Results 11 to 20 of about 114,998 (297)

What drives amyloid molecules to assemble into oligomers and fibrils? [PDF]

, 2010
We develop a general theory for three states of equilibrium of amyloid peptides: the monomer, oligomer, and fibril. We assume that the oligomeric state is a disordered micelle-like collection of a few peptide chains held together loosely by hydrophobic ...
Ahmad, Auer, Bitan, Chen, Chimon, Conway, Dill, Dill, Dill, Dobson, DuBay, Fernandez-Escamilla, Ghosh, Ghosh, Glabe, Hall, Hamada, Hardy, Jarrett, Jeremy D. Schmit, Kashchiev, Ken Dill, Kim, Kingshuk Ghosh, Klement, Knowles, Lashuel, Lee, Lee, Lifson, Lührs, Modler, Nelson, Pallitto, Petkova, Petkova, Poland, Powers, Sawaya, Schellmann, Serio, Sillero, Tartaglia, Terzi, Tiana, Trovato, van Gestel, van Gestel, van Raaij, Wang, Wasmer, Wolf, Yong, Zhang, Zimm   +54 more
core   +4 more sources

Fibril elongation mechanisms of HET-s prion-forming domain: Topological evidence for growth polarity [PDF]

Proteins 79, 3067-3081 (2011), 2011
The prion-forming C-terminal domain of the fungal prion HET-s forms infectious amyloid fibrils at physiological pH. The conformational switch from the non-prion soluble form to the prion fibrillar form is believed to have a functional role, since HET-s ...
Aguzzi, Alm, Auer, Auer, Baker, Baulgerie, Baumketner, Blackley, Borroguero, Bryngelson, Buchete, Cannon, Castellani, Cecchini, Clementi, DePace, Ding, Esler, Fang, Favrin, Fawzi, Fawzi, Go, Greenwald, Hardy, Hoang, Hoang, Hubner, Huet, Jang, Krishnan, Kusumoto, Lam, Lam, Lange, Lange, Lange, Levy, Ma, Metropolis, Micheletti, Miyazawa, Nguyen, O'Brien, Petkova, Petkova, Prusiner, Reddy, Ritter, Rojas, Sabaté, Saupe, Shewmaker, Straub, Sulkowska, Takeda, Takeda, Tarus, Tesi, Tessier, Trovato, Trovato, Tuite, Urbanc, Urbanc, Wang, Wasmer, Wasmer, Wei, Wei, Wells, Will, Zamparo   +72 more
core   +2 more sources

Multiscale Characterization of Type I Collagen Fibril Stress–Strain Behavior under Tensile Load: Analytical vs. MD Approaches

Bioengineering, 2022
Type I collagen is one of the most important proteins in the human body because of its role in providing structural support to the extracellular matrix of the connective tissues.
Afif Gouissem, Raouf Mbarki, Fadi Al Khatib, Malek Adouni   +3 more
doaj   +1 more source

Quantitative flow cytometric selection of tau conformational nanobodies specific for pathological aggregates

Frontiers in Immunology, 2023
Single-domain antibodies, also known as nanobodies, are broadly important for studying the structure and conformational states of several classes of proteins, including membrane proteins, enzymes, and amyloidogenic proteins.
Jennifer M. Zupancic, Jennifer M. Zupancic, Matthew D. Smith, Matthew D. Smith, Hanna Trzeciakiewicz, Mary E. Skinner, Sean P. Ferris, Emily K. Makowski, Emily K. Makowski, Michael J. Lucas, Michael J. Lucas, Michael J. Lucas, Nikki McArthur, Ravi S. Kane, Henry L. Paulson, Henry L. Paulson, Henry L. Paulson, Peter M. Tessier, Peter M. Tessier, Peter M. Tessier, Peter M. Tessier, Peter M. Tessier, Peter M. Tessier   +22 more
doaj   +1 more source

Conformational Variability of Amyloid-β and the Morphological Diversity of Its Aggregates

Molecules, 2022
Protein folding is the most fundamental and universal example of biomolecular self-organization and is characterized as an intramolecular process. In contrast, amyloidogenic proteins can interact with one another, leading to protein aggregation.
Maho Yagi-Utsumi, Koichi Kato
doaj   +1 more source

Beyond Amyloid Fibers: Accumulation, Biological Relevance, and Regulation of Higher-Order Prion Architectures

Viruses, 2022
The formation of amyloid fibers is associated with a diverse range of disease and phenotypic states. These amyloid fibers often assemble into multi-protofibril, high-order architectures in vivo and in vitro.
Wesley R. Naeimi, Tricia R. Serio
doaj   +1 more source

Transferrin-Functionalized Liposomes for the Delivery of Gallic Acid: A Therapeutic Approach for Alzheimer’s Disease

Pharmaceutics, 2022
Senile plaques composed of amyloid β (Aβ) fibrils are considered the leading cause of Alzheimer’s disease (AD). Molecules with the ability to inhibit Aβ aggregation and/or promote Aβ clearance are thus a promising approach for AD therapy.
Stéphanie Andrade, Joana A. Loureiro, Maria C. Pereira   +2 more
doaj   +1 more source

Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel. [PDF]

, 2018
α-Synuclein (aSyn) fibrillar polymorphs have distinct in vitro and in vivo seeding activities, contributing differently to synucleinopathies. Despite numerous prior attempts, how polymorphic aSyn fibrils differ in atomic structure remains elusive.
Boyer, David R, Eisenberg, David S, Ge, Peng, Jiang, Lin, Li, Binsen, Murray, Kevin A, Nair, Gayatri, Sawaya, Michael R, Sheth, Phorum, Shin, Woo Shik, Ye, Shulin, Zhang, Meng, Zhou, Z Hong   +12 more
core   +2 more sources

Digital Light Processing of 2D Lattice Composites for Tunable Self‐Sensing and Mechanical Performance

Advanced Engineering Materials, EarlyView., 2023
The study presents the mechanical and in situ sensing performance of digital light processing‐enabled 2D lattice nanocomposites under monotonic tensile and repeated cyclic loading, and provides guidelines for the design of architectures suitable for strain sensors and smart lightweight structures.
Omar Waqas Saadi, Mohammed Ayaz Uddin, Andreas Schiffer, Shanmugam Kumar   +3 more
wiley   +1 more source

D-band strain underestimates fibril strain for twisted collagen fibrils at low strains [PDF]

, 2021
Collagen fibrils are the main structural component of load-bearing tissues such as tendons, ligaments, skin, the cornea of the eye, and the heart. The D-band of collagen fibrils is an axial periodic density modulation that can be easily characterized by tissue-level X-ray scattering. During mechanical testing, D-band strain is often used as a proxy for
arxiv   +1 more source