نتایج جستجو برای: fibril inhibitor

تعداد نتایج: 218571  

Journal: :The journal of physical chemistry. B 2009
Edward P O'Brien Yuko Okamoto John E Straub Bernard R Brooks D Thirumalai

The mechanism of addition of a soluble unstructured monomer to a preformed ordered amyloid fibril is a complex process. On the basis of the kinetics of monomer disassociation of Abeta(1-40) from the amyloid fibril, it has been suggested that deposition is a multistep process involving a rapid reversible association of the unstructured monomer to the fibril surface (docking) followed by a slower...

2007
E. Prabhu Raman Takako Takeda Valeri Barsegov Dmitri K. Klimov

In most cases authors are permitted to post their version of the article (e.g. in Word or Tex form) to their personal website or institutional repository. Authors requiring further information regarding Elsevier's archiving and manuscript policies are encouraged to visit: Using the experimental structures of Aβ amyloid fibrils and all-atom molecular dynamics, we study the force-induced unbindin...

Journal: :Journal of anatomy 1998
V Ottani M Franchi V De Pasquale L Leonardi M Morocutti A Ruggeri

Collagen fibre organisation and fibril size were studied in the buccal gingival and hard palate mucosa of Macacus rhesus monkey. Light and electron microscopy analysis showed connective papillae exhibiting a similar inner structure in the different areas examined, but varying in distribution, shape and size. Moving from the deep to surface layers of the buccal gingival mucosa (free and attached...

Journal: :Protein science : a publication of the Protein Society 2008
Zhefeng Guo David Eisenberg

Numerous human disorders are associated with the formation of protein fibrils. The fibril-forming capacity of a protein has been found in recent studies to be determined by a short segment of residues that forms a dual beta-sheet, called a steric zipper, in the spine of the fibril. The question arises as to whether a fibril-forming segment, when inserted within the sequence of a globular protei...

2011
Shannon E. Hill Tatiana Miti Tyson Richmond Martin Muschol

Formation of large protein fibrils with a characteristic cross β-sheet architecture is the key indicator for a wide variety of systemic and neurodegenerative amyloid diseases. Recent experiments have strongly implicated oligomeric intermediates, transiently formed during fibril assembly, as critical contributors to cellular toxicity in amyloid diseases. At the same time, amyloid fibril assembly...

Journal: :علوم و تکنولوژی پلیمر 0
احسان باغبان کوچک الهام فلاحی محمد حقیقت کیش

atechnical feasibility study has been conducted on production of nano- and micro-fibrils from nylon 6/polypropylene grafted with maleic anhydride/polypropylene blended films. fibrils are prepared in four consecutive steps.in the first step the polymers melt blended in an extruder with and without compatibilizers to produce chips; in the second step films are extruded from polymer blends chips, ...

Journal: :Connective tissue research 2003
Todd C Battaglia Randall T Clark Anikar Chhabra Veronique Gaschen Ernst B Hunziker Borjana Mikic

The mechanisms by which tendon strength is established during growth and development and restored following injury are not completely understood and are likely to be complex, multifactorial processes. Several studies examining the relationship between mechanical behavior and ultrastructural characteristics of tendons and ligaments during growth and maturation suggest that collagen fibril diamet...

Journal: :Organic & biomolecular chemistry 2013
Weipeng Li Xiaowei Duan Hong Yan Hongxing Xin

4H-1,4-oxazines were designed as transthyretin (TTR) amyloid fibril inhibitors based on an analysis of the interactions between known small molecule inhibitors and TTR by molecular docking. A series of 2,4,6-triaryl-4H-1,4-oxazines was synthesized by the cyclization of N,N-bis(phenacyl)anilines with POCl3 in pyridine. Inhibition of TTR amyloid fibril was evaluated by a fibril formation assay. T...

Journal: :The journal of physical chemistry. B 2015
L G Rizzi S Auer

It is well established that amyloid fibril solubility is protein specific, but how solubility depends on the interactions between the fibril building blocks is not clear. Here we use a simple protein model and perform Monte Carlo simulations to directly measure the solubility of amyloid fibrils as a function of the interaction between the fibril building blocks. Our simulations confirms that th...

2018

Polymorphism is a key feature of amyloid fibril structures but it remains challenging to explain these variations for a particular sample. Here, we report electron cryomicroscopy-based reconstructions from different fibril morphologies formed by a peptide fragment from an amyloidogenic immunoglobulin light chain. The observed fibril morphologies vary in the number and cross-sectional arrangemen...

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