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Nature structural & molecular biology, ISSN 1545-9993, 08/2011, Volume 18, Issue 8, pp. 941 - 946
.... Recent studies indicate that the same SNARE-binding protein, complexin (CPX), can act either as a facilitator or as an inhibitor of membrane fusion, constituting a controversial dilemma... 
BIOPHYSICS | FORCE | NEUROTRANSMITTER RELEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | DISTINCT DOMAINS | SWITCH | BINDING | CELL BIOLOGY | Adaptor Proteins, Signal Transducing - chemistry | Humans | Vesicle-Associated Membrane Protein 2 - physiology | Syntaxin 1 - metabolism | Adaptor Proteins, Vesicular Transport - metabolism | Nerve Tissue Proteins - chemistry | SNARE Proteins - chemistry | Vesicle-Associated Membrane Protein 2 - chemistry | Adaptor Proteins, Vesicular Transport - chemistry | Syntaxin 1 - chemistry | Binding Sites | Protein Structure, Tertiary | Nerve Tissue Proteins - physiology | Adaptor Proteins, Vesicular Transport - physiology | SNARE Proteins - physiology | Models, Molecular | Rats | Synaptosomal-Associated Protein 25 - chemistry | Nerve Tissue Proteins - metabolism | Adaptor Proteins, Signal Transducing - physiology | Animals | Synaptosomal-Associated Protein 25 - physiology | Mice | Synaptosomal-Associated Protein 25 - metabolism | Lipid Bilayers - metabolism | Adaptor Proteins, Signal Transducing - metabolism | Membrane Fusion - physiology | Vesicle-Associated Membrane Protein 2 - metabolism | SNARE Proteins - metabolism | Syntaxin 1 - physiology | Cell hybridization | Physiological aspects | Research | Exocytosis | Membrane proteins | Proteins | Neurotransmitters | Membranes | Molecular biology | Vesicle-Associated Membrane Protein 2 | Membrane Fusion | Biochemistry, Molecular Biology | Nerve Tissue Proteins | Biophysics | Cellular Biology | Adaptor Proteins, Vesicular Transport | Life Sciences | Adaptor Proteins, Signal Transducing | Lipid Bilayers | Syntaxin 1 | Synaptosomal-Associated Protein 25 | SNARE Proteins
Journal Article
The Journal of biological chemistry, ISSN 0021-9258, 07/2011, Volume 286, Issue 28, pp. 25065 - 25075
.... We recently demonstrated that CCM3, a protein mutated in familial CCMs, resides predominantly within the STRIPAK complex... 
CEREBRAL CAVERNOUS MALFORMATIONS | STRIATIN FAMILY | PHOSPHATASE 2A | PATHWAY | BIOCHEMISTRY & MOLECULAR BIOLOGY | VASCULAR INTEGRITY | KINASE | RHO GTPASES | CELL-GROWTH | SACCHAROMYCES-CEREVISIAE | GENOME-SCALE | Protein Phosphatase 2 - chemistry | Humans | Multiprotein Complexes - genetics | Proto-Oncogene Proteins - chemistry | Structure-Activity Relationship | Multiprotein Complexes - metabolism | Nerve Tissue Proteins - chemistry | HEK293 Cells | Apoptosis Regulatory Proteins - genetics | Membrane Proteins - metabolism | Golgi Apparatus - chemistry | Protein-Serine-Threonine Kinases - metabolism | Calmodulin-Binding Proteins - genetics | Proto-Oncogene Proteins - metabolism | Membrane Proteins - genetics | Apoptosis Regulatory Proteins - chemistry | Protein Phosphatase 2 - genetics | Protein-Serine-Threonine Kinases - genetics | Proto-Oncogene Proteins - genetics | Calmodulin-Binding Proteins - chemistry | Calmodulin-Binding Proteins - metabolism | Nerve Tissue Proteins - genetics | Apoptosis Regulatory Proteins - metabolism | Nerve Tissue Proteins - metabolism | Multiprotein Complexes - chemistry | Animals | Membrane Proteins - chemistry | Protein Phosphatase 2 - metabolism | Golgi Apparatus - metabolism | Mice | Protein-Serine-Threonine Kinases - chemistry | HeLa Cells | Golgi Apparatus - genetics | MST4 | Striatin | Signal Transduction | Mass Spectrometry (MS) | Golgi | PP2A | Serine Threonine Protein Phosphatase | Serine Threonine Protein Kinase | Cerebral Cavernous Malformations | Protein-Protein Interactions
Journal Article
Nature chemical biology, ISSN 1552-4469, 2014, Volume 10, Issue 10, pp. 810 - 812
.... Here we show that a single archaeal protein, the homolog of the third subunit of the eukaryotic Elongator complex (Elp3... 
DOMAIN | PROTEIN | POLYMERASE-II HOLOENZYME | BIOCHEMISTRY & MOLECULAR BIOLOGY | HISTONE ACETYLTRANSFERASE | SACCHAROMYCES-CEREVISIAE | ELONGATOR COMPLEX | EXPRESSION | SAM | Histone Acetyltransferases - chemistry | Archaeal Proteins - chemistry | Histone Acetyltransferases - genetics | Molecular Sequence Data | S-Adenosylmethionine - chemistry | Protein Subunits - metabolism | Nerve Tissue Proteins - chemistry | Histone Acetyltransferases - metabolism | Escherichia coli - metabolism | Conserved Sequence | Free Radicals - metabolism | Archaeal Proteins - genetics | RNA, Transfer - chemistry | Methanocaldococcus - chemistry | Uridine - chemistry | Protein Subunits - genetics | Archaeal Proteins - metabolism | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Amino Acid Sequence | Gene Expression | Biocatalysis | Free Radicals - chemistry | RNA, Transfer - metabolism | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Nerve Tissue Proteins - genetics | Nerve Tissue Proteins - metabolism | Escherichia coli - genetics | Methanocaldococcus - enzymology | Saccharomyces cerevisiae Proteins - metabolism | Uridine - metabolism | Protein Subunits - chemistry | Structural Homology, Protein | S-Adenosylmethionine - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Proteins | Eukaryotes | Biocatalysts | Cytoplasm | Transfer RNA
Journal Article
Science (American Association for the Advancement of Science), ISSN 1095-9203, 2004, Volume 303, Issue 5657, pp. 495 - 499
.... From this, we predict that BAR domains are in many protein families, including sorting nexins, centaurins, and oligophrenins... 
Proteins | String theory | Drosophila | Liver | Lipids | Cell membranes | Dimers | Liposomes | Curvature | Research Article | P branes | CLATHRIN-MEDIATED ENDOCYTOSIS | ADP-RIBOSYLATION FACTORS | LYSOPHOSPHATIDIC ACID | TERMINAL DOMAIN | DROSOPHILA AMPHIPHYSIN | SYNAPTIC VESICLE ENDOCYTOSIS | MULTIDISCIPLINARY SCIENCES | ACTIN CYTOSKELETON | GTPASE-ACTIVATING PROTEIN | BINDING | SH3 DOMAIN | Cytoskeletal Proteins | Coated Vesicles - metabolism | Drosophila - chemistry | Molecular Sequence Data | Crystallography, X-Ray | GTPase-Activating Proteins - metabolism | Drosophila Proteins - metabolism | Phosphoproteins - metabolism | Clathrin-Coated Vesicles - metabolism | Phosphoproteins - chemistry | Cell Membrane - chemistry | Coated Vesicles - chemistry | Nerve Tissue Proteins - chemistry | Carrier Proteins - chemistry | Cell Membrane - metabolism | ADP-Ribosylation Factors - metabolism | ADP-Ribosylation Factors - genetics | Dimerization | Protein Structure, Tertiary | Amino Acid Sequence | Protein Structure, Secondary | COP-Coated Vesicles - metabolism | Models, Molecular | Nuclear Proteins - metabolism | Drosophila Proteins - chemistry | GTPase-Activating Proteins - chemistry | Nuclear Proteins - chemistry | Nerve Tissue Proteins - genetics | Clathrin - metabolism | Nerve Tissue Proteins - metabolism | Carrier Proteins - genetics | ADP-Ribosylation Factors - chemistry | Adaptor Proteins, Signal Transducing | Liposomes - chemistry | Animals | Carrier Proteins - metabolism | Protein Binding | Liposomes - metabolism | Mutation | Synapses | Chemical properties | Membranes | Yeast | Cellular biology | Cells
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
PLoS biology, ISSN 1545-7885, 2017, Volume 15, Issue 8, p. e2002354
.... In ventricular cardiomyocytes, the membrane deformation protein cardiac bridging integrator 1 (cBIN1 or BIN1+13+17) creates transverse-tubule... 
HYPERTROPHY | IN-VITRO | T-TUBULE MEMBRANE | BIOCHEMISTRY & MOLECULAR BIOLOGY | HEART-FAILURE | ABSCISSION | BIOLOGY | TRAFFICKING | CARDIOVASCULAR-DISEASES | AMPHIPHYSIN-2 BIN1 | PLASMA BIN1 | REQUIREMENT | Adaptor Proteins, Signal Transducing - blood | Humans | Endosomal Sorting Complexes Required for Transport - genetics | RNA Interference | Tumor Suppressor Proteins - chemistry | Cell-Derived Microparticles - metabolism | Endosomal Sorting Complexes Required for Transport - chemistry | Tumor Suppressor Proteins - metabolism | Recombinant Proteins - chemistry | Mice, Transgenic | Nuclear Proteins - chemistry | Particle Size | Myocytes, Cardiac - pathology | Endosomal Sorting Complexes Required for Transport - ultrastructure | Peptide Fragments - chemistry | Myocytes, Cardiac - metabolism | HeLa Cells | Adaptor Proteins, Signal Transducing - chemistry | Nerve Tissue Proteins - blood | Endosomal Sorting Complexes Required for Transport - blood | Exons | Cell-Derived Microparticles - chemistry | Heart Failure - blood | Nerve Tissue Proteins - chemistry | Endosomal Sorting Complexes Required for Transport - antagonists & inhibitors | Tumor Suppressor Proteins - genetics | Peptide Fragments - blood | Protein Interaction Domains and Motifs | Nuclear Proteins - genetics | Cell-Derived Microparticles - ultrastructure | Recombinant Proteins - metabolism | Microscopy, Electron, Transmission | Nuclear Proteins - blood | Peptide Fragments - metabolism | Enzyme-Linked Immunosorbent Assay | Myocytes, Cardiac - cytology | Cells, Cultured | Endosomal Sorting Complexes Required for Transport - metabolism | Nuclear Proteins - metabolism | Heart Failure - pathology | Nerve Tissue Proteins - genetics | Protein Transport | Nerve Tissue Proteins - metabolism | Animals | Tumor Suppressor Proteins - blood | Adaptor Proteins, Signal Transducing - genetics | Heterozygote | Adaptor Proteins, Signal Transducing - metabolism | Myocytes, Cardiac - ultrastructure | Health aspects | Heart cells | Heart | Flow cytometry | Plasma | Neurosciences | Intercellular signalling | Deformation | Calcium | Physicians | Biology | Cell interactions | Cell surface | Microparticles | Fission | Blood plasma | Proteins | Calcium signalling | Osmotic shock | Vesicles | Clonal deletion | Actin | BAR protein | Physiology | Ion channels | Bathing | Protein transport | Heart diseases | Enzyme-linked immunosorbent assay | Heart failure | Enzymes | Cardiac muscle | Deformation mechanisms | Membrane vesicles | Cardiomyocytes | Electron microscopy | Membrane proteins | Mutants | Medicine | Cytometry | Data collection | Ventricle | Alzheimers disease | Plasmas (physics)
Journal Article
Cell (Cambridge), ISSN 0092-8674, 2012, Volume 149, Issue 5, pp. 1035 - 1047
Journal Article
Proceedings of the National Academy of Sciences - PNAS, 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
PloS one, ISSN 1932-6203, 2014, Volume 9, Issue 4, p. e94380
Nesprin-1-giant and nesprin-2-giant regulate nuclear positioning by the interaction of their C-terminal KASH domains with nuclear membrane SUN proteins and their N- terminal calponin-homology domains... 
REAL-TIME PCR | SKELETAL-MUSCLE | CELLS | ROLES | SUN PROTEINS | MULTIDISCIPLINARY SCIENCES | ENVELOPE | DREIFUSS MUSCULAR-DYSTROPHY | LAMIN A/C | ACTIN CYTOSKELETON | NUCLEAR-MEMBRANE PROTEIN | Embryonic Stem Cells - metabolism | Conserved Sequence - genetics | Humans | DNA, Complementary - genetics | Molecular Sequence Data | Muscle, Skeletal - metabolism | Gene Expression Profiling | RNA, Messenger - metabolism | Organ Specificity - genetics | Nerve Tissue Proteins - chemistry | Protein Isoforms - metabolism | Proteolysis | Myocardium - metabolism | Microfilament Proteins - metabolism | Nuclear Proteins - genetics | Microfilament Proteins - genetics | Protein Structure, Tertiary | Amino Acid Sequence | Cell Line | Microfilament Proteins - chemistry | Muscular Dystrophy, Emery-Dreifuss - genetics | Alternative Splicing - genetics | RNA, Messenger - genetics | Exons - genetics | Nuclear Proteins - metabolism | Nuclear Proteins - chemistry | Nerve Tissue Proteins - genetics | Nerve Tissue Proteins - metabolism | Spleen - metabolism | Protein Isoforms - genetics | Analysis | Monoclonal antibodies | Muscles | Physiological aspects | Smooth muscle | Muscle proteins | Health aspects | Heart | Alternative splicing | Cardiomyopathy | Genes | Emery-Dreifuss muscular dystrophy | Homology | Kinases | Tissues | Muscular dystrophy | Western blotting | Proteins | Calponin | Cell growth | Actin | Bioinformatics | Heart diseases | Neuromuscular diseases | Immunoglobulins | Degradation products | Splicing | Gene expression | Skeletal muscle | Polymerase chain reaction | Dilated cardiomyopathy | Cell lines | Isoforms | Stem cells | Cytoskeleton | Mutation | Dystrophy
Journal Article
PLoS pathogens, ISSN 1553-7374, 2013, Volume 9, Issue 9, p. e1003636
.... Moreover, 80% of potential EBNA 3A, 3B or 3C target genes were also targeted by EBNA 2, implicating extensive interplay between EBNA 2 and 3 proteins in cellular reprogramming... 
SIGNAL-BINDING-PROTEIN | RBP-J-KAPPA | GROWTH TRANSFORMATION | NUCLEAR ANTIGEN 3C | MICROBIOLOGY | TRANSFORMATION IN-VITRO | EBNA-2-MEDIATED TRANSACTIVATION | NUCLEAR-PROTEIN-2 ACIDIC DOMAIN | LONG-RANGE INTERACTION | VIROLOGY | BURKITTS-LYMPHOMA | LATENT MEMBRANE-PROTEIN | PARASITOLOGY | Protein-Tyrosine Kinases - metabolism | Humans | Epstein-Barr Virus Nuclear Antigens - chemistry | Viral Proteins - metabolism | Cellular Reprogramming | Alcohol Oxidoreductases - genetics | Cell Cycle Proteins - chemistry | Nerve Tissue Proteins - chemistry | Protein-Tyrosine Kinases - genetics | Protein-Tyrosine Kinases - chemistry | Cell Cycle Proteins - genetics | Nuclear Proteins - genetics | Binding Sites | Epstein-Barr Virus Nuclear Antigens - metabolism | Repressor Proteins - metabolism | Binding, Competitive | Recombinant Proteins - metabolism | Cell Line | Gene Targeting | Repressor Proteins - chemistry | Epstein-Barr Virus Nuclear Antigens - genetics | Viral Proteins - chemistry | Cell Cycle Proteins - metabolism | Recombinant Proteins - chemistry | Repressor Proteins - genetics | Viral Proteins - genetics | Alcohol Oxidoreductases - metabolism | Nuclear Proteins - metabolism | Nuclear Proteins - chemistry | Nerve Tissue Proteins - genetics | Epstein-Barr Virus Infections - pathology | Host-Pathogen Interactions | Nerve Tissue Proteins - metabolism | Enhancer Elements, Genetic | Alcohol Oxidoreductases - chemistry | Models, Biological | Herpesvirus 4, Human - metabolism | Epstein-Barr Virus Infections - metabolism | Transcription factors | Physiological aspects | Epstein-Barr virus | Genetic aspects | Research | Gene expression | Health aspects | Proteins | Medical research | Genomes | Genes
Journal Article