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.
about
Sequence of human villin: a large duplicated domain homologous with other actin-severing proteins and a unique small carboxy-terminal domain related to villin specificityVillin-like actin-binding proteins are expressed ubiquitously in ArabidopsisVillin sequence and peptide map identify six homologous domainsX-ray structures of isoforms of the actin-binding protein profilin that differ in their affinity for phosphatidylinositol phosphatesThree-dimensional solution structure of Acanthamoeba profilin-IIn vivo, villin is required for Ca(2+)-dependent F-actin disruption in intestinal brush bordersCharacterization of actin filament severing by actophorin from Acanthamoeba castellaniiMbh 1: a novel gelsolin/severin-related protein which binds actin in vitro and exhibits nuclear localization in vivo.Structure of the human villin gene.Murine adseverin (D5), a novel member of the gelsolin family, and murine adseverin are induced by interleukin-9 in T-helper lymphocytesPhysarum actin is phosphorylated as the actin-fragmin complex at residues Thr203 and Thr202 by a specific 80 kDa kinase.Isolation and characterization of cDNA encoding the alpha subunit of Cap Z(36/32), an actin-capping protein from the Z line of skeletal muscle.Structural analysis of an Echinococcus granulosus actin-fragmenting protein by small-angle x-ray scattering studies and molecular modelingA novel type of protein kinase phosphorylates actin in the actin-fragmin complex.Identification of critical functional and regulatory domains in gelsolinAcanthamoeba actin and profilin can be cross-linked between glutamic acid 364 of actin and lysine 115 of profilin.Xenopus actin depolymerizing factor/cofilin (XAC) is responsible for the turnover of actin filaments in Listeria monocytogenes tails.In vivo analysis of functional domains from villin and gelsolin.Radixin is a novel member of the band 4.1 family.Identification and characterization of the actin-binding motif of phostensinA gelsolin-related protein from lobster muscle: cloning, sequence analysis and expression.Regulatory role of the second gelsolin-like domain of Caenorhabditis elegans gelsolin-like protein 1 (GSNL-1) in its calcium-dependent conformation and actin-regulatory activities.The intron-containing gene for yeast profilin (PFY) encodes a vital functionPhototactic migration of Dictyostelium cells is linked to a new type of gelsolin-related protein.Identification of a region in segment 1 of gelsolin critical for actin binding.Gelsolin-related amyloidosis. Identification of the amyloid protein in Finnish hereditary amyloidosis as a fragment of variant gelsolin.A Dictyostelium mutant deficient in severin, an F-actin fragmenting protein, shows normal motility and chemotaxisExpression of human plasma gelsolin in Escherichia coli and dissection of actin binding sites by segmental deletion mutagenesis.Structural and functional variations in skeletal-muscle and scallop muscle actins.Control of actin filament length by phosphorylation of fragmin-actin complexIdentification of secreted and cytosolic gelsolin in DrosophilaDomain structure in actin-binding proteins: expression and functional characterization of truncated severin.Are the conserved sequences in segment 1 of gelsolin important for binding actin?
P2860
Q24293108-408B25C6-6B6A-4EDC-B51D-E2330A1E9BC3Q24555179-9F06FAC4-94E7-4555-A6DD-03773E2D1294Q24653949-61041D5B-B783-499E-966C-AC174596700EQ27730902-08D5685D-E3F3-45A7-897E-36BF28B73C7EQ27732049-755C5426-EB7C-42A9-AF3C-3B8D0CAA76B7Q28593765-447823C1-43A9-4B4F-8E1C-E48D6B407104Q33288000-5C79B4E3-07AB-4D0F-B34E-FAB37CDC6520Q33336043-44526251-CFFA-4E15-8BA9-15F11617AD4AQ33484104-57A76E5C-D025-4045-BFFA-3C9399BB821EQ33775199-F91B1618-BFEC-409E-BF1E-1D679CD23B59Q33938337-D433E4AF-53E0-4FF3-A54D-D1AE8CDF104FQ34294146-A2B7A42A-9F8D-460D-B6FA-878310DB4950Q34524620-8AF1845F-11A4-40F6-A370-916BF5013F30Q35910750-A8939F2B-8066-4F65-8C68-1113AE47D18FQ36220686-C81BB423-7601-4BCD-A55C-1EC3A5059115Q36221284-14427E1D-E1BC-41BC-96BC-794756B0A191Q36254640-A6DD726B-0106-4B01-94CB-103E47EDFB09Q36531081-23DC6947-452B-432C-BD19-6C59DEE5C7A6Q36532958-36D1BCB4-0393-4E7D-B0FA-BEE35406E56BQ36538341-D7CDE11C-83E9-45E7-8C5A-46F81ED713ECQ36714977-A119E096-FC18-4887-86E2-95DE2E1948EFQ36849236-B3A3B843-11D9-4486-84BF-9AECC43FD812Q36849872-B5ED3190-B462-49E5-A6D0-7C155725201FQ38329736-48A7980D-A1CC-4AEA-9146-43B936422E76Q38338042-C2A0245D-E0E5-4D78-921B-42ED6545E674Q40340220-8CAEEC03-D5A3-4A29-B1AF-E7737DBFEE1EQ41565554-3568E544-188C-4D5B-81C2-710DD5785C74Q41584348-CEB3BB08-9739-45DA-AAF6-987E652B43EAQ41903513-27D0F56A-03CF-4884-A927-AFED6E66A72DQ42762835-89A4436F-56CB-4844-845C-305FCFA4371CQ42770540-41BDFDE5-1407-45BD-BE98-E955EAC6A98CQ43107722-D7B503C4-3080-4CBF-9732-67F882E4628CQ43108239-1AF89B9E-1E71-40DA-B34D-44B30D5760E6
P2860
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.
description
1987 nî lūn-bûn
@nan
1987 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1987 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
name
The F-actin capping proteins o ...... n; cap42(b) is Physarum actin.
@ast
The F-actin capping proteins o ...... n; cap42(b) is Physarum actin.
@en
type
label
The F-actin capping proteins o ...... n; cap42(b) is Physarum actin.
@ast
The F-actin capping proteins o ...... n; cap42(b) is Physarum actin.
@en
prefLabel
The F-actin capping proteins o ...... n; cap42(b) is Physarum actin.
@ast
The F-actin capping proteins o ...... n; cap42(b) is Physarum actin.
@en
P2860
P1433
P1476
The F-actin capping proteins o ...... n; cap42(b) is Physarum actin.
@en
P2093
Vandekerckhove J
P2860
P304
P407
P577
1987-12-01T00:00:00Z