Results 31 to 40 of about 288,605 (343)

β-microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pH [PDF]

, 2014
Although the molecular mechanisms underlying the pathology of amyloidoses are not well understood, the interaction between amyloid proteins and cell membranes is thought to play a role in several amyloid diseases. Amyloid fibrils of β-microglobulin (βm),
Eric W. Hewitt, Xue, W-F, Beales Paul A., Sheynis, T, Radford, SE, Neil A. Ranson (610030), Sheena E. Radford (197775), Beales, Paul A, Goodchild Sophia C., Thompson, Rebecca, Xue Wei-Feng, Neil A. Ranson, Thompson Rebecca, Sheena E Radford, Sophia C. Goodchild, Sheynis Tania, Eric W Hewitt, Kevin W. Tipping (610028), Radford Sheena E., Tipping Kevin W., Sheena E. Radford, Hewitt, EW, Xue, Wei-Feng, Beales, PA, Radford, Sheena E, Tipping, KW, Sophia C Goodchild, Paul A Beales, Goodchild, SC, Ranson, Neil A, Rebecca Thompson, Wei-Feng Xue (610029), Ranson Neil A., Neil A Ranson, Tipping, Kevin W, Tania Sheynis (610026), Kevin W Tipping, Tania Sheynis, Sheynis, Tania, Wei-Feng Xue, Goodchild, Sophia C, Eric W. Hewitt (197779), Hewitt, Eric W, Hewitt Eric W., Sophia C. Goodchild (283440), Ranson, NA, Rebecca Thompson (610027), Paul A. Beales (435545), Thompson, R, Paul A. Beales   +49 more
core   +1 more source

Cryo-EM structure of a catalytic amyloid fibril

Scientific Reports, 2023
Catalytic amyloid fibrils are novel types of bioinspired, functional materials that combine the chemical and mechanical robustness of amyloids with the ability to catalyze a certain chemical reaction.
Thomas Heerde, Akanksha Bansal, Matthias Schmidt, Marcus Fändrich   +3 more
doaj   +1 more source

Cryo-EM structure of amyloid fibrils formed by the entire low complexity domain of TDP-43

Nature Communications, 2020
Amyotrophic lateral sclerosis and several other neurodegenerative diseases are associated with brain deposits of amyloid-like aggregates formed by the C-terminal fragments of TDP-43 that contain the low complexity domain of the protein.
Qiuye Li, W. M. Babinchak, W. Surewicz
semanticscholar   +1 more source

Mouse senile amyloid fibrils deposited in skeletal muscle exhibit amyloidosis-enhancing activity. [PDF]

PLoS Pathogens, 2010
Amyloidosis describes a group of protein folding diseases in which amyloid proteins are abnormally deposited in organs and/or tissues as fine fibrils.
Jinze Qian, Jingmin Yan, Fengxia Ge, Beiru Zhang, Xiaoying Fu, Hiroshi Tomozawa, Jinko Sawashita, Masayuki Mori, Keiichi Higuchi   +8 more
doaj   +1 more source

Effect of the fluorescent probes ThT and ANS on the mature amyloid fibrils

Prion, 2020
Fluorescent probes thioflavin T (ThT) and 1-anilino-8-naphthalene sulfonate (ANS) are widely used to study amyloid fibrils that accumulate in the body of patients with serious diseases, such as Alzheimer’s, Parkinson’s, prion diseases, etc.
M. Sulatsky, A. I. Sulatskaya, O. Povarova, I. A. Antifeeva, I. Kuznetsova, K. Turoverov   +5 more
semanticscholar   +1 more source

Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly [PDF]

, 2008
Self-assembly of misfolded proteins into ordered fibrillar aggregates known as amyloid results in numerous human diseases. Despite an increasing number of proteins and peptide fragments being recognised as amyloidogenic, how these amyloid aggregates ...
Xue, Wei-Feng, Radford, Sheena E., Homans, Steve W.   +2 more
core   +1 more source

Concentration-dependent polymorphism of insulin amyloid fibrils [PDF]

PeerJ, 2019
Protein aggregation into highly structured fibrils has long been associated with several neurodegenerative disorders, such as Alzheimer’s or Parkinson’s disease.
Andrius Sakalauskas, Mantas Ziaunys, Vytautas Smirnovas   +2 more
doaj   +2 more sources

Amyloid tracers detect multple binding sites in Alzheimer´s disease brain tissue. [PDF]

, 2013
Imaging fibrillar amyloid-β deposition in the human brain in vivo by positron emission tomography has improved our understanding of the time course of amyloid-β pathology in Alzheimer’s disease. The most widely used amyloid-β imaging tracer so far is 11C-
Nordberg, A,, Ni, Ruiqing, Marutle, Amelia, Gillberg, P-G, Marutle, A,, Bergfors, A, Nordberg, Agneta, Gillberg, Per-Göran, Bergfors, Assar, Ni, R,   +9 more
core   +1 more source

Apolipoprotein E Regulates Amyloid Formation within Endosomes of Pigment Cells

Cell Reports, 2015
Accumulation of toxic amyloid oligomers is a key feature in the pathogenesis of amyloid-related diseases. Formation of mature amyloid fibrils is one defense mechanism to neutralize toxic prefibrillar oligomers.
Guillaume van Niel, Ptissam Bergam, Aurelie Di Cicco, Ilse Hurbain, Alessandra Lo Cicero, Florent Dingli, Roberta Palmulli, Cecile Fort, Marie Claude Potier, Leon J. Schurgers, Damarys Loew, Daniel Levy, Graça Raposo   +12 more
doaj   +1 more source

Nucleation of Polymorphic Amyloid Fibrils [PDF]

Biophysical Journal, 2015
One and the same protein can self-assemble into amyloid fibrils with different morphologies. The phenomenon of fibril polymorphism is relevant biologically because different fibril polymorphs can have different toxicity, but there is no tool for predicting which polymorph forms and under what conditions.
openaire   +4 more sources