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Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2009, Volume 106, Issue 32, pp. 13341 - 13346
Formins are present in all eukaryotes and are essential for the creation of actin-based structures responsible for diverse cellular processes. Because... 
Cell growth | Phenotypes | Nucleation | Plant growth | Microfilaments | Profilins | Mosses | Actins | Plants | Plant cells | profilin | physcomitrella-patens | pollen-tube | cytokinesis | proteins | arp2/3 complex | fission yeast | homology-2 domain | tip growth | cable formation | RNAi | Profilin | Moss | Physcomitrella patens | Tip growth | FISSION YEAST | MULTIDISCIPLINARY SCIENCES | CABLE FORMATION | ARP2/3 COMPLEX | moss | CYTOKINESIS | HOMOLOGY-2 DOMAIN | PHYSCOMITRELLA-PATENS | POLLEN-TUBE | PROTEINS | Protein Structure, Tertiary | Cell Polarity | Microfilament Proteins - chemistry | Actin Cytoskeleton - metabolism | Actins - metabolism | Gene Silencing | Molecular Sequence Data | Nuclear Proteins - metabolism | Fetal Proteins - metabolism | Nuclear Proteins - chemistry | Genetic Complementation Test | Protein Transport | Bryopsida - growth & development | Nerve Tissue Proteins - metabolism | Nerve Tissue Proteins - chemistry | Protein Isoforms - metabolism | Protein Isoforms - chemistry | Microfilament Proteins - metabolism | Bryopsida - cytology | Bryopsida - anatomy & histology | PTEN Phosphohydrolase - chemistry | Fetal Proteins - chemistry | Physiological aspects | Genetic aspects | Plant cells and tissues | Research | Actin | Growth | Nerve Tissue Proteins | Cellular Biology | Nuclear Proteins | Life Sciences | PTEN Phosphohydrolase | Microfilament Proteins | Protein Isoforms | Fetal Proteins | Development Biology | Bryopsida | Biological Sciences
Journal Article
FEBS Letters, ISSN 0014-5793, 08/2012, Volume 586, Issue 17, pp. 2740 - 2750
.... Similarly, many growth factor receptors, for example EGF receptor, insulin receptor and c-Met, signal via huge protein complexes built on large platform proteins... 
Intrinsic disorder | Macromolecular crowding | Signalosome | Molecular architecture | Signaling network | Signaling complex | SH3 domain | SH2 domain | Sic1 | hepatocyte growth-factor receptor | Frs | CDK | CRKL | growth factor receptor-bound protein 2 | T-cell receptor | GRIP1 | PI3K | signal transducer and activator of transcription 1 | eukaryotic linear motif | NFN hypothesis | glutamate receptor interacting protein 1 | ZBP1 | Dok | sarcoma kinase | CASK | p130Cas | CT-10 related kinase | NR2B | disrupted in schizophrenia 1 | sterile 5 protein | MALS | SLiM | cyclin-dependent kinase | epidermal growth factor | Src-homology 2 domain | Erk | MAPK/Erk kinase | JIP1 | cell division control protein 4 | IGFR | Abl | COP9 | Irs | cAMP | short linear motif | neuronal munc18-1 binding protein 1 | estrogen receptor beta 2 | caudal type homeobox 2 | PTB domain | San1 | N-methyl d-aspartate receptor subtype 2B | insulin receptor substrate | large multi-site docking | ADAP1 | ApoER2 | Cdc4 | NMR | cyclic adenosine monophosphate | constitutive photomorphogenesis protein 9 | N-terminal folding nucleation hypothesis | arf-GAP with dual PH domain-containing protein 1 | Grb2 | Src-homology 3 domain | LAT | breast cancer anti-estrogen resistance 1 | c-Jun-amino-terminal kinase-interacting protein 1 | Mint1 | extracellular signal-regulated kinase | Abelson tyrosine-protein kinase 1 | Crk-associated substrate | PI3 kinase | ELM | SH2 containing protein tyrosine phosphatase 2 | UTR | insulin-like growth factor 1 receptor | Pbs2 | linker for activation of T-cells | Ste5 | ErB2 | calcium/calmodulin-dependent serine protein kinase | apolipoprotein E receptor 2 | PH domain | sterile 11 protein | phosphatidylinositol (3,4,5)-triphosphate | Crk-like protein | Gab | untranslated region | Rack1 | atomic force microscopy | MEK | PIP3 | small angle X-ray scattering | Crk | cryo-electron microscopy | DLK | TCR | Src | AFM | pleckstrin homology domain | phosphotyrosine-binding domain | zip code-binding protein 1 | SHP2 | substrate/subunit/inhibitor of cyclin-dependent protein kinase 1 | receptor of activated protein kinase C 1 | c-Met | DAP-like kinase | DISC1 | cryo-EM | sir antagonist 1 | fibroblast growth factor receptor substrate | LMD | mammalian lin-seven protein | Ste11 | Cdx2 | EGF | STAT1 | docking protein 1 | Rev/Rex activation domain-binding protein | nuclear magnetic resonance | SAXS | Polymyxin B resistance protein 2 | Rab | Grb2-associated-binding protein | insulin receptor | BCAR1 | UNSTRUCTURED PROTEINS | SRC FAMILY KINASE | TYROSINE PHOSPHORYLATION | MAP-KINASE | PROTEIN-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | PROCESSIVE PHOSPHORYLATION | MESSENGER-RNA LOCALIZATION | CELL BIOLOGY | BIOPHYSICS | COP9 SIGNALOSOME | IN-VIVO | Fungal Proteins - chemistry | Neoplasms - metabolism | Computational Biology - methods | Signal Transduction | Humans | Gene Expression Regulation | Phosphoproteins - metabolism | Protein Interaction Mapping - methods | Insulin - metabolism | Receptor, Epidermal Growth Factor - metabolism | Animals | Models, Biological | Insulin Receptor Substrate Proteins | Receptor, Insulin - metabolism | Tyrosine | Atomic force microscopy | Epidermal growth factor | Phosphatases | Sarcoma | Soups | Fibroblast growth factors | Glutamate | Adenylic acid | T cells | Protein kinases | Protein binding
Journal Article
Trends in biochemical sciences (Amsterdam. Regular ed.), ISSN 0968-0004, 2016, Volume 41, Issue 6, pp. 478 - 490
.... PRDs serve as a platform for protein–protein interactions, often mediating the binding of profilin–actin... 
PROMOTING FACTOR | ATP-ACTIN | CORDON-BLEU | STRUCTURAL BASIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | RICKETTSIA SCA2 | ARP2/3 COMPLEX | SYNDAPIN I | MUSCLE-CELLS | BACTERIAL EFFECTOR VOPL | FILAMENT NUCLEATION | Autoantigens - metabolism | Cytoskeletal Proteins - genetics | Actin-Related Protein 2-3 Complex - ultrastructure | Humans | Actins - metabolism | Fetal Proteins - metabolism | Autoantigens - genetics | Drosophila melanogaster - genetics | Actins - genetics | Drosophila melanogaster - metabolism | Actin-Related Protein 2-3 Complex - metabolism | Cell Nucleus - metabolism | Actins - chemistry | Cytoskeletal Proteins - metabolism | Microfilament Proteins - metabolism | Protein Interaction Domains and Motifs | Nuclear Proteins - genetics | Microfilament Proteins - genetics | Amino Acid Sequence | Microfilament Proteins - chemistry | Bacteria - metabolism | Actin Cytoskeleton - metabolism | Protein Structure, Secondary | Polymerization | Nuclear Proteins - metabolism | Autoantigens - chemistry | Cytoskeletal Proteins - chemistry | Nuclear Proteins - chemistry | Bacteria - genetics | Sequence Homology, Amino Acid | Sequence Alignment | Animals | Cell Nucleus - genetics | Fetal Proteins - genetics | Actin Cytoskeleton - ultrastructure | Fetal Proteins - chemistry | Physiological aspects | Muscle proteins | Actin | Protein-protein interactions | Protein binding
Journal Article
Nature (London), ISSN 1476-4687, 2012, Volume 483, Issue 7389, pp. 336 - 340
Journal Article
Journal Article
The Journal of cell biology, ISSN 1540-8140, 2003, Volume 162, Issue 6, pp. 1079 - 1088
... of ∼90 proteins implicated in actin function on lamella formation in Drosophila S2 cells... 
Cell motility | Scars | Delta cells | Microfilaments | Neurons | Drosophila | Cell lines | Actins | Actin depolymerizing factors | Cells | Polymerization | Lamella | Cytokinesis | Actin | SCAR | RNA INTERFERENCE | MIGRATION | polymerization | lamella | cytokinesis | ARP2/3 COMPLEX | HOMOLOG | MOTILITY DRIVEN | CELL BIOLOGY | YEAST | actin | FILAMENTS | CYCLASE-ASSOCIATED PROTEIN | DYNAMICS | NUCLEATION | Pseudopodia - ultrastructure | Cytoskeletal Proteins - antagonists & inhibitors | Cytoskeletal Proteins - genetics | Actins - metabolism | rac GTP-Binding Proteins - metabolism | Eukaryotic Cells - metabolism | Drosophila Proteins - metabolism | Cell Movement - physiology | Actins - genetics | Cell Cycle Proteins - antagonists & inhibitors | Actins - deficiency | RNA Interference | Profilins | Cell Cycle Proteins - genetics | Cytoskeletal Proteins - metabolism | Destrin | Drosophila Proteins - antagonists & inhibitors | Microfilament Proteins - genetics | Cell Line | Actin Cytoskeleton - metabolism | Microfilament Proteins - deficiency | Carrier Proteins - antagonists & inhibitors | Cell Cycle Proteins - metabolism | Actin Depolymerizing Factors | Carrier Proteins - genetics | Adaptor Proteins, Signal Transducing | Actins - antagonists & inhibitors | Animals | Carrier Proteins - metabolism | Microfilament Proteins - antagonists & inhibitors | Caenorhabditis elegans Proteins - antagonists & inhibitors | Pseudopodia - metabolism | Drosophila Proteins - deficiency | Actin-Related Protein 2 | Eukaryotic Cells - cytology | Drosophila Proteins - genetics | Actin Cytoskeleton - ultrastructure | Caenorhabditis elegans Proteins - genetics | Drosophila melanogaster | Contractile Proteins | RNA | Listeria | Bacterial proteins | Cytology | Physiological aspects | Genetic aspects | Research | Cell migration | actin; lamella; polymerization; SCAR; cytokinesis
Journal Article
The Journal of cell biology, ISSN 1540-8140, 1999, Volume 146, Issue 6, pp. 1319 - 1332
.... Using a combination of bacterial motility assays in platelet extracts with Escherichia coli expressing the Shigella IcsA protein and in vitro analysis of reconstituted systems from purified proteins... 
Nucleation | Listeria | Microfilaments | Profilins | Actins | Polymerization | HeLa cells | Platelets | Shigella | Cells | Arp2/3 complex | Shigella flexneri | IcsA | N-WASP | Actin | LISTERIA-MONOCYTOGENES | VIRULENCE GENE | F-ACTIN | SURFACE PROTEIN | BARBED ENDS | WISKOTT-ALDRICH-SYNDROME | PROFILIN | CELL BIOLOGY | actin | FILAMENTS | VINCULIN | DEPOLYMERIZING PROTEIN | Physiological aspects | Research | Bacterial proteins | Cdc42 protein | N-WASP protein | IcsA protein | Arp2/3 protein
Journal Article