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Nature cell biology, ISSN 1476-4679, 2014, Volume 17, Issue 1, pp. 68 - 80
.... We show that FAM40A negatively regulates the MST3 and MST4 kinases, which promote the co-localization of the contractile actomyosin machinery with the Ezrin/Radixin/Moesin family proteins... 
ACTIVATION | INVASION | COMPLEX | KINASE | PP2A | PROTEIN PHOSPHATASE 2A | MYOSIN PHOSPHATASE | MICROARRAY DATA | SUBUNIT | FAMILY | CELL BIOLOGY | Phosphorylation | Autoantigens - metabolism | Humans | Phosphoprotein Phosphatases - metabolism | Autoantigens - genetics | Cell Movement - genetics | Neoplasm Metastasis | RNA Interference | rho-Associated Kinases - metabolism | Apoptosis Regulatory Proteins - genetics | Cytoskeletal Proteins - metabolism | Female | Membrane Proteins - metabolism | Microfilament Proteins - metabolism | Calmodulin-Binding Proteins - genetics | Actin Cytoskeleton - metabolism | Signal Transduction | Membrane Proteins - genetics | Computational Biology | Protein-Serine-Threonine Kinases - genetics | Proto-Oncogene Proteins - genetics | Calmodulin-Binding Proteins - metabolism | Actomyosin - metabolism | Protein-Serine-Threonine Kinases - biosynthesis | Carrier Proteins - genetics | Protein Phosphatase 1 - metabolism | Animals | Breast Neoplasms - genetics | Carrier Proteins - metabolism | Breast Neoplasms - pathology | Protein Phosphatase 2 - metabolism | Cell Line, Tumor | RNA, Small Interfering | Drosophila melanogaster | Metastasis | Muscle proteins | Health aspects | Phosphotransferases | Analysis | Cancer cells | Cytoskeletal Proteins | Medical and Health Sciences | Medicin och hälsovetenskap | Protein-Serine-Threonine Kinases | Breast Neoplasms | Klinisk medicin | Calmodulin-Binding Proteins | Journal Article | rho-Associated Kinases | Proto-Oncogene Proteins | Protein Phosphatase 2 | Protein Phosphatase 1 | Carrier Proteins | Phosphoprotein Phosphatases | Actin Cytoskeleton | Actomyosin | Autoantigens | Membrane Proteins | Clinical Medicine | Apoptosis Regulatory Proteins | Microfilament Proteins | Research Support, Non-U.S. Gov't | Cancer and Oncology | Cell Movement | Cancer och onkologi
Journal Article
The Journal of cell biology, ISSN 0021-9525, 1/2005, Volume 168, Issue 3, pp. 441 - 452
Invadopodia are actin-rich membrane protrusions with a matrix degradation activity formed by invasive cancer cells. We have studied the molecular mechanisms of... 
Receptors | Microfilaments | Actin depolymerizing factors | Small interfering RNA | Actins | Antibodies | Polymerization | Cultured cells | Cell membranes | Cells | CARCINOMA-CELLS | GROWTH-FACTOR RECEPTOR | MAMMARY ADENOCARCINOMA | ACTIN POLYMERIZATION | LAMELLIPOD EXTENSION | N-WASP | EXTRACELLULAR-MATRIX | SPECIALIZED SURFACE PROTRUSIONS | ALDRICH-SYNDROME PROTEIN | INVASIVE CELLS | CELL BIOLOGY | Oncogene Proteins - genetics | RNA, Small Interfering - genetics | Epidermal Growth Factor - physiology | Cytoskeletal Proteins - genetics | Actins - metabolism | Microfilament Proteins - physiology | Extracellular Matrix - metabolism | cdc42 GTP-Binding Protein - metabolism | Quinazolines | Oncogene Proteins - physiology | Cell Movement - physiology | Transfection | Cytoskeletal Proteins - metabolism | Microfilament Proteins - metabolism | Cytoskeletal Proteins - physiology | Wiskott-Aldrich Syndrome Protein Family | Microfilament Proteins - genetics | Carrier Proteins - physiology | Nerve Tissue Proteins - physiology | Wiskott-Aldrich Syndrome Protein, Neuronal | ErbB Receptors - antagonists & inhibitors | Cell Surface Extensions - metabolism | Neoplasm Invasiveness | RNA, Small Interfering - pharmacology | Enzyme Inhibitors - pharmacology | Oncogene Proteins - metabolism | Rats | Tyrphostins - pharmacology | Actin Depolymerizing Factors | cdc42 GTP-Binding Protein - physiology | Nerve Tissue Proteins - genetics | Fibronectins - metabolism | Nerve Tissue Proteins - metabolism | Carrier Proteins - genetics | Adaptor Proteins, Signal Transducing - physiology | Animals | Carrier Proteins - metabolism | GRB2 Adaptor Protein | Models, Biological | cdc42 GTP-Binding Protein - genetics | Cell Surface Extensions - drug effects | Adaptor Proteins, Signal Transducing - genetics | Actin-Related Protein 2 | Cell Line, Tumor | Actin-Related Protein 3 | Adaptor Proteins, Signal Transducing - metabolism | Microscopy, Fluorescence | Cell Surface Extensions - physiology | Epidermal growth factor | Metastasis | Cancer invasiveness | Cancer cells
Journal Article
Molecular cell, ISSN 1097-2765, 2015, Volume 60, Issue 2, pp. 220 - 230
Journal Article
Nature (London), ISSN 1476-4687, 2017, Volume 543, Issue 7645, pp. 438 - 442
...). Multiple protein complexes regulate the Rag GTPases in response to amino acids, including GATOR1, a GTPase activating protein for RAGA, and GATOR2, a positive regulator of unknown molecular function... 
ENCEPHALOPATHY | COMPLEX | SZT2 | RAG GTPASES | GENE | SIGNALING PATHWAY | AMINO-ACIDS | MULTIDISCIPLINARY SCIENCES | TUMOR-SUPPRESSOR | MUTATIONS | FOCAL EPILEPSIES | Lysosomes | Physiological aspects | Protein research | Research | Biological control systems | Protein-protein interactions | Proteins | Amino acids | Phosphorylation | Mutation | Glucose | Molecular weight
Journal Article
eLife, ISSN 2050-084X, 2014, Volume 3, p. e01612
... mitochondria remains unclear. In this study, we demonstrate that TBC1D15, a mitochondrial Rab GTPase-activating protein (Rab-GAP... 
Fis1 | rab7 | autophagy | TBC1D15 | Drp1 | Parkin | PARKIN | FIS1 | RECRUITMENT | GTPASE-ACTIVATING PROTEINS | MEMBRANE | PEROXISOMAL FISSION | P62/SQSTM1 | BIOLOGY | DEGRADATION | MAMMALIAN-CELLS | SELECTIVE AUTOPHAGY | Mitochondria - enzymology | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Humans | Protein Multimerization | rab GTP-Binding Proteins - genetics | Mitochondrial Proteins - genetics | GTPase-Activating Proteins - metabolism | Autophagy | Microtubules - metabolism | Ubiquitination | Lysosomes - metabolism | Transfection | Time Factors | Mitochondrial Proteins - metabolism | HEK293 Cells | Lysosomes - pathology | Membrane Proteins - metabolism | Microfilament Proteins - metabolism | Microfilament Proteins - genetics | rab GTP-Binding Proteins - metabolism | Signal Transduction | Membrane Proteins - genetics | HCT116 Cells | Ubiquitin-Protein Ligases - metabolism | Mitochondria - pathology | Mitochondrial Degradation | Autophagy-Related Protein 8 Family | Adaptor Proteins, Signal Transducing - genetics | Protein Binding | GTPase-Activating Proteins - genetics | HeLa Cells | Adaptor Proteins, Signal Transducing - metabolism | Ubiquitin-Protein Ligases - genetics | Membranes | Yeast | Cloning | Glycerol | Guanosine triphosphatases | Mammals | Morphogenesis | Proteins | Mitochondria | GTPase-activating protein | Microscopy | PTEN-induced putative kinase | Morphology | Parkin protein | GABARAP protein
Journal Article
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
Autophagy, ISSN 1554-8635, 2014, Volume 7, Issue 9, pp. 993 - 1010
Journal Article
The Journal of biological chemistry, ISSN 0021-9258, 01/2016, Volume 291, Issue 3, pp. 1103 - 1114
MFAP4 (microfibrillar-associated protein 4) is an extracellular glycoprotein found in elastic fibers without a clearly defined role in elastic fiber assembly... 
SWISS-MODEL | DOMAIN | CRYSTAL-STRUCTURE | COACERVATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | CROSS-LINKING | FICOLIN | LYSYL-OXIDASE | EXPRESSION | GLYCOPROTEIN MAGP-36 | INNATE IMMUNITY | Humans | Protein Multimerization | Glycoproteins - metabolism | Male | Elastic Tissue - metabolism | Protein Isoforms - metabolism | Desmosine - metabolism | Mice, Mutant Strains | Protein Isoforms - chemistry | Tropoelastin - metabolism | Carrier Proteins - chemistry | Microfilament Proteins - metabolism | Protein Interaction Domains and Motifs | Glycoproteins - chemistry | Microfilament Proteins - genetics | Peptide Fragments - genetics | Extracellular Matrix Proteins - metabolism | Glycoproteins - genetics | Recombinant Proteins - metabolism | Microfilament Proteins - chemistry | Extracellular Matrix Proteins - chemistry | Fibrillin-1 | Peptide Fragments - metabolism | Extracellular Matrix Proteins - genetics | Mice, Inbred C57BL | Models, Molecular | Recombinant Proteins - chemistry | Fibrillins | Protein Transport | Carrier Proteins - genetics | Peptide Fragments - chemistry | Animals | Carrier Proteins - metabolism | Tropoelastin - genetics | Ligands | Mutation | Microfibrils - metabolism | Tropoelastin - chemistry | Amino Acid Substitution | Protein Isoforms - genetics | Index Medicus | site-directed mutagenesis | analytical ultracentrifugation | calcium-binding protein | microfibrillar-associated protein 4 | Glycobiology and Extracellular Matrices | surface plasmon resonance (SPR) | elastin | fibrillin
Journal Article
PloS one, ISSN 1932-6203, 10/2012, Volume 7, Issue 10, p. e48854
...) in the host involves the migration of immature dendritic cells (iDCs). iDCs migrate in response to the HIV-1 envelope protein, gp120, and inhibiting such migration may limit the mucosal transmission of HIV-1... 
SLIT | PROTEIN | REPELLENT | HIV | ANGIOGENESIS | CHEMOTAXIS | MULTIDISCIPLINARY SCIENCES | GUIDANCE | RECEPTORS | ROBO | MIDLINE | Paxillin - metabolism | Proto-Oncogene Proteins pp60(c-src) - immunology | Pseudopodia - immunology | Human Umbilical Vein Endothelial Cells - metabolism | Dendritic Cells - immunology | Humans | Actins - metabolism | Human Umbilical Vein Endothelial Cells - immunology | cdc42 GTP-Binding Protein - metabolism | Paxillin - immunology | Actins - immunology | HIV Envelope Protein gp120 - metabolism | Cell Movement - immunology | HIV Envelope Protein gp120 - immunology | Intercellular Signaling Peptides and Proteins - metabolism | Signal Transduction - immunology | rac1 GTP-Binding Protein - immunology | Actin-Related Protein 2-3 Complex - metabolism | Focal Adhesion Kinase 2 - metabolism | RNA Interference | cdc42 GTP-Binding Protein - immunology | Wiskott-Aldrich Syndrome Protein - metabolism | Microfilament Proteins - metabolism | Receptors, Immunologic - immunology | Microfilament Proteins - genetics | Dendritic Cells - metabolism | Nerve Tissue Proteins - immunology | Cells, Cultured | Protein Binding - immunology | Blotting, Western | Actin-Related Protein 2-3 Complex - immunology | Nerve Tissue Proteins - metabolism | Microscopy, Confocal | Wiskott-Aldrich Syndrome Protein - immunology | Proto-Oncogene Proteins pp60(c-src) - metabolism | Microfilament Proteins - immunology | Intercellular Signaling Peptides and Proteins - immunology | Receptors, Immunologic - metabolism | rac1 GTP-Binding Protein - metabolism | Focal Adhesion Kinase 2 - immunology | Dendritic cells | HIV (Viruses) | Muscle proteins | Actin | Protein binding | Cdc42 protein | Sexually transmitted diseases--STD | Motility | Leukocyte migration | Mucosa | Viruses | Smooth muscle | Kinases | Tissues | Medical schools | Cell adhesion & migration | Proteins | Angiogenesis | Human immunodeficiency virus--HIV | Inhibition | Sequestering | Localization | Wiskott-Aldrich syndrome | LSP1 protein | Envelope protein | Rac1 protein | Glycoproteins | White blood cells | Medicine | Actin-related protein 2 | Signaling | Disease transmission | Ligands | Paxillin | Glycoprotein gp120 | Cell migration | STD | Sexually transmitted diseases | Human immunodeficiency virus
Journal Article
The New England journal of medicine, ISSN 1533-4406, 2011, Volume 365, Issue 25, pp. 2377 - 2388
...) associated with Charcot–Marie–Tooth neuropathy. The findings provide insight into mechanisms linking formin proteins to podocyte and Schwann-cell function. Charcot–Marie... 
GLOMERULOSCLEROSIS | MEDICINE, GENERAL & INTERNAL | MYELIN | PROTEIN | NEUROPATHY | EPITHELIAL-CELLS | GENE | RHO | MEDIATED TRANSPORT | FORMIN | NEPHROPATHY | Humans | Middle Aged | Proteolipids - metabolism | Actins - metabolism | Male | Charcot-Marie-Tooth Disease - genetics | Young Adult | Kidney - metabolism | Glomerulosclerosis, Focal Segmental - etiology | Myelin and Lymphocyte-Associated Proteolipid Proteins | Adult | Female | Membrane Transport Proteins - metabolism | Microfilament Proteins - metabolism | Child | Microfilament Proteins - genetics | Charcot-Marie-Tooth Disease - complications | Schwann Cells - metabolism | Phenotype | Animals | Adolescent | Age of Onset | Heterozygote | Mice | Mutation | Myelin Proteins - metabolism | Glomerulonephritis | Gene mutations | Charcot-Marie-Tooth disease | Causes of | Genetic aspects | Research | Myelin proteins | Cdc42 protein | Disease | Exons | Genes | Amino acids | Nervous system | Neuropathy | Guanine nucleotide-binding protein | Proteins | Myelin P0 protein | Peripheral myelin protein 22 | Localization | Deoxyribonucleic acid--DNA | Kidneys | Schwann cells | Polymerization | Guanosine triphosphatases | Myelination | Genotyping | Biopsy | Glomerulus | Cytoskeleton | Genetic testing | Cytoplasm | Schwann Cells | Genomics | Kidney | Charcot-Marie-Tooth Disease | Life Sciences | Proteolipids | Biochemistry, Molecular Biology | Actins | Microfilament Proteins | Membrane Transport Proteins | Myelin Proteins | Glomerulosclerosis, Focal Segmental
Journal Article