About: Peptides from the Conserved Ends of the Rod Domain of Desmin Disassemble Intermediate Filaments and Reveal Unexpected Structural Features: A Circular Dichroism, Fourier Transform Infrared, and Electron Microscopic Study

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About: Peptides from the Conserved Ends of the Rod Domain of Desmin Disassemble Intermediate Filaments and Reveal Unexpected Structural Features: A Circular Dichroism, Fourier Transform Infrared, and Electron Microscopic Study Goto Sponge NotDistinct Permalink

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rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в травні 1993 (uk) article scientifique publié en 1993 (fr) im Mai 1993 veröffentlichter wissenschaftlicher Artikel (de) 1993 മെയ് 1നു പ്രസിദ്ധീകരിച്ച ശാസ്ത്രീയ ലേഖനം (ml)
publication date	wds:Q56936623-E6A35346-FAC5-44F7-A08C-B9CEEC81A4BA
publication date	1993-05-01 00:00:00Z (xsd:dateTime)
author name string	wds:Q56936623-15F629E8-157F-49C7-9202-6E0697423829 wds:Q56936623-41A8AA0E-0A2C-4CDC-BEBD-80F65D5264FD wds:Q56936623-698AC21C-7E05-4A16-8A3B-C7251EB58A18
author name string	Klaus Weber Jürgen Schünemann Norbert Geisler
rdfs:label	Peptides from the Conserved Ends of the Rod Domain of Desmin Disassemble Intermediate Filaments and Reveal Unexpected Structural Features: A Circular Dichroism, Fourier Transform Infrared, and Electron Microscopic Study (en) Peptides from the Conserved Ends of the Rod Domain of Desmin Disassemble Intermediate Filaments and Reveal Unexpected Structural Features: A Circular Dichroism, Fourier Transform Infrared, and Electron Microscopic Study (nl)
skos:prefLabel	Peptides from the Conserved Ends of the Rod Domain of Desmin Disassemble Intermediate Filaments and Reveal Unexpected Structural Features: A Circular Dichroism, Fourier Transform Infrared, and Electron Microscopic Study (en) Peptides from the Conserved Ends of the Rod Domain of Desmin Disassemble Intermediate Filaments and Reveal Unexpected Structural Features: A Circular Dichroism, Fourier Transform Infrared, and Electron Microscopic Study (nl)
name	Peptides from the Conserved Ends of the Rod Domain of Desmin Disassemble Intermediate Filaments and Reveal Unexpected Structural Features: A Circular Dichroism, Fourier Transform Infrared, and Electron Microscopic Study (en) Peptides from the Conserved Ends of the Rod Domain of Desmin Disassemble Intermediate Filaments and Reveal Unexpected Structural Features: A Circular Dichroism, Fourier Transform Infrared, and Electron Microscopic Study (nl)
author	wds:Q56936623-459FB66E-AD48-4796-87FE-DA1F4FB5986B
author	Thomas Heimburg
title	wds:Q56936623-7B195FD5-688C-4E93-ABAE-C0929DED905C
title	Peptides from the Conserved Ends of the Rod Domain of Desmin Disassemble Intermediate Filaments and Reveal Unexpected Structural Features: A Circular Dichroism, Fourier Transform Infrared, and Electron Microscopic Study (en)
page(s)	wds:Q56936623-4FA7C16F-8E89-4641-9C99-BFBA9888CC3D
page(s)	205-214
instance of	wds:Q56936623-3234173D-94F2-4EFB-9329-CD1436BEBDE5
instance of	scholarly article
PubMed ID	wds:Q56936623-02195BFB-5472-456A-84AE-6D4AEF7911F6
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8373701
PubMed ID	8373701
published in	wds:Q56936623-1BD87BAE-C316-47B0-8C5E-5A1D12923C8B
published in	Journal of Structural Biology
issue	wds:Q56936623-3D9F7FAB-888E-4A66-8245-439CEA5112C5
volume	wds:Q56936623-7A58FB25-C811-4CDE-A2F9-1C338C21EDE1
issue	3
volume	110
DOI	wds:Q56936623-F8F5239A-BD73-47D6-8096-C8549F70141F
DOI	http://dx.doi.org/10.1006/JSBI.1993.1023
DOI	10.1006/JSBI.1993.1023
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q56936623
is cites work of	Primary sequence, secondary structure, gene structure, and assembly properties suggests that the lens-specific cytoskeletal protein filensin represents a novel class of intermediate filament protein Functional complexity of intermediate filament cytoskeletons: from structure to assembly to gene ablation Domains of tau protein, differential phosphorylation, and dynamic instability of microtubules Head and rod 1 interactions in vimentin: identification of contact sites, structure, and changes with phosphorylation using site-directed spin labeling and electron paramagnetic resonance Structure of tau protein and assembly into paired helical filaments A novel mutation in the helix termination motif of keratin K12 in a US family with Meesmann corneal dystrophy Involvement of the lamin rod domain in heterotypic lamin interactions important for nuclear organization Responsive gels formed by the spontaneous self-assembly of peptides into polymeric beta-sheet tapes A novel mutation in the keratin 13 gene causing oral white sponge nevus Laryngeal involvement in the Dowling-Meara variant of epidermolysis bullosa simplex with keratin mutations of severely disruptive potential.
is cites work of	wds:Q24329143-318E3D6F-1535-4E72-BA62-EA1C05ADE6B5 wds:Q58859919-48155071-3EFC-4824-890F-47FB27340B84 wds:Q33971326-CECC1EC5-803A-4C30-B752-ED4A85908D70 wds:Q40665458-45C1A2E1-8E82-4C3D-B877-FC8CC1EE71EE wds:Q42736271-884FC95D-C3A6-4A59-8BF1-3D293F236E8F wds:Q35086651-1B0EC0B7-F53C-4507-947A-6A194AAD4A2A wds:Q28191257-B15D2593-4A31-4D1B-A29D-CEE70D7B61E9 wds:Q34419528-01560260-7892-4E7A-AECA-2DE774E34052 wds:Q42485419-3A735264-9000-4AAA-99F8-9A8078509D95 wds:Q36360354-96B3F211-FC30-4615-B843-1808EC91B90E

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