Results 41 to 50 of about 160,241 (252)

Supersaturation-Dependent Formation of Amyloid Fibrils

Molecules, 2022
The supersaturation of a solution refers to a non-equilibrium phase in which the solution is trapped in a soluble state, even though the solute’s concentration is greater than its thermodynamic solubility. Upon breaking supersaturation, crystals form and the concentration of the solute decreases to its thermodynamic solubility. Soon after the discovery
Yuji Goto, Masahiro Noji, Kichitaro Nakajima, Keiichi Yamaguchi   +3 more
openaire   +3 more sources

Towards Optimal Control of Amyloid Fibrillation

Bulletin of Mathematical Biology, 2023
26pages, 7 ...
Mengshou Wang, Gao Li, Liangrong Peng, Liu Hong   +3 more
openaire   +3 more sources

Epigallocatechin-3-gallate rapidly remodels PAP85-120, SEM1(45-107), and SEM2(49-107) seminal amyloid fibrils

Biology Open, 2015
Semen harbors amyloid fibrils formed by proteolytic fragments of prostatic acid phosphatase (PAP248-286 and PAP85-120) and semenogelins (SEM1 and SEM2) that potently enhance HIV infectivity.
Laura M. Castellano, Rebecca M. Hammond, Veronica M. Holmes, Drew Weissman, James Shorter   +4 more
doaj   +1 more source

Modulation of β-Amyloid Fibril Formation in Alzheimer’s Disease by Microglia and Infection

Frontiers in Molecular Neuroscience, 2020
Amyloid plaques are a pathological hallmark of Alzheimer’s disease. The major component of these plaques are highly ordered amyloid fibrils formed by amyloid-β (Aβ) peptides.
Madeleine R. Brown, Sheena E. Radford, Eric W. Hewitt   +2 more
doaj   +1 more source

Exploring the sequence–structure relationship for amyloid peptides [PDF]

, 2012
Amyloid fibril formation is associated with misfolding diseases, as well as fulfilling a functional role. The cross-β molecular architecture has been reported in increasing numbers of amyloid-like fibrillar systems. The Waltz algorithm is able to predict
Morris, Kyle L., Rousseau, F. (Frederic), Maya Debulpaep (16158989), Rodger, Alison, Frederic Rousseau (5872), Schymkowitz, Joost, Joost Schymkowitz (5868), Serpell, Louise C., Matthew R Hicks (16064381), Louise Serpell (4461124), Rousseau, Frederic, Hicks, Matthew R., Kyle L Morris (9164846), Alison Rodger (282425), Debulpaep, Maya   +14 more
core   +1 more source

Binding of serum-derived amyloid-associated proteins to amyloid fibrils

, 2022
Amyloid signature proteins such as serum amyloid P component, apolipoprotein E (ApoE), and ApoA-IV generally co-localise with amyloid, regardless of the types of amyloid precursor protein or the organs.
Yohei Misumi (3190254), Konen Obayashi (3634996), Yuri Tabata (13774993), Masayoshi Tasaki (3190260), Toshiya Nomura (3635002), Mitsuharu Ueda (3190248), Shiori Yamakawa (13774996)   +6 more
core   +1 more source

Regional distribution of amyloid-Bri deposition and its association with neurofibrillary degeneration in familial British dementia [PDF]

, 2001
Familial British dementia (FBD), pathologically characterized by cerebral amyloid angiopathy (CAA), amyloid plaques, and neurofibrillary degeneration, is associated with a stop codon mutation in the BRI gene resulting in the production of an ...
Tammaryn Lashley, Ghiso, J, Vidal, R, Ayling, H., Gibb, G, Anderton, B H, Hilary Ayling, Rostagno, A., Anderton, B.H., Plant, G., Janice L. Holton, Tamas Revesz, Revesz, T, Martinian, L, Henry Houlden, Ruben Vidal, Nicholas W. Wood, Lashley, T, Revesz, T., Frangione, B., Jorge Ghiso, Ayling, H, Holton, J.L., Christopher J. Guerin, Houlden, H, Plant, G, Holton, J L, Gordon Plant, Rostagno, A, Lashle, T., Gibb, G., Lillian Martinian, Ghiso, J., Graham Gibb, Martinian, L., Brian H. Anderton, Agueda Rostagno, Houlden, H., Wood, N.W., Frangione, B, Vidal, R., Guerin, C J, Wood, N W, Guerin, C.J., Blas Frangione   +44 more
core   +1 more source

Self-assembling nanomaterials: monitoring the formation of amyloid fibrils, with a focus on small-angle X-ray scattering.

, 2013
Amyloid fibrils are attractive targets for applications in biotechnology. These thin, nanoscale protein fibers are highly ordered structures that self-assemble from their component proteins or peptides.
Gras, Sally L, Sawyer, Elizabeth B, Sally L. Gras, Elizabeth B. Sawyer, Sawyer, E.B., Gras, S.L.   +5 more
core   +2 more sources

Amyloid fibril proteomics of AD brains reveals modifiers of aggregation and toxicity

Molecular Neurodegeneration, 2023
Background The accumulation of amyloid beta (Aβ) peptides in fibrils is prerequisite for Alzheimer’s disease (AD). Our understanding of the proteins that promote Aβ fibril formation and mediate neurotoxicity has been limited due to technical challenges ...
Arun Upadhyay, Deepak Chhangani, Nalini R. Rao, Julia Kofler, Robert Vassar, Diego E. Rincon-Limas, Jeffrey N. Savas   +6 more
doaj   +1 more source

Fibril Fragmentation Enhances Amyloid Cytotoxicity [PDF]

, 2009
Fibrils associated with amyloid disease are molecular assemblies of key biological importance, yet how cells respond to the presence of amyloid remains unclear. Cellular responses may not only depend on the chemical composition or molecular properties of
Xue, Wei-Feng, Hellewell, Andrew L., Gosal, Walraj S., Hewitt, Eric W., Radford, Sheena E., Homans, Steve W.   +5 more
core   +1 more source