The Dictyostelium gelation factor shares a putative actin binding site with alpha-actinins and dystrophin and also has a rod domain containing six 100-residue motifs that appear to have a cross-beta conformation
about
Cloning and characterization of a novel RING finger protein that interacts with class V myosinsMyozenin: an alpha-actinin- and gamma-filamin-binding protein of skeletal muscle Z linesHuman beta-filamin is a new protein that interacts with the cytoplasmic tail of glycoprotein IbalphaHuman endothelial actin-binding protein (ABP-280, nonmuscle filamin): a molecular leaf springFimbrin is a homologue of the cytoplasmic phosphoprotein plastin and has domains homologous with calmodulin and actin gelation proteinsThe repeating segments of the F-actin cross-linking gelation factor (ABP-120) have an immunoglobulin-like foldFilamin repeat segments required for photosensory signalling in Dictyostelium discoideum.Interaptin, an actin-binding protein of the alpha-actinin superfamily in Dictyostelium discoideum, is developmentally and cAMP-regulated and associates with intracellular membrane compartments.Filamins in mechanosensing and signaling.Expression patterns of cell-type-specific genes in Dictyostelium.Genetic analysis of the fimbrin-actin binding interaction in Saccharomyces cerevisiaeA cell number-counting factor regulates the cytoskeleton and cell motility in Dictyostelium.Mechanical perturbation elicits a phenotypic difference between Dictyostelium wild-type cells and cytoskeletal mutants.Cell-substrate interactions and locomotion of Dictyostelium wild-type and mutants defective in three cytoskeletal proteins: a study using quantitative reflection interference contrast microscopy.The spectrin skeleton: from red cells to brainCell type-specific filamin complex regulation by a novel class of HECT ubiquitin ligase is required for normal cell motility and patterning.The murine mutation jaundiced is caused by replacement of an arginine with a stop codon in the mRNA encoding the ninth repeat of beta-spectrin.Sequence similarity of the amino-terminal domain of Drosophila beta spectrin to alpha actinin and dystrophinA Dictyostelium mutant lacking an F-actin cross-linking protein, the 120-kD gelation factorGenetic deletion of ABP-120 alters the three-dimensional organization of actin filaments in Dictyostelium pseudopods.Dictyostelium discoideum cells lacking the 34,000-dalton actin-binding protein can grow, locomote, and develop, but exhibit defects in regulation of cell structure and movement: a case of partial redundancy.Cloning and sequencing of rat plectin indicates a 466-kD polypeptide chain with a three-domain structure based on a central alpha-helical coiled coil.Targeted disruption of the ABP-120 gene leads to cells with altered motility.TaWRKY68 responses to biotic stresses are revealed by the orthologous genes from major cereals.Interaction of a Dictyostelium member of the plastin/fimbrin family with actin filaments and actin-myosin complexes.The identification and characterisation of an actin-binding site in alpha-actinin by mutagenesis.Analysis of the actin-binding domain of alpha-actinin by mutagenesis and demonstration that dystrophin contains a functionally homologous domain.Cap100, a novel phosphatidylinositol 4,5-bisphosphate-regulated protein that caps actin filaments but does not nucleate actin assembly.Evidence for functional homology in the F-actin binding domains of gelsolin and alpha-actinin: implications for the requirements of severing and capping.CP250, a novel acidic coiled-coil protein of the Dictyostelium centrosome, affects growth, chemotaxis, and the nuclear envelope.A novel Amoeba proteus 120 kDa actin-binding protein with only 1 filamin repeat and a coiled-coil region.A beta-spectrin isoform from Drosophila (beta H) is similar in size to vertebrate dystrophin.The Ca(2+)-binding domains in non-muscle type alpha-actinin: biochemical and genetic analysis
P2860
Q22010202-0EA7C431-54AE-4FBD-9B5B-470AB622E7E8Q24290814-8B9C494D-5E38-48F5-836A-E4B177E4D473Q24311451-C2BC808B-61D6-47D8-BD34-B0927D02B998Q24314875-59CA9E17-C996-4E1C-8A4B-1F5B622765E3Q24678811-111D0344-F1EE-469F-B6E8-C1646D967143Q27738361-8CC77038-1E27-47DD-8431-B3A2981DABB3Q30838101-FD6B966C-A55A-4C07-B8E9-A123B0621749Q32040709-2CAFECE9-A03A-4870-B871-D97AA2FAFF19Q33900830-51AD3CC4-6BB5-44E8-AB11-EF7D2FFCC8DEQ33946660-B8DFA704-6BE7-44F2-8F84-D62CAD27E87DQ33965158-3435C9D9-2908-4E6D-A0A9-FCC965C27020Q34009399-63FF2D45-EA95-49FA-B77B-E287562BB9C8Q34017280-8CBA3DD5-34DE-40BD-BC5A-863D30EF56DFQ34128776-D2E9F86C-AB21-4C85-9323-FC04716038B9Q34186672-ACABFA7C-25CC-42C9-8ADF-DEEE07B05F37Q34707679-2A605FFF-D4EE-463E-B979-A39504F6579CQ35833485-05961842-9D70-495A-AEF6-D1229F871BCFQ35894823-AFCD893A-7235-4F90-8A4C-86F1E14D06BFQ36223652-DECAA262-51C8-4EB6-9DDB-FD1406C43A4BQ36235376-6E8BEA63-B779-4506-9960-E58846C255CEQ36256894-559F4F78-11AC-44F1-AD7A-54F98AB6426AQ36529960-76762203-D956-439A-8E6C-CB448103D51CQ36531025-C36030A3-66C6-4939-96BC-79B8EF9684F7Q37644416-BEC6E719-7E2B-4F68-A6DC-19D432EFA09EQ40243219-82ADABBD-5B78-4210-B668-7F2835B318DEQ41125964-A933B460-B52D-48D0-B2EB-FA0AB6CDD4F4Q41637266-254C460B-E9C1-42FB-8AE3-6EDFF6CBC4B5Q42016074-C1A7EF6C-2C03-429F-98D1-128931AD1742Q42183113-1660C954-77F1-40CF-B21F-11A6612C9278Q42583891-1912F86C-7FBF-4428-B3DC-80D8D96258EEQ42618466-7EB8BF33-4CEF-410B-A1D5-56110A9E0EDCQ42762897-DFE41D2F-A84C-4066-A560-DD69EBD249FFQ42769630-67136D75-AFF1-49B5-B762-DDA644939DFA
P2860
The Dictyostelium gelation factor shares a putative actin binding site with alpha-actinins and dystrophin and also has a rod domain containing six 100-residue motifs that appear to have a cross-beta conformation
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
1989年论文
@zh
1989年论文
@zh-cn
name
The Dictyostelium gelation fac ...... have a cross-beta conformation
@ast
The Dictyostelium gelation fac ...... have a cross-beta conformation
@en
type
label
The Dictyostelium gelation fac ...... have a cross-beta conformation
@ast
The Dictyostelium gelation fac ...... have a cross-beta conformation
@en
prefLabel
The Dictyostelium gelation fac ...... have a cross-beta conformation
@ast
The Dictyostelium gelation fac ...... have a cross-beta conformation
@en
P2093
P2860
P356
P1476
The Dictyostelium gelation fac ...... have a cross-beta conformation
@en
P2093
P2860
P304
P356
10.1083/JCB.109.2.607
P407
P577
1989-08-01T00:00:00Z