About: The isolated sixth gelsolin repeat and headpiece domain of villin bundle F-actin in the presence of calcium and are linked by a 40-residue unstructured sequence.

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About: The isolated sixth gelsolin repeat and headpiece domain of villin bundle F-actin in the presence of calcium and are linked by a 40-residue unstructured sequence. Goto Sponge NotDistinct Permalink

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scientific article published on 05 June 2007

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rdf:type	Item
description	videnskabelig artikel (da) article científic (ca) articolo scientifico (it) artigo científico (pt) bilimsel makale (tr) vedecký článok (sk) vetenskaplig artikel (sv) vědecký článek (cs) wetenschappelijk artikel (nl) wissenschaftlicher Artikel (de) научни чланак (sr) article scientifique (fr) artículu científicu espublizáu en 2007 (ast) наукова стаття, опублікована в червні 2007 (uk) scientific article published on 05 June 2007 (en) مقالة علمية نشرت في 05 يونيو 2007 (ar)
publication date	wds:Q37171330-8F30A580-1A02-48A9-8946-12FA1CB7A866
publication date	2007-06-05 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q37171330-CBFBE134-1489-4355-9181-743F0876FC7B
language of work or name	English
cites work	wds:Q37171330-00E76B7C-B9F5-4835-BB0D-31B45EC221FB wds:Q37171330-07E414D1-95CF-43EC-97DC-6EC2BBAD9C7C wds:Q37171330-0C6C0407-CFEC-4226-AA93-639AAAC2EAB5 wds:Q37171330-0CF789AC-0B79-40A4-AD3C-CF19D8423248 wds:Q37171330-0EC39054-05D3-4612-8B01-A4910AE33974 wds:Q37171330-11ECC075-1A3D-4095-BC20-124F326103C4 wds:Q37171330-132B1FA2-FA6C-46E1-9AE0-7D0B59ED4424 wds:Q37171330-16D81074-5AC4-46A8-99B9-9C28B64596D7 wds:Q37171330-205C2FC4-E346-487A-ACC7-8FB64C04B849 wds:Q37171330-22E8052C-602D-4F29-A358-91289C86B580 wds:Q37171330-2652467B-96BE-4910-9904-28AFF589140B wds:Q37171330-48BDCB72-3670-48CE-8380-617BFF934AA3 wds:Q37171330-4A5BEDD4-7E1C-4377-AC58-CAD79A2E0A20 wds:Q37171330-4B969F97-C9D9-43F8-B45B-1C04CEDEB4B8 wds:Q37171330-64565342-7E65-4646-926B-5BEFBA63A883 wds:Q37171330-6EB1C492-9259-4C15-810E-C885AA3CE181 wds:Q37171330-73E968D6-4961-4D39-8FF0-84861EF90EA1 wds:Q37171330-7A3919FD-9440-4626-9413-F4FFCC80A0F5 wds:Q37171330-7E59AE8E-E658-4530-A459-6CE61AF3A82E wds:Q37171330-7E705F87-E985-467C-A8DE-5F114DC93505 wds:Q37171330-801E8DB9-9FD2-4707-BD10-0F0F01E6A024 wds:Q37171330-8061A711-FDBD-437A-913B-3D75B9B293EC wds:Q37171330-8309FF22-67F1-4D8D-BBD2-2961E03EDB5C wds:Q37171330-8B09CFE4-8C56-41F5-874F-12E6D1E4E4C2 wds:Q37171330-9B4D6508-9D50-4130-AAE2-DA4B2529849F wds:Q37171330-A624A9B7-6077-420E-B99C-223629E063C7 wds:Q37171330-A9E6D784-49C7-41E5-B89B-8909EBC84584 wds:Q37171330-B93CDE04-60C8-4089-A1BB-EC4B538D37D0 wds:Q37171330-BBF646E0-C273-4455-8EC3-ED5BB912D16E wds:Q37171330-CA5ECEBB-27E3-4BCD-84F3-9C73CBF0F906 wds:Q37171330-DE5323EC-9DEE-4868-960E-E2208339B5AA wds:Q37171330-E0BDAFE1-C659-4B4C-8D76-CD0C002519C0 wds:Q37171330-F03F2C5E-6191-4121-A6DB-0073CDAE582C wds:Q37171330-F04BC029-2CB7-4689-9F36-947850F69FCE wds:Q37171330-FEEF0470-A8CA-4BDA-B5A7-67A9E5656B84
cites work	FAST-Modelfree: a program for rapid automated analysis of solution NMR spin-relaxation data NMRPipe: a multidimensional spectral processing system based on UNIX pipes A method for efficient isotopic labeling of recombinant proteins Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins. Cloning of human erythroid dematin reveals another member of the villin family Characterisation of the F-actin binding domains of villin: classification of F-actin binding proteins into two groups according to their binding sites on actin The villin-like protein encoded by the Drosophila quail gene is required for actin bundle assembly during oogenesis. Spectroscopic Determination of Tryptophan and Tyrosine in Proteins* Purification of muscle actin 1H, 13C and 15N chemical shift referencing in biomolecular NMR Isoform cloning, actin binding, and chromosomal localization of human erythroid dematin, a member of the villin superfamily NMR View: A computer program for the visualization and analysis of NMR data Protein backbone angle restraints from searching a database for chemical shift and sequence homology Supervillin (p205): A novel membrane-associated, F-actin-binding protein in the villin/gelsolin superfamily Pieces in the actin-severing protein puzzle Structure of severin domain 2 in solution Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain The crystal structure of plasma gelsolin: implications for actin severing, capping, and nucleation Solution structures of the C-terminal headpiece subdomains of human villin and advillin, evaluation of headpiece F-actin-binding requirements Villin sequence and peptide map identify six homologous domains NMR structure of an F-actin-binding "headpiece" motif from villin Villin is a major protein of the microvillus cytoskeleton which binds both G and F actin in a calcium-dependent manner Calcium control of microfilaments: uncoupling of the F-actin-severing and -bundling activity of villin by limited proteolysis in vitro Functional comparison of villin and gelsolin. Effects of Ca2+, KCl, and polyphosphoinositides Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme In vivo, villin is required for Ca(2+)-dependent F-actin disruption in intestinal brush borders Villin function in the organization of the actin cytoskeleton. Correlation of in vivo effects to its biochemical activities in vitro Effect of librational motion on fluorescence depolarization and nuclear magnetic resonance relaxation in macromolecules and membranes Solution structure of villin 14T, a domain conserved among actin-severing proteins Assignment of the side-chain proton and carbon-13 resonances of interleukin-1.beta. using double- and triple-resonance heteronuclear three-dimensional NMR spectroscopy High-resolution crystal structures of villin headpiece and mutants with reduced F-actin binding activity Identification of a functional switch for actin severing by cytoskeletal proteins In vivo analysis of functional domains from villin and gelsolin Gelsolin Domains 4–6 in Active, Actin-free Conformation Identifies Sites of Regulatory Calcium Ions Refined structure of villin 14T and a detailed comparison with other actin-severing domains
author name string	wds:Q37171330-5B2E0C13-8DA8-41A2-AD50-9F0034B3DDCE wds:Q37171330-6CB17540-E1ED-4B9F-8016-A4F3DF75CCEE
author name string	David W Hoyt Serge L Smirnov
rdfs:label	The isolated sixth gelsolin repeat and headpiece domain of villin bundle F-actin in the presence of calcium and are linked by a 40-residue unstructured sequence. (en) The isolated sixth gelsolin repeat and headpiece domain of villin bundle F-actin in the presence of calcium and are linked by a 40-residue unstructured sequence. (nl) The isolated sixth gelsolin repeat and headpiece domain of villin bundle F-actin in the presence of calcium and are linked by a 40-residue unstructured sequence. (ast)
skos:prefLabel	The isolated sixth gelsolin repeat and headpiece domain of villin bundle F-actin in the presence of calcium and are linked by a 40-residue unstructured sequence. (en) The isolated sixth gelsolin repeat and headpiece domain of villin bundle F-actin in the presence of calcium and are linked by a 40-residue unstructured sequence. (nl)

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