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Journal Article
Trends in Biochemical Sciences, ISSN 0968-0004, 06/2016, Volume 41, Issue 6, pp. 478 - 490
Two types of sequences, proline-rich domains (PRDs) and the WASP-homology 2 (WH2) domain, are found in most actin filament nucleation and elongation factors... 
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
Annual Review of Biochemistry, ISSN 0066-4154, 2007, Volume 76, Issue 1, pp. 593 - 627
Formins are a widely expressed family of proteins that govern cell shape, adhesion, cytokinesis, and morphogenesis by remodeling the actin and microtubule... 
Cytokinesis | Polarity | Nucleation | BARBED-END | SRC TYROSINE KINASE | cytokinesis | BIOCHEMISTRY & MOLECULAR BIOLOGY | BUNDLING ACTIVITY | DIAPHANOUS-RELATED FORMIN | ARP2/3 COMPLEX | SACCHAROMYCES-CEREVISIAE | CONTRACTILE RING | nucleation | FISSION YEAST CYTOKINESIS | LIMB DEFORMITY GENE | HOMOLOGY-2 DOMAIN | polarity | Adaptor Proteins, Signal Transducing - chemistry | Cell Polarity | Humans | Actins - metabolism | Fetal Proteins - metabolism | Cell Movement - physiology | Morphogenesis | Microtubules - metabolism | Protein Isoforms - metabolism | Protein Isoforms - classification | Cytokinesis - physiology | Protein Isoforms - chemistry | Fetal Proteins - classification | Actins - chemistry | Nuclear Proteins - classification | Microfilament Proteins - metabolism | Nuclear Proteins - genetics | Microfilament Proteins - genetics | Microfilament Proteins - classification | Protein Structure, Tertiary | Microfilament Proteins - chemistry | Models, Molecular | Nuclear Proteins - metabolism | Nuclear Proteins - chemistry | Endocytosis - physiology | Animals | Cell Adhesion - physiology | rho GTP-Binding Proteins - metabolism | Adaptor Proteins, Signal Transducing - genetics | Protein Conformation | Fetal Proteins - genetics | Enzyme Activation | Adaptor Proteins, Signal Transducing - metabolism | Profilins - metabolism | Fetal Proteins - chemistry | Protein Isoforms - genetics
Conference Proceeding
Science, ISSN 0036-8075, 9/2012, Volume 337, Issue 6099, pp. 1231 - 1235
The brain tumor glioblastoma multiforme (GBM) is among the most lethal forms of human cancer. Here, we report that a small subset of GBMs (3.1%; 3 of 97 tumors... 
Exons | Neurons | Genes | REPORTS | Stem cells | Aneuploidy | Chromosomes | Cells | Tumors | Daughter cells | Cancer | ANEUPLOIDY | SELECTIVE INHIBITOR | POTENT | MULTIDISCIPLINARY SCIENCES | CANCER | RECEPTOR TYROSINE KINASE | DISCOVERY | CHROMOSOMAL INSTABILITY | FAMILY | Microtubule-Associated Proteins - chemistry | Neoplasm Transplantation | Translocation, Genetic | Oncogene Proteins, Fusion - metabolism | Receptor, Fibroblast Growth Factor, Type 3 - chemistry | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Mitosis | Humans | Receptor, Fibroblast Growth Factor, Type 1 - metabolism | Receptor, Fibroblast Growth Factor, Type 3 - antagonists & inhibitors | Fetal Proteins - metabolism | Receptor, Fibroblast Growth Factor, Type 1 - genetics | Receptor, Fibroblast Growth Factor, Type 3 - metabolism | Brain Neoplasms - metabolism | Oncogene Proteins, Fusion - chemistry | Spindle Apparatus - metabolism | Glioblastoma - genetics | Oncogene Fusion | Glioblastoma - metabolism | Antineoplastic Agents - pharmacology | Benzamides - pharmacology | Nuclear Proteins - genetics | Chromosomal Instability | Pyrazoles - pharmacology | Protein Structure, Tertiary | Receptor, Fibroblast Growth Factor, Type 3 - genetics | Enzyme Inhibitors - pharmacology | Brain Neoplasms - genetics | Nuclear Proteins - metabolism | Pyrimidines - pharmacology | Nuclear Proteins - chemistry | Piperazines - pharmacology | Receptor, Fibroblast Growth Factor, Type 1 - antagonists & inhibitors | Xenograft Model Antitumor Assays | Animals | Cell Transformation, Neoplastic | Oncogene Proteins, Fusion - genetics | Fetal Proteins - genetics | Mice | Receptor, Fibroblast Growth Factor, Type 1 - chemistry | Fetal Proteins - chemistry | Physiological aspects | Development and progression | Fibroblast growth factors | Genetic aspects | Research | Health aspects | Glioblastoma multiforme | Proteins | Kinases | Brain cancer | Genomics | Pharmaceutical sciences
Journal Article
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
Cancer Research, ISSN 0008-5472, 08/2011, Volume 71, Issue 15, pp. 5296 - 5306
The switch of tumor cells from an epithelial to a mesenchymal-like phenotype [designated as epithelial-to-mesenchymal transition (EMT)] is known to induce... 
BREAST-CARCINOMA | STEM-CELLS | IN-VITRO | ONCOLOGY | SERUM INTERLEUKIN-8 | PROSTATE-CANCER | METASTATIC PHENOTYPE | MALIGNANT-MELANOMA | TUMOR-GROWTH | EXPRESSION | PROGRESSION | Receptors, Interleukin-8 - genetics | T-Box Domain Proteins - physiology | Breast Neoplasms - secretion | Fibronectins - biosynthesis | Carcinoma - secretion | T-Box Domain Proteins - antagonists & inhibitors | Epithelial-Mesenchymal Transition - physiology | Humans | Neoplasm Proteins - physiology | T-Box Domain Proteins - biosynthesis | Culture Media, Conditioned - pharmacology | Culture Media, Serum-Free | Interleukin-8 - physiology | Neoplasm Proteins - antagonists & inhibitors | Bystander Effect | Tumor Microenvironment - physiology | Recombinant Fusion Proteins - antagonists & inhibitors | Cell Line, Tumor - pathology | Receptors, Interleukin-8 - biosynthesis | Cell Line, Tumor - secretion | Gene Expression Regulation, Neoplastic - drug effects | Intercellular Signaling Peptides and Proteins - secretion | Carcinoma - pathology | Neoplasm Proteins - genetics | Pancreatic Neoplasms - secretion | Promoter Regions, Genetic | Chemokines - secretion | Neoplasm Invasiveness | Neoplasm Proteins - biosynthesis | Pancreatic Neoplasms - pathology | RNA, Small Interfering - pharmacology | Cytokines - secretion | Fetal Proteins - physiology | Fetal Proteins - antagonists & inhibitors | Fetal Proteins - biosynthesis | T-Box Domain Proteins - genetics | Breast Neoplasms - pathology | Fetal Proteins - genetics | Fibronectins - genetics | Cell Movement | Brachyury | tumor microenvironment | IL-8 | metastasis | EMT
Journal Article
The Journal of Cell Biology, ISSN 0021-9525, 6/2003, Volume 161, Issue 5, pp. 875 - 887
Journal Article
Circulation, ISSN 0009-7322, 03/2016, Volume 133, Issue 11, pp. 1081 - 1092
BACKGROUND—Adult mammalian cardiomyocytes (CMs) have the potential to proliferate, but this is not sufficient to generate adequate CMs after myocardial... 
Myocardial infarction | Regeneration | Myocytes, cardiac | Molecular biology | Cell cycle | molecular biology | RENEWAL | CARDIAC & CARDIOVASCULAR SYSTEMS | cell cycle | regeneration | STAGE | myocardial infarction | GENES | YAP | PERIPHERAL VASCULAR DISEASE | myocytes | cardiac | Single-Blind Method | T-Box Domain Proteins - physiology | RNA, Small Interfering - genetics | T-Box Domain Proteins - biosynthesis | Muscle Proteins - biosynthesis | RNA, Messenger - biosynthesis | RNA Interference | Cell Division | Myocardial Infarction - pathology | Tumor Suppressor Proteins - genetics | Cell Cycle Proteins - genetics | Electrocardiography | Female | Myocardial Infarction - physiopathology | Genes, Reporter | Heart - physiopathology | Immediate-Early Proteins - physiology | Cell Size - drug effects | Immediate-Early Proteins - biosynthesis | RNA, Messenger - genetics | Genes, cdc - drug effects | Mice, Transgenic | Myocardium - pathology | Cell Cycle Proteins - biosynthesis | Myocardial Infarction - metabolism | Random Allocation | Fetal Proteins - biosynthesis | T-Box Domain Proteins - genetics | Gene Expression Regulation - drug effects | Muscle Proteins - genetics | Myocytes, Cardiac - pathology | Tumor Suppressor Proteins - physiology | Organ Size - drug effects | Animals | Immediate-Early Proteins - genetics | Signal Transduction - drug effects | Tamoxifen - pharmacology | Myocytes, Cardiac - metabolism | Fetal Proteins - genetics | Mice | Tumor Suppressor Proteins - biosynthesis | Cell proliferation | Care and treatment | Transcription factors | Research | Heart attack | Heart cells | remodeling
Journal Article
Journal Article
Biochemical Journal, ISSN 0264-6021, 02/2010, Volume 426, Issue 1, pp. 109 - 118
Activation of AMPK (AMP-activated protein kinase) by phosphorylation at Thr(172) is catalysed by at least two distinct upstream kinases, i.e. the tumour... 
calmodulin-dependent protein kinase (CaMK) | AMP-activated protein kinase-related kinase (ARK) | calmodulin-dependent protein kinase kinase (CaMKK) | AMP-activated protein kinase (AMPK) | Ca | TUMOR-SUPPRESSOR LKB1 | RESPIRATORY-CHAIN | CELLS | LOCALIZATION | ENERGY | Ca2+/calmodulin-dependent protein kinase kinase (CaMKK) | PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | CASCADE | UPSTREAM KINASE | Ca2+/calmodulin-dependent protein kinase (CaMK) | SUBSTRATE-SPECIFICITY | METABOLISM | Amino Acid Sequence | Cell Line | AMP-Activated Protein Kinases - metabolism | Immunoprecipitation | Calcium - metabolism | Humans | Molecular Sequence Data | Calcimycin - pharmacology | Phenformin - pharmacology | Cyclic AMP - pharmacology | Sequence Homology, Amino Acid | Calcium - physiology | Adenosine Triphosphate - metabolism | Calcium-Calmodulin-Dependent Protein Kinase Kinase - metabolism | Protein Binding | Adenosine Diphosphate - metabolism | HeLa Cells | Phosphorylation - drug effects | Ionophores - pharmacology | ACC, acetyl-CoA carboxylase | calmodulin-dependent protein kinase kinase | HEK, human embryonic kidney | MARK, microtubule affinity-regulating kinase | AMPK, AMP-activated protein kinase | TBS, Tris-buffered saline | BRSK, brain-specific kinase | UBA, ubiquitin-associated | MO25, mouse protein 25 | CaMK, Ca2 | ARK, AMPK-related kinase | NUAK, SNF1 (sucrose-non-fermenting kinase-1)-like kinase | AMPactivated protein kinase-related kinase (ARK) | GST, glutathione transferase | STRAD, Ste20-related adaptor | GFP, green fluorescent protein | calmodulin-dependent protein kinase | SIK, salt-inducible kinase | calmodulindependent protein kinase (CaMK) | Ca2 | AICAR, 5-amino-4-imidazolecarboxamide riboside | FBS, foetal bovine serum | CaMKK, Ca2
Journal Article