Results 91 to 100 of about 69,622 (226)

Sequence-based identification of amyloidogenic β-hairpins reveals a prostatic acid phosphatase fragment promoting semen amyloid formation

open access: yesComputational and Structural Biotechnology Journal
β-Structure-rich amyloid fibrils are hallmarks of several diseases, including Alzheimer’s (AD), Parkinson’s (PD), and type 2 diabetes (T2D). While amyloid fibrils typically consist of parallel β-sheets, the anti-parallel β-hairpin is a structural motif ...
Laetitia F. Heid   +10 more
doaj   +1 more source

On the border of the amyloidogenic sequences: prefix analysis of the parallel beta sheets in the PDB_Amyloid collection

open access: yesJournal of Integrative Bioinformatics, 2021
The Protein Data Bank (PDB) today contains more than 174,000 entries with the 3-dimensional structures of biological macromolecules. Using the rich resources of this repository, it is possible identifying subsets with specific, interesting properties for
Takács Kristóf, Grolmusz Vince
doaj   +1 more source

Membrane permeabilization by Islet Amyloid Polypeptide

open access: yes, 2009
Membrane permeabilization by Islet Amyloid Polypeptide (IAPP) is suggested to be the main mechanism for IAPP-induced cytotoxicity and death of insulin-producing -cells in type 2 diabetes mellitus (T2DM).
Engel, Maarten F.M.
core   +1 more source

The role and therapeutic targeting of α-, β- and γ-secretase in Alzheimer's disease [PDF]

open access: yes, 2015
Alzheimer's disease (AD) is the most common form of dementia in the elderly and its prevalence is set to increase rapidly in coming decades. However, there are as yet no available drugs that can halt or even stabilize disease progression. One of the main
Baillie, George S.   +3 more
core   +1 more source

Investigating transthyretin variants H88R and I107V in amyloid priming: From destabilization to complete dissociation

open access: yesThe FEBS Journal, EarlyView.
Investigated mutations in transthyretin (TTR) disrupt the F87‐centered hydrophobic core that stabilizes its tetrameric structure. The mild I107V mutation weakens inter‐chain packing, while H88R fully abolishes tetramer formation, yielding a monomeric, aggregation‐prone form. Structural, biophysical, and computational analyses reveal that both mutations
István L. Bódy   +7 more
wiley   +1 more source

Utilization and Prognosis of Cardiac Device Implantation in AL Versus ATTR Amyloidosis

open access: yesPacing and Clinical Electrophysiology, EarlyView.
ABSTRACT Introduction Cardiac amyloidosis can cause congestive heart failure, arrhythmias, and heart blocks, which frequently require cardiac device implantation (CDI). However, the differences between light chain (AL) amyloidosis and transthyretin (ATTR) amyloidosis CDI requirements are unknown. Methods A retrospective analysis was conducted using the
Bilal Hussain   +7 more
wiley   +1 more source

Cross-seeding of prions by aggregated α-synuclein leads to transmissible spongiform encephalopathy.

open access: yesPLoS Pathogens, 2017
Aggregation of misfolded proteins or peptides is a common feature of neurodegenerative diseases including Alzheimer's, Parkinson's, Huntington's, prion and other diseases.
Elizaveta Katorcha   +6 more
doaj   +1 more source

Desmin forms toxic, seeding-competent amyloid aggregates that persist in muscle fibers [PDF]

open access: yes, 2019
Desmin-associated myofibrillar myopathy (MFM) has pathologic similarities to neurodegeneration-associated protein aggregate diseases. Desmin is an abundant muscle-specific intermediate filament, and disease mutations lead to its aggregation in cells ...
Arhzaouy, Khalid   +6 more
core   +1 more source

LRP1 Has a Predominant Role in Production over Clearance of Aβ in a Mouse Model of Alzheimer's Disease. [PDF]

open access: yes, 2019
The low-density lipoprotein receptor-related protein-1 (LRP1) has a dual role in the metabolism of the amyloid precursor protein (APP). In cellular models, LRP1 enhances amyloid-β (Aβ) generation via APP internalization and thus its amyloidogenic ...
Gordts, Philip LSM   +7 more
core   +3 more sources

Fluctuating β‐Sheet Secondary Structure in DS119 Explains the Small Effects of Backbone N‐Amination on Thermal Stability

open access: yesJournal of Peptide Science, Volume 32, Issue 5, May 2026.
Residues with backbone N‐amination have been introduced into a region of parallel β‐sheet secondary structure. Contrary to predictions, the N‐amination of Trp9 or Phe33 did not give an increase in the thermal stability of DS119. MD simulations suggest this is due to the highly fluctuating nature of the β‐sheet region. ABSTRACT The miniprotein DS119 has
Yushi Qiao   +4 more
wiley   +1 more source

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