Results 71 to 80 of about 288,605 (343)

A Peptide Derived from the HIV-1 gp120 Coreceptor-Binding Region Promotes Formation of PAP248-286 Amyloid Fibrils to Enhance HIV-1 Infection.

open access: yesPLoS ONE, 2015
BackgroundSemen is a major vehicle for HIV transmission. Prostatic acid phosphatase (PAP) fragments, such as PAP248-286, in human semen can form amyloid fibrils to enhance HIV infection.
Jinquan Chen   +9 more
doaj   +1 more source

Aggregate Geometry in Amyloid Fibril Nucleation [PDF]

open access: yesPhysical Review Letters, 2013
We present and study a minimal structure-based model for the self-assembly of peptides into ordered beta-sheet-rich fibrils. The peptides are represented by unit-length sticks on a cubic lattice and interact by hydrogen bonding and hydrophobicity forces.
Irbäck, Anders   +4 more
openaire   +3 more sources

Site-specific perturbations of alpha-synuclein fibril structure by the Parkinson's disease associated mutations A53T and E46K.

open access: yes, 2013
PMCID: PMC3591419This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited ...
Chad M Rienstra   +33 more
core   +1 more source

Functional Blood‐Brain Barrier Crossing by Biomimetic M13 Phage Vectors for Targeted Neuronal Delivery

open access: yesAdvanced Healthcare Materials, EarlyView.
This study investigates the M13 bacteriophage as a biomimetic nanovector capable of crossing in vitro models of the blood–brain barrier. By exploiting peculiar transcellular pathways, M13 avoids lysosomal degradation and preserves its structural integrity and functionality.
Silvia Vercellino   +12 more
wiley   +1 more source

On the heat stability of amyloid-based biological activity: insights from thermal degradation of insulin fibrils.

open access: yesPLoS ONE, 2014
Formation of amyloid fibrils in vivo has been linked to disorders such as Alzheimer's disease and prion-associated transmissible spongiform encephalopathies.
Weronika Surmacz-Chwedoruk   +4 more
doaj   +1 more source

Cryo-EM structure of cardiac amyloid fibrils from an immunoglobulin light chain AL amyloidosis patient

open access: yesNature Communications, 2018
Systemic light chain amyloidosis (AL) is a life-threatening disease caused by aggregation and deposition of monoclonal immunoglobulin light chains (LC) in target organs.
P. Swuec   +13 more
semanticscholar   +1 more source

Structural Studies of Cystatin B Amyloid Fibre and Oligomer [PDF]

open access: yes, 2013
Amyloid fibres are characteristic of over 25 degenerative human diseases including Alzheimer’s and Parkinson’s disease. Amyloid fibres are insoluble, highly stable, ordered cross-β sheet structures, which form as a result of conformational change and ...
Davis, Peter J.
core  

Kelvin Probe Force Microscopy in Bionanotechnology: Current Advances and Future Perspectives

open access: yesAdvanced Materials, EarlyView.
Kelvin probe force microscopy (KPFM) enables the nanoscale mapping of electrostatic surface potentials. While widely applied in materials science, its use in biological systems remains emerging. This review presents recent advances in KPFM applied to biological samples and provides a critical perspective on current limitations and future directions for
Ehsan Rahimi   +4 more
wiley   +1 more source

Identification of transmissible proteotoxic oligomer-like fibrils that expand conformational diversity of amyloid assemblies

open access: yesCommunications Biology, 2021
Nguyen et al identified cytotoxic amyloid fibrils with oligomer-like characteristics, which were assembled from an islet amyloid polypeptide (IAPP) derivative containing an Asn-to-Gln substitution (N21Q). They presented evidence to show that these stable
Phuong Trang Nguyen   +5 more
doaj   +1 more source

Protein Disulfide Isomerase Disassembles TDP‐43/G3BP1 Condensates and Antagonizes TDP‐43 Pathological Aggregates

open access: yesAdvanced Science, EarlyView.
Cytoplasmic aggregation of TDP‐43 is a common pathological feature in amyotrophic lateral sclerosis, frontotemporal lobar degeneration, and Alzheimer's disease with TDP‐43 pathology. This study reports that wild‐type PDI slows down phase separation of TDP‐43 through direct interaction with TDP‐43.
Jia‐Qi Liu   +14 more
wiley   +1 more source

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