Results 21 to 30 of about 160,241 (252)

Analysis of Toxic Amyloid Fibril Interactions at Natively Derived Membranes by Ellipsometry [PDF]

, 2015
There is an ongoing debate regarding the culprits of cytotoxicity associated with amyloid disorders. Although small pre-fibrillar amyloid oligomers have been implicated as the primary toxic species, the fibrillar amyloid material itself can also induce ...
Smith, Rachel A. S., Xue, Wei-Feng, Blakeman Ben J. F., Blakeman, Ben J. F., Smith, David P., Benjamin Abell (769585), Rachel A S Smith, David P. Smith (131751), Benjamin Abell, Wei-Feng Xue (610029), Ben J F Blakeman, Aleksey Nabok, David P Smith, Rachel A. S. Smith (769582), Smith Rachel A. S., Xue Wei-Feng, Nabok Aleksey, Abell Benjamin, Wei-Feng Xue, Ben J. F. Blakeman (769584), Abell, Benjamin, Aleksey Nabok (769583), Smith David P., Nabok, Aleksey, Leonenko, Zoya   +24 more
core   +2 more sources

Immunoprecipitation of amyloid fibrils by the use of an antibody that recognizes a generic epitope common to amyloid fibrils.

PLoS ONE, 2014
Amyloid fibrils are associated with many maladies, including Alzheimer's disease (AD). The isolation of amyloids from natural materials is very challenging because the extreme structural stability of amyloid fibrils makes it difficult to apply ...
Erin R Greiner, Jeffery W Kelly, Fernando L Palhano   +2 more
doaj   +1 more source

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

Interfacial Electrostatic Self‐Assembly of Amyloid Fibrils into Multifunctional Protein Films

Advanced Science, 2023
Amyloid fibrils have generated steadily increasing traction in the development of natural and artificial materials. However, it remains a challenge to construct bulk amyloid films directly from amyloid fibrils due to their intrinsic brittleness.
Yangyang Han, Yiping Cao, Jiangtao Zhou, Yang Yao, Xiaodong Wu, Sreenath Bolisetty, Michael Diener, Stephan Handschin, Canhui Lu, Raffaele Mezzenga   +9 more
doaj   +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

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

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

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

Structural diversity and polymorphism in amyloid fibrils from single organs and single patients with AL amyloidosis [PDF]

Structural Dynamics
Amyloidogenic light chain (AL) amyloidosis is a complicated disease that results from aggregation of antibody light chain proteins into amyloid fibrils, that then disrupt organ function.
Parker T Bassett, Lorena Saelices, Binh Nguyen, Virender Singh, Gareth Morgan   +4 more
doaj   +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