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000126901 1001_ $$aKornreich, M.$$b0
000126901 245__ $$aComposite bottlebrush mechanics: α-internexin fine-tunes neurofilament network properties.
000126901 260__ $$aLondon$$bRoyal Soc. of Chemistry$$c2015
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000126901 520__ $$aNeuronal cytoplasmic intermediate filaments are principal structural and mechanical elements of the axon. Their expression during embryonic development follows a differential pattern, while their unregulated expression is correlated to neurodegenerative diseases. The largest neurofilament proteins of medium (NF-M) and high molecular weight (NF-H) were shown to modulate the axonal architecture and inter-filament spacing. However, the individual roles of the remaining α-internexin (α-Inx) and neurofilament of low molecular weight (NF-L) proteins in composite filaments remained elusive. In contrast to previous predictions, we show that when co-assembled with NF-M, the shortest and the least charged α-Inx protein increases inter-filament spacing. These findings suggest a novel structural explanation for the expression pattern of neurofilament proteins during embryonic development. We explain our results by an analysis of ionic cross-links between the disordered polyampholytic C-terminal tails and suggest that a collapsed conformation of the α-Inx tail domain interferes with tail cross-linking near the filament backbone.
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000126901 650_7 $$2NLM Chemicals$$aIntermediate Filament Proteins
000126901 650_7 $$2NLM Chemicals$$aNeurofilament Proteins
000126901 650_7 $$2NLM Chemicals$$aRecombinant Proteins
000126901 650_7 $$2NLM Chemicals$$aalpha-internexin
000126901 650_7 $$025852-47-5$$2NLM Chemicals$$aHydrogel
000126901 7001_ $$aMalka-Gibor, E.$$b1
000126901 7001_ $$aLaser-Azogui, A.$$b2
000126901 7001_ $$aDoron, O.$$b3
000126901 7001_ $$0P:(DE-He78)7892a89fee19b8e3912c7423d660765d$$aHerrmann, Harald$$b4$$udkfz
000126901 7001_ $$aBeck, R.$$b5
000126901 773__ $$0PERI:(DE-600)2191476-X$$a10.1039/C5SM00662G$$gVol. 11, no. 29, p. 5839 - 5849$$n29$$p5839 - 5849$$tSoft matter$$v11$$x1744-6848$$y2015
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