نتایج جستجو برای: amyloid fibrils

تعداد نتایج: 41968  

Journal: :Biochemistry 2003
Scott C Hartsel Theodore R Weiland

The membrane-active antifungal agent amphotericin B (AmB) is one of the few agents shown to slow the course of prion diseases in animals. Congo Red and other small molecules have been reported to directly inhibit amyloidogenesis in both prion and Alzheimer peptide model systems via specific binding. We propose that it is possible that AmB may act similarly to physically prevent conversion of th...

Journal: :Journal of physics. Condensed matter : an Institute of Physics journal 2012
Chiu Fan Lee

We investigate the length distribution of self-assembled, long and stiff polymers at thermal equilibrium. Our analysis is based on calculating the partition functions of stiff polymers of variable lengths in the elastic regime. Our conclusion is that the length distribution of this self-assembled system follows closely the exponential distribution, except at the short length limit. We then disc...

Journal: :Physical chemistry chemical physics : PCCP 2013
Vipin Agarwal Rasmus Linser Muralidhar Dasari Uwe Fink Juan-Miguel Lopez del Amo Bernd Reif

The amyloid β-peptide (Aβ) is the major structural component of amyloid fibrils in the plaques of brains of Alzheimer's disease patients. Numerous studies have addressed important aspects of secondary and tertiary structure of fibrils. In electron microscopic images, fibrils often bundle together. The mechanisms which drive the association of protofilaments into bundles of fibrils are not known...

2017
Nadia R Roan Nathallie Sandi-Monroy Nargis Kohgadai Shariq M Usmani Katherine G Hamil Jason Neidleman Mauricio Montano Ludger Ständker Annika Röcker Marielle Cavrois Jared Rosen Kara Marson James F Smith Christopher D Pilcher Friedrich Gagsteiger Olena Sakk Michael O'Rand Polina V Lishko Frank Kirchhoff Jan Münch Warner C Greene

Unlike other human biological fluids, semen contains multiple types of amyloid fibrils in the absence of disease. These fibrils enhance HIV infection by promoting viral fusion to cellular targets, but their natural function remained unknown. The similarities shared between HIV fusion to host cell and sperm fusion to oocyte led us to examine whether these fibrils promote fertilization. Surprisin...

Journal: :Biomacromolecules 2013
Jacob A Irwin H Edward Wong Inchan Kwon

Amyloid fibrils implicated in numerous human diseases are thermodynamically very stable. Stringent conditions that would not be possible in a physiological environment are often required to disrupt the stable fibrils. Recently, there is increasing evidence that small molecules can remodel amyloid fibrils in a physiologically relevant manner. In order to investigate possible fibril remodeling me...

Journal: :Journal of the American Society of Nephrology : JASN 2004
Suguru Yamamoto Itaru Yamaguchi Kazuhiro Hasegawa Shinobu Tsutsumi Yuji Goto Fumitake Gejyo Hironobu Naiki

beta(2)-Microglobulin-related (A beta 2M) amyloidosis is a frequent and serious complication in patients on long-term dialysis, and beta(2)-microglobulin is a major structural component of A beta 2M amyloid fibrils. Several biologic molecules inhibiting the depolymerization of A beta 2M amyloid fibrils at a neutral pH were found recently. The effect of trifluoroethanol and glycosaminoglycans (G...

Journal: :Cell 2013
Adriano Aguzzi Aaron D. Gitler

Alzheimer's disease (AD) is associated with the deposition of β-amyloid (Aβ) plaques in the brain. In this issue, by cleverly processing patient samples, Lu et al. define a novel structural model of Aβ fibrils from AD brain, revealing surprising differences from in vitro fibrils. These findings may lead to structure-specific inhibitors and more selective amyloid-imaging methods.

Journal: :Angewandte Chemie 2012
Vanessa K Morris Rasmus Linser Karyn L Wilde Anthony P Duff Margaret Sunde Ann H Kwan

GrEASy fibrils: Hydrophobins are fungal proteins that assemble into an amphipathic fibrillar monolayer with amyloid properties and a hydrophobic face as water-resistant as Teflon. Solid-state NMR studies on EAS hydrophobin fibrils reveal direct evidence of a partial molecular rearrangement on assembly and an ordered β-sheet-rich core in the context of a whole protein in this functional amyloid.

2017
Clara Iannuzzi Margherita Borriello Marianna Portaccio Gaetano Irace Ivana Sirangelo

Human insulin is a widely used model protein for the study of amyloid formation as both associated to insulin injection amyloidosis in type II diabetes and highly prone to form amyloid fibrils in vitro. In this study, we aim to gain new structural insights into insulin fibril formation under two different aggregating conditions at neutral and acidic pH, using a combination of fluorescence, circ...

2013
Kathryn E Tiller Peter M Tessier

High resolution structures and computational methods have been used to identify compounds that prevent amyloid fibrils associated with Alzheimer's disease from dissociating into toxic species.

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