-
1
-
-
0025685347
-
Effect of Filamin and Controlled Linear Shear on the Microheterogeneity of F-Actin/Gelsolin Gels
-
of special interest
-
(1990)
Cell Motil Cytoskeleton
, vol.17
, pp. 236-249
-
-
Cortese1
Frieden2
-
2
-
-
0025292782
-
Brownian Motion of Inert Tracer Macromolecules in Polymerized and Spontaneously Bundled Mixtures of Actin and Filamin
-
(1990)
J Cell Biol
, vol.110
, pp. 1645-1654
-
-
Hou1
Luby-Phelps2
Lanni3
-
3
-
-
0027162413
-
Affinity of Alpha-Actinin for Actin Determines the Structure and Mechanical Properties of Actin Filament Gels
-
of outstanding interest, α-Actinin induces either bundles or isotropic gels of actin depending on their relative concentrations. A computer model is presented that predicts the threshold for α-actinin to bundle actin filaments on the basis of four variables.
-
(1993)
Biophys J
, vol.65
, pp. 205-214
-
-
Wachsstock1
Schwarz2
Pollard3
-
7
-
-
0021339817
-
Assembly-Disassembly of Actin Bundles in Starfish Oocytes: An Analysis of Actin-Associated Proteins in the Isolated Cortex
-
(1984)
Dev Biol
, vol.101
, pp. 263-273
-
-
Otto1
Schroeder2
-
8
-
-
0027424655
-
Fascin, an Echinoid Actin-Bundling Protein, is a Homolog of the Drosophila singed Gene Product
-
of outstanding interest, A cDNA encoding sea urchin fascin was cloned and sequenced. The predicted amino acid sequence is highly similar to that for the singed gene in Drosophila. No similarity to the actin-binding domains in other crosslinking proteins is apparent.
-
(1993)
Proc Natl Acad Sci USA
, vol.90
, pp. 9115-9119
-
-
Bryan1
Edwards2
Matsudaira3
Otto4
Wulfkuhle5
-
9
-
-
0014115449
-
The Fine Structure of Developing Bristles in Wild Type and Mutant Drosophila melanogaster
-
(1967)
J Morphol
, vol.122
, pp. 367-380
-
-
Overton1
-
11
-
-
0022535995
-
Intracellular Localization of the 55-kD Actin-Bundling Protein in Cultured Cells: Spatial Relationships with Actin, Alpha-Actinin, Tropomyosin, and Fimbrin
-
(1986)
J Cell Biol
, vol.103
, pp. 631-640
-
-
Yamashiro-Matsumura1
Matsumura2
-
12
-
-
0021759450
-
Isolation and Characterization of a 30,000-Dalton Calcium-Sensitive Actin Crosslinking Protein from Dictyostelium discoideum
-
(1984)
J Biol Chem
, vol.259
, pp. 4514-4520
-
-
Fechheimer1
Taylor2
-
15
-
-
0026645917
-
Inhibition of Actin Filament Depolymerization by the Dictyostelium 30,000-D Actin-Bundling Protein
-
of special interest, The 30 kDa actin bundling protein inhibits the rate of actin depolymerization at both ends of the actin filament but has little effect on actin assembly. This inhibition occurs even under conditions in which the 30 kDa protein is not crosslinking actin filaments, which suggests that actin-crosslinking proteins may stabilize actin filaments, preventing their disassembly.
-
(1992)
J Cell Biol
, vol.119
, pp. 559-567
-
-
Zigmond1
Furukawa2
Fechheimer3
-
16
-
-
0027397491
-
2+-Regulated Actin Cross-Linking but Lacks Bundling Activity
-
2+-regulated actin-crosslinking activity; however, it canot bundle actin filaments, suggesting that the missing regions are critical for this function.
-
(1993)
J Cell Biol
, vol.120
, pp. 1169-1176
-
-
Fechheimer1
Furukawa2
-
17
-
-
0025637073
-
Localization, Expression, Evolutionary Conservation, and Structure of the 30,000 Dalton Actin Bundling Protein of Dictyostelium discoideum
-
(1990)
Dev Genetics
, vol.11
, pp. 362-368
-
-
Furukawa1
Fechheimer2
-
20
-
-
0023188266
-
The Dictyostelium discoideum 30,000-Dalton Protein is an Actin Filament-Bundling Protein that is Selectively Present in Filopodia
-
(1987)
J Cell Biol
, vol.104
, pp. 1539-1551
-
-
Fechheimer1
-
21
-
-
0002036804
-
The Dictyostelium discoideum 30,000 Dalton Protein Contributes to Phagocytosis
-
of special interest, The 30 kDa protein, along with actin, is localized around the phagocytic cup during its formation. An antibody that blocks the interaction between actin and the 30 kDa protein inhibits phagocytosis when it is introduced into cells, suggesting that the bundling protein is required for the process.
-
(1992)
Protoplasma
, vol.169
, pp. 18-27
-
-
Furukawa1
Butz2
Fleischmann3
Fechheimer4
-
23
-
-
0026773096
-
An actin-Binding Site Containing a Conserved Motif of Charged Amino Acid Residues is Essential for the Morphogenic Effect of Villin
-
of outstanding interest, Cells transfected with cDNAs encoding villin develop microvilli on their upper surface and have altered organization of the actin-based cytoskeleton. This reorganization of actin required an actin-binding site at the carboxy terminus; this site must contain the sequence Leu-Leu-Glu-Leu. Peptides containing this sequence nucleate actin filament assembly.
-
(1992)
Cell
, vol.70
, pp. 81-92
-
-
Friederich1
Vancompernolle2
Huet3
Goethals4
Finidori5
Vandekerckhove6
Louvard7
-
24
-
-
0027222064
-
Villin-induced growth of microvilli is reversibly inhibited by cytochalasin D.
-
••]). These results suggest that actin filaments that are prevented from binding the plasma membrane, in this case by cytochalasin D, cannot participate in the morphogenesis of microvilli.
-
(1993)
J Cell Sci
, vol.105
, pp. 765-775
-
-
Friederich1
Kreis2
Louvard3
-
26
-
-
0025895403
-
Sea Urchin Egg Villin: Identification of Villin in a Non-Epithelial Cell from an Invertebrate Species
-
(1991)
J Cell Sci
, vol.100
, pp. 61-71
-
-
Wang1
Bonder2
-
28
-
-
0026783523
-
Cap100, a Novel Phosphatidylinositol 4,5-Biphosphate-Regulated Protein that Caps Actin Filaments but does not Nucleate Actin Assembly
-
2+ concentration but is inhibited in the presence of phosphatidylinositol 4,5-bisposphate.
-
(1992)
Cell Motil Cytoskeleton
, vol.23
, pp. 133-144
-
-
Hofmann1
Eichinger2
André3
Rieger4
Schleicher5
-
29
-
-
0027244831
-
Cloning of Human Erythroid Dematin Reveals Another Member of the Villin Family
-
of outstanding interest, The primary sequence of dematin, an actin-bundling protein originally identified in human erythrocytes, is shown to encode a region homologous to the headpiece of villin. Dematin transcripts are present in a variety of cells besides reticulocytes.
-
(1993)
Proc Natl Acad Sci USA
, vol.90
, pp. 6651-6655
-
-
Rana1
Ruff2
Maalouf3
Speicher4
Chishti5
-
31
-
-
0025091625
-
Fimbrin is a Homologue of the Cytoplasmic of the Cytoplasmic Phosphoprotein Plastin and Has Domains Homologous with Calmodulin and Actin Gelation Proteins
-
(1990)
J Cell Biol
, vol.111
, pp. 1069-1079
-
-
De Arruda1
Watson2
Lin3
Leavitt4
Matsudaira5
-
32
-
-
0027324435
-
Fimbrin Localized to an Insoluble Cytoskeletal Fraction is Constitutively Phosphorylated on its Headpiece Domain in Adherent Macrophages
-
of special interest, Macrophages were fractionated into soluble, cytoskeletal and insoluble cytoskeletal fractions. Fimbrin phosphorylated on the head-piece domain is concentrated in the insoluble cytoskeletal fraction.
-
(1993)
Cell Motil Cytoskeleton
, vol.25
, pp. 223-233
-
-
Messier1
Shaw2
Chafel3
Matsudaira4
Mercurio5
-
33
-
-
0025983823
-
Requirement of Yeast Fimbrin for Actin Organization and Morphogenesis In Vivo
-
(1991)
Nature
, vol.354
, pp. 404-408
-
-
Adams1
Botstein2
Drubin3
-
34
-
-
0027195989
-
Unexpected Combinations of Null Mutations in Genes Encoding the Actin Cytoskeleton are Lethal in Yeast
-
of outstanding interest, Single null mutations in tropomyosin, fimbrin, actin-binding protein Abplp, and capping protein are not lethal and have relatively mild effects in yeast. Double null mutants of fimbrin and Abplp or fimbrin and capping protein have major effects on growth rates and can be lethal, whereas other double mutants for the proteins studied were not.
-
(1993)
Mol Biol Cell
, vol.4
, pp. 459-468
-
-
Adams1
Cooper2
Drubin3
-
35
-
-
0026593102
-
Redundancy in the Microfilament System: Abnormal Development of Dictyostelium Cells Lacking Two F-Actin Cross-Linking Proteins
-
(1992)
Cell
, vol.68
, pp. 53-62
-
-
Witke1
Schleicher2
Noegel3
-
37
-
-
0027416724
-
Further Characterization of the Alpha-Actinin-Actin Interface and Compararison with Filamin-Binding Sites on Actin
-
of outstanding interest, α-Actinin is shown to bind to two peptides of actin. These two segments are in subdomain 1 in close proximity and are thus proposed to comprise one binding site for α-actinin on actin.
-
(1993)
J Biol Chem
, vol.268
, pp. 5642-5648
-
-
Lebart1
Méjean2
Roustan3
Benyamin4
-
38
-
-
0026495427
-
Evidence for Functional Homology in the F-Actin Binding Domains of Gelsolin and Alpha-Actinin: Implications for the Requirements of Severing and Capping
-
2+-dependent severing.
-
(1992)
J Cell Biol
, vol.119
, pp. 835-842
-
-
Way1
Pope2
Weeds3
-
39
-
-
0027390673
-
Macrophage Alpha-Actinin is not a Calcium-Modulated Actin-Binding Protein
-
2+.
-
(1993)
Biochemistry
, vol.32
, pp. 363-374
-
-
Pacaud1
Harricane2
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