Are the conserved sequences in segment 1 of gelsolin important for binding actin? - Wikidata - wikimedia - TriplyDB

Are the conserved sequences in segment 1 of gelsolin important for binding actin?

Are the conserved sequences in segment 1 of gelsolin important for binding actin?

http://www.wikidata.org/entity/Q43108239

about

The Drosophila melanogaster flightless-I gene involved in gastrulation and muscle degeneration encodes gelsolin-like and leucine-rich repeat domains and is conserved in Caenorhabditis elegans and humans Developmentally essential protein flightless I is a nuclear receptor coactivator with actin binding activity Molecular basis for the dual function of Eps8 on actin dynamics: bundling and capping The structure of nonvertebrate actin: Implications for the ATP hydrolytic mechanism The actin binding domain of ACF7 binds directly to the tetratricopeptide repeat domains of rapsyn.The COOH terminus of the c-Abl tyrosine kinase contains distinct F- and G-actin binding domains with bundling activity.Dominant negative mutation in cell surface beta 1,4-galactosyltransferase inhibits cell-cell and cell-matrix interactions A gelsolin-related protein from lobster muscle: cloning, sequence analysis and expression.Recruitment of the SWI/SNF chromatin remodeling complex to steroid hormone-regulated promoters by nuclear receptor coactivator flightless-I.Gelsolin: the tail of a molecular gymnast.DeActs: genetically encoded tools for perturbing the actin cytoskeleton in single cells.Evidence for functional homology in the F-actin binding domains of gelsolin and alpha-actinin: implications for the requirements of severing and capping.Separate functions of gelsolin mediate sequential steps of collagen phagocytosis.Identification of secreted and cytosolic gelsolin in Drosophila Definition of the EGTA-independent interface involved in the serum gelsolin-actin complex Solution structure of villin 14T, a domain conserved among actin-severing proteins.The Ca(2+)-induced conformational change of gelsolin is located in the carboxyl-terminal half of the molecule.Probing Dictyostelium severin structure and function by cross linking to actin.A gelsolin-like protein from Papaver rhoeas pollen (PrABP80) stimulates calcium-regulated severing and depolymerization of actin filaments.An actin-related protein from Dictyostelium discoideum is developmentally regulated and associated with mitochondria.Binding of gelsolin domain 2 to actin 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

P2860

Q24563766-FE21E303-8426-4F48-84EF-E031408414D7 Q24607485-EEF5F76A-4927-4138-8296-6A245AC06591 Q27324384-686CDFB3-8849-4CF2-A512-F7525D8438A2 Q27641158-4A2A7252-7649-4871-902C-08F7B84452D0 Q35792700-B846F421-1844-4163-A6B4-F310C3E2072C Q36233735-97D11C95-1FE5-468C-B08A-5B8723A5B0DF Q36383062-F11A9D26-C79E-4545-B9F5-6A27A85DE3DF Q36714977-D890CBA0-CC5F-4BF7-A1EF-B5B6E4336C04 Q37447611-7B814A31-8408-44FC-9797-8B6934D01330 Q38113172-CEA77E05-AA87-498C-BD4C-BDF0EC9F66A0 Q42172880-A99158F8-D3E3-4F6B-B47A-ACAA71A15F85 Q42183113-B2C9713D-0ECE-4458-B8BF-4ED702DFE7FF Q42590890-AA641426-6014-40A7-8859-F927BCDC3AA1 Q42770540-F82DE98A-B809-4CB4-9BB0-C2700C665642 Q42811310-BF75274D-AA58-49D7-9E3F-08115FABECF0 Q42843244-A1E0AFD6-FEB7-4B9A-9317-C7CCC3F0CBA2 Q43005982-EE963393-9C5B-4921-85D3-D503E7701278 Q44827377-52D57AAF-618A-4996-9BE0-359457AE0B7B Q47897294-74496590-5320-4E48-AC02-D17BDA669488 Q52209514-BC90F968-F0F9-44E0-AB06-EA75537093EE Q56593562-94625143-D58E-4CAA-BC30-02AD105FA07A Q57601970-36E16309-6DA6-401C-AECC-5F5D195FAD46

P2860

Are the conserved sequences in segment 1 of gelsolin important for binding actin?

http://www.wikidata.org/entity/Q43108239

description

1992 nî lūn-bûn

@nan

1992年の論文

@ja

1992年学术文章

@wuu

1992年学术文章

@zh

1992年学术文章

@zh-cn

1992年学术文章

@zh-hans

1992年学术文章

@zh-my

1992年学术文章

@zh-sg

1992年學術文章

@yue

1992年學術文章

@zh-hant

name

Are the conserved sequences in segment 1 of gelsolin important for binding actin?

@en

Are the conserved sequences in segment 1 of gelsolin important for binding actin?

@nl

type

label

Are the conserved sequences in segment 1 of gelsolin important for binding actin?

@en

Are the conserved sequences in segment 1 of gelsolin important for binding actin?

@nl

prefLabel

Are the conserved sequences in segment 1 of gelsolin important for binding actin?

@en

Are the conserved sequences in segment 1 of gelsolin important for binding actin?

@nl

P1433

Q43108239-AEE41C57-90D4-48A9-AFF7-EEDFEB0ADBEC

P1476

Q43108239-A100C189-6F01-4B03-8C11-AAE31C28E1EA

P2093

Q43108239-A2AEBB53-B17D-45CC-904B-ECF0F66137F8

Q43108239-A480E12D-0ABB-43C1-A197-94FBF7714724

Q43108239-AD818C20-7AA4-487B-9625-EDFAA0663DEB

P2860

Q43108239-141422C5-8B3A-466B-8001-0449A94B7BFD

Q43108239-1AF89B9E-1E71-40DA-B34D-44B30D5760E6

Q43108239-20DB39EA-874A-46C0-B712-A1EA3D42B84C

Q43108239-28FB78AF-C1F2-447A-93D1-461C74BBD7C6

Q43108239-3D8E933C-53CD-4585-9C50-B809852D1C80

Q43108239-3E39B8E3-2A88-4EE2-A030-8F47BA8135E0

Q43108239-40D6B7CC-6864-4FA2-BF9C-6E797A2737D8

Q43108239-4B1998B6-E772-45E2-BEC5-79E1D8D8BF28

Q43108239-4E225CE0-6541-4560-AA87-4B948C404CA6

Q43108239-51C35923-A121-4BE4-BB26-AFC8833B4324

P304

Q43108239-892A3810-CEBD-4719-972C-E448E89C241C

P31

Q43108239-7498A686-651A-4E65-B0A7-A645CB0E6147

P356

Q43108239-70D83BAD-C7EF-45F7-B26B-6EFB40BEA33B

P407

Q43108239-6C05AC5D-1E99-4032-A35B-FF9E6615A24D

P433

Q43108239-77E19E47-70AF-439A-9DAB-8CBD23668E55

P478

Q43108239-B3BE1AE4-E629-41F1-B477-B38E25959964

P577

Q43108239-541B2E5B-D527-4551-B815-19E02EF97A79

P5875

Q43108239-67CE4119-748D-402D-8C2F-BEDBD4C21459

P698

Q43108239-4CF3B91A-8A01-440A-BC02-1B527AF22148

P932

Q43108239-5E20B060-971A-47FD-9BAC-3249BABBE546

P356

P1433

Journal of Cell Biology

P1476

Are the conserved sequences in segment 1 of gelsolin important for binding actin?

@en

P2093

Pope B

http://www.w3.org/2001/XMLSchema#string

Way M

http://www.w3.org/2001/XMLSchema#string

Weeds AG

http://www.w3.org/2001/XMLSchema#string

P2860

Sequence of human villin: a large duplicated domain homologous with other actin-severing proteins and a unique small carboxy-terminal domain related to villin specificity

Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain

Villin sequence and peptide map identify six homologous domains

Atomic structure of the actin:DNase I complex

Nucleotide sequence of pig plasma gelsolin. Comparison of protein sequence with human gelsolin and other actin-severing proteins shows strong homologies and evidence for large internal repeats

pH-induced denaturation of proteins: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme

Atomic model of the actin filament

Mbh 1: a novel gelsolin/severin-related protein which binds actin in vitro and exhibits nuclear localization in vivo.

Destrin, a mammalian actin-depolymerizing protein, is closely related to cofilin. Cloning and expression of porcine brain destrin cDNA.

The F-actin capping proteins of Physarum polycephalum: cap42(a) is very similar, if not identical, to fragmin and is structurally and functionally very homologous to gelsolin; cap42(b) is Physarum actin.

P304

1135-1143

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1083/JCB.116.5.1135

http://www.w3.org/2001/XMLSchema#string

P407

P433

5

http://www.w3.org/2001/XMLSchema#string

P478

116

http://www.w3.org/2001/XMLSchema#string

P577

1992-03-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

273808897

http://www.w3.org/2001/XMLSchema#string

P698

1310993

http://www.w3.org/2001/XMLSchema#string

P932

2289352

http://www.w3.org/2001/XMLSchema#string