, April 2026.
Abstract The deposition of cytotoxic human islet amyloid polypeptide (IAPP) aggregates is a hallmark feature of Type 2 Diabetes. However, the structural evolution and cytotoxicity of IAPP aggregate species remain poorly understood. This study combines kinetics, biophysical and cell assays to resolve the morphological dynamics of IAPP aggregation. Using
Daniel Warren, Jadon Sitton, Dmitry Kurouski   +2 more
wiley   +1 more source

The Potential Regulators of Amyloidogenic Pathway of APP Processing in Alzheimer’s Disease

Biomedicines
The amyloidogenic processing of amyloid precursor protein (APP) plays a pivotal role in the pathogenesis of Alzheimer’s disease (AD), primarily through the generation of amyloid-beta (Aβ) peptides, which aggregate to form toxic plaques in the brain.
Daria Krawczuk, Agnieszka Kulczyńska-Przybik, Barbara Mroczko   +2 more
doaj   +1 more source

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

Protein 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, Carmelo La Rosa, Ayyalusamy Ramamoorthy   +2 more
wiley   +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

Protein 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, Sabine M. Ulamec, David J. Brockwell, Sheena E. Radford, Carol K. Hall   +4 more
wiley   +1 more source

Pore formation by human stefin B in its native and oligomeric states and the consequent amyloid induced toxicity.

Frontiers in Molecular Neuroscience, 2012
It is well documented that amyloid forming peptides and proteins interact with membranes and that this correlates with cytotoxicity. To introduce the theme we give a brief description of some amyloidogenic proteins and note their similarities with pore ...
Gregor eAnderluh, Eva eZerovnik
doaj   +1 more source

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

Protein 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, Joshua W. Trowbridge, Shannon McMahon, Nicholas R. Marzano, Lauren Rice, Justin J. Yerbury, Heath Ecroyd, Luke McAlary   +7 more
wiley   +1 more source