Home > Publications database > Composite bottlebrush mechanics: α-internexin fine-tunes neurofilament network properties. > print |
001 | 126901 | ||
005 | 20240228140853.0 | ||
024 | 7 | _ | |a 10.1039/C5SM00662G |2 doi |
024 | 7 | _ | |a pmid:26100609 |2 pmid |
024 | 7 | _ | |a 1744-683X |2 ISSN |
024 | 7 | _ | |a 1744-6848 |2 ISSN |
024 | 7 | _ | |a altmetric:4194375 |2 altmetric |
037 | _ | _ | |a DKFZ-2017-02929 |
041 | _ | _ | |a eng |
082 | _ | _ | |a 530 |
100 | 1 | _ | |a Kornreich, M. |b 0 |
245 | _ | _ | |a Composite bottlebrush mechanics: α-internexin fine-tunes neurofilament network properties. |
260 | _ | _ | |a London |c 2015 |b Royal Soc. of Chemistry |
336 | 7 | _ | |a article |2 DRIVER |
336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1508498497_28086 |2 PUB:(DE-HGF) |
336 | 7 | _ | |a ARTICLE |2 BibTeX |
336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
520 | _ | _ | |a Neuronal 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. |
536 | _ | _ | |a 312 - Functional and structural genomics (POF3-312) |0 G:(DE-HGF)POF3-312 |c POF3-312 |f POF III |x 0 |
588 | _ | _ | |a Dataset connected to CrossRef, PubMed, |
650 | _ | 7 | |a Intermediate Filament Proteins |2 NLM Chemicals |
650 | _ | 7 | |a Neurofilament Proteins |2 NLM Chemicals |
650 | _ | 7 | |a Recombinant Proteins |2 NLM Chemicals |
650 | _ | 7 | |a alpha-internexin |2 NLM Chemicals |
650 | _ | 7 | |a Hydrogel |0 25852-47-5 |2 NLM Chemicals |
700 | 1 | _ | |a Malka-Gibor, E. |b 1 |
700 | 1 | _ | |a Laser-Azogui, A. |b 2 |
700 | 1 | _ | |a Doron, O. |b 3 |
700 | 1 | _ | |a Herrmann, Harald |0 P:(DE-He78)7892a89fee19b8e3912c7423d660765d |b 4 |u dkfz |
700 | 1 | _ | |a Beck, R. |b 5 |
773 | _ | _ | |a 10.1039/C5SM00662G |g Vol. 11, no. 29, p. 5839 - 5849 |0 PERI:(DE-600)2191476-X |n 29 |p 5839 - 5849 |t Soft matter |v 11 |y 2015 |x 1744-6848 |
909 | C | O | |o oai:inrepo02.dkfz.de:126901 |p VDB |
910 | 1 | _ | |a Deutsches Krebsforschungszentrum |0 I:(DE-588b)2036810-0 |k DKFZ |b 4 |6 P:(DE-He78)7892a89fee19b8e3912c7423d660765d |
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914 | 1 | _ | |y 2015 |
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980 | _ | _ | |a I:(DE-He78)B065-20160331 |
980 | _ | _ | |a UNRESTRICTED |
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