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Molecular cell, ISSN 1097-2765, 2005, Volume 17, Issue 3, pp. 393 - 403
Apoptosis is initiated when Bcl-2 and its prosurvival relatives are engaged by proapoptotic BH3-only proteins via interaction of its BH3 domain with a groove on the Bcl-2-like proteins... 
CYTOCHROME-C | COMPLEX | SURVIVAL FACTOR | BIOCHEMISTRY & MOLECULAR BIOLOGY | MITOCHONDRIA | BIM | RELEASE | PEPTIDE | CELL-DEATH | FAMILY | MEMBER | CELL BIOLOGY | Humans | Molecular Sequence Data | Proto-Oncogene Proteins - chemistry | Neoplasm Proteins - metabolism | Genetic Complementation Test | Proto-Oncogene Proteins c-bcl-2 - metabolism | Bcl-2-Like Protein 11 | Carrier Proteins - chemistry | Proto-Oncogene Proteins c-bcl-2 - chemistry | Membrane Proteins - metabolism | Neoplasm Proteins - genetics | Peptide Fragments - genetics | Cell Survival - physiology | Binding, Competitive | Protein Structure, Tertiary | Proto-Oncogene Proteins - metabolism | Recombinant Proteins - metabolism | Amino Acid Sequence | bcl-X Protein | Peptide Fragments - metabolism | Membrane Proteins - genetics | Models, Molecular | Recombinant Proteins - chemistry | Neoplasm Proteins - chemistry | Proto-Oncogene Proteins - genetics | Recombinant Proteins - genetics | Proteins - genetics | Sequence Homology, Amino Acid | Carrier Proteins - genetics | Peptide Fragments - chemistry | Animals | Apoptosis Regulatory Proteins | Carrier Proteins - metabolism | Proteins - metabolism | Membrane Proteins - chemistry | Models, Biological | Myeloid Cell Leukemia Sequence 1 Protein | Biosensing Techniques | Ligands | Mice | Apoptosis - physiology | Proteins - chemistry | In Vitro Techniques | Proto-Oncogene Proteins c-bcl-2 - genetics
Journal Article
Proceedings of the National Academy of Sciences - PNAS, ISSN 1091-6490, 2013, Volume 110, Issue 37, pp. 14942 - 14947
Journal Article
The Journal of biological chemistry, ISSN 1083-351X, 2016, Volume 291, Issue 13, pp. 6689 - 6695
Intrinsically disordered proteins (IDPs) are characterized by a lack of persistent structure... 
signaling | residual structure | electrostatics | coupled folding and binding | BIOCHEMISTRY & MOLECULAR BIOLOGY | protein electrostatics | C-MYB | TRANSITION-STATE | INDUCED FIT | protein-protein interactions | INTRINSICALLY DISORDERED PROTEINS | LINEAGE LEUKEMIA PROTEIN | IDP | MOLECULAR RECOGNITION | KIX DOMAIN | SEQUENCE | protein folding | phi-value | TRANSACTIVATION DOMAIN | kinetics | biophysics | protein dynamic | CONFORMATIONAL SELECTION | Cyclic AMP Response Element-Binding Protein - chemistry | Humans | Myeloid Cell Leukemia Sequence 1 Protein - metabolism | CREB-Binding Protein - chemistry | Proto-Oncogene Proteins - chemistry | CREB-Binding Protein - genetics | CREB-Binding Protein - metabolism | Thermodynamics | Apoptosis Regulatory Proteins - genetics | Myeloid Cell Leukemia Sequence 1 Protein - chemistry | Protein Interaction Domains and Motifs | Proto-Oncogene Proteins - metabolism | Signal Transduction | Apoptosis Regulatory Proteins - chemistry | Proto-Oncogene Proteins - genetics | Static Electricity | Intrinsically Disordered Proteins - genetics | Molecular Dynamics Simulation | Myeloid Cell Leukemia Sequence 1 Protein - genetics | Protein Folding | Apoptosis Regulatory Proteins - metabolism | Cyclic AMP Response Element-Binding Protein - genetics | Intrinsically Disordered Proteins - chemistry | Cyclic AMP Response Element-Binding Protein - metabolism | Hydrophobic and Hydrophilic Interactions | Protein Binding | Kinetics | Intrinsically Disordered Proteins - metabolism | Minireviews
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
The Journal of biological chemistry, ISSN 0021-9258, 02/2015, Volume 290, Issue 8, pp. 4908 - 4927
synGAP is a neuron-specific Ras and Rap GTPase-activating protein (GAP) found in high concentrations in the postsynaptic density (PSD... 
NMDA RECEPTOR | DOMAIN | STIMULATION | INHIBITION | CALPAIN | CLONING | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | MUTATIONS | HIPPOCAMPAL-NEURONS | PLASTICITY | Oncogene Proteins - genetics | ras Proteins - genetics | Phosphorylation | ras GTPase-Activating Proteins - chemistry | rap1 GTP-Binding Proteins - chemistry | Proto-Oncogene Proteins p21(ras) - genetics | Humans | Receptors, N-Methyl-D-Aspartate - metabolism | ras Proteins - metabolism | Neurons - cytology | GTPase-Activating Proteins - metabolism | Receptors, N-Methyl-D-Aspartate - genetics | Cyclin-Dependent Kinase 5 - chemistry | Cyclin-Dependent Kinase 5 - genetics | ras GTPase-Activating Proteins - genetics | Receptors, N-Methyl-D-Aspartate - chemistry | ras Proteins - chemistry | Proto-Oncogene Proteins p21(ras) - chemistry | Calcium-Calmodulin-Dependent Protein Kinase Type 2 - metabolism | Proto-Oncogene Proteins p21(ras) - metabolism | rap1 GTP-Binding Proteins - metabolism | ras GTPase-Activating Proteins - metabolism | Oncogene Proteins - chemistry | Cells, Cultured | Oncogene Proteins - metabolism | Rats | Synapses - enzymology | GTPase-Activating Proteins - chemistry | Cyclin-Dependent Kinase 5 - metabolism | Calcium-Calmodulin-Dependent Protein Kinase Type 2 - genetics | Animals | Calcium-Calmodulin-Dependent Protein Kinase Type 2 - chemistry | Neurons - enzymology | GTPase-Activating Proteins - genetics | rap1 GTP-Binding Proteins - genetics | rap GTP-Binding Proteins | Ras Protein | Ras-related Protein 1 (Rap1) | Postsynaptic Density | Ca2 | Synaptic Plasticity | Small GTPase | Neurobiology | Mass Spectrometry (MS) | Cyclin-dependent Kinase 5 (CDK5) | Protein Kinase | Calmodulin-dependent Protein Kinase II (CaMKII) | Synaptic GTPase-activating Protein (synGAP)
Journal Article
Science (American Association for the Advancement of Science), ISSN 1095-9203, 2014, Volume 343, Issue 6173, pp. 885 - 888
.... We discovered that a domain in placenta growth factor-2 (PlGF-2123-144) binds exceptionally strongly and promiscuously to ECM proteins... 
Proteins | Granulation tissue | Angiogenesis | Wound healing | Endothelial growth factors | Tissue engineering | Chemical engineering | REPORTS | Healing | Bones | Tissue repair | FACTOR-BINDING | REPAIR | ANGIOGENESIS | MULTIDISCIPLINARY SCIENCES | Pregnancy Proteins - chemistry | Proto-Oncogene Proteins c-sis - chemistry | Humans | Pregnancy Proteins - genetics | Extracellular Matrix - metabolism | Intercellular Signaling Peptides and Proteins - chemistry | Bone Morphogenetic Protein 2 - chemistry | Male | Pregnancy Proteins - metabolism | Vascular Endothelial Growth Factor A - metabolism | Wound Healing | Vascular Endothelial Growth Factor A - genetics | Heparitin Sulfate - metabolism | Vascular Endothelial Growth Factor A - chemistry | Intercellular Signaling Peptides and Proteins - metabolism | Bone Morphogenetic Protein 2 - metabolism | Protein Engineering | Extracellular Matrix Proteins - metabolism | Disease Models, Animal | Protein Structure, Tertiary | Bone Morphogenetic Protein 2 - genetics | Extracellular Matrix Proteins - chemistry | Proto-Oncogene Proteins c-sis - genetics | Proto-Oncogene Proteins c-sis - metabolism | Mice, Inbred C57BL | Intercellular Signaling Peptides and Proteins - genetics | Animals | Heparitin Sulfate - chemistry | Placenta Growth Factor | Mice | Physiological aspects | Extracellular matrix | Genetic aspects | Regeneration (Biology) | Growth factors | Health aspects | Cellular biology | Tissue | Matrix
Journal Article
Cell Death and Differentiation, ISSN 1350-9047, 01/2007, Volume 14, Issue 1, pp. 128 - 136
All BH3-only proteins, key initiators of programmed cell death, interact tightly with multiple binding partners and have sequences of low complexity, properties that are the hallmark of intrinsically... 
Bcl-2 | intrinsically unstructured | APOPTOSIS | EGL-1 | RECOGNITION | BIOCHEMISTRY & MOLECULAR BIOLOGY | UNFOLDED PROTEINS | DISORDERED PROTEINS | BH3-only | FAMILY | MEMBER | CELL BIOLOGY | STRUCTURAL BASIS | ROLES | molecular recognition | PEPTIDE COMPLEX | Adaptor Proteins, Signal Transducing - chemistry | Recombinant Fusion Proteins - isolation & purification | Adaptor Proteins, Signal Transducing - isolation & purification | Apoptosis Regulatory Proteins - isolation & purification | Proto-Oncogene Proteins - chemistry | Recombinant Fusion Proteins - metabolism | Bcl-2-Like Protein 11 | Apoptosis Regulatory Proteins - genetics | Nuclear Magnetic Resonance, Biomolecular | bcl-Associated Death Protein - metabolism | Membrane Proteins - metabolism | Circular Dichroism | Proto-Oncogene Proteins - isolation & purification | Protein Structure, Tertiary | Proto-Oncogene Proteins - metabolism | bcl-Associated Death Protein - genetics | Membrane Proteins - isolation & purification | Protein Structure, Secondary | bcl-Associated Death Protein - chemistry | Membrane Proteins - genetics | bcl-Associated Death Protein - isolation & purification | Apoptosis Regulatory Proteins - chemistry | Proto-Oncogene Proteins - genetics | Recombinant Fusion Proteins - chemistry | Protein Folding | Apoptosis Regulatory Proteins - metabolism | Animals | Membrane Proteins - chemistry | Adaptor Proteins, Signal Transducing - genetics | Recombinant Fusion Proteins - genetics | Mice | Adaptor Proteins, Signal Transducing - metabolism
Journal Article
Nature (London), ISSN 1476-4687, 2004, Volume 431, Issue 7010, pp. 873 - 878
.... The complex, termed hPRC1L (human Polycomb repressive complex 1-like), is composed of several Polycomb-group proteins including Ring1, Ring2, Bmi1 and HPH2... 
CORE | RECRUITMENT | TRANSCRIPTIONAL ACTIVATION | COMPLEX | LIGASE ACTIVITY | MULTIDISCIPLINARY SCIENCES | RAD6 | H3 LYSINE-27 METHYLATION | UBIQUITYLATION | RING FINGER PROTEINS | DROSOPHILA | Nuclear Proteins - isolation & purification | Nucleosomes - chemistry | Humans | Multiprotein Complexes | Ubiquitin - metabolism | Molecular Sequence Data | Drosophila melanogaster - genetics | Promoter Regions, Genetic - genetics | Protein Subunits - metabolism | DNA-Binding Proteins - metabolism | Protein Subunits - isolation & purification | Repressor Proteins - isolation & purification | Response Elements - genetics | Nuclear Proteins - genetics | Proto-Oncogene Proteins - isolation & purification | Repressor Proteins - metabolism | Protein Subunits - genetics | Proto-Oncogene Proteins - metabolism | Amino Acid Sequence | Cell Line | Catalytic Domain | Repressor Proteins - chemistry | Gene Silencing | Ubiquitin-Protein Ligases - metabolism | Nucleosomes - metabolism | Repressor Proteins - genetics | Nuclear Proteins - metabolism | Proto-Oncogene Proteins - genetics | Polycomb-Group Proteins | Transcription Factors - genetics | DNA-Binding Proteins - genetics | DNA-Binding Proteins - isolation & purification | Ubiquitin-Protein Ligases - chemistry | DNA-Binding Proteins - chemistry | Homeodomain Proteins - genetics | Transcription Factors - metabolism | Polycomb Repressive Complex 2 | Animals | Polycomb Repressive Complex 1 | Transcription Factors - isolation & purification | Ubiquitin-Protein Ligases - isolation & purification | Protein Subunits - chemistry | Drosophila Proteins - genetics | HeLa Cells | Histones - metabolism | Ubiquitin-Protein Ligases - genetics | Proteins | Enzymes | Cell culture | Chromatin | Biochemistry
Journal Article
Structure (London), ISSN 0969-2126, 2018, Volume 26, Issue 1, pp. 85 - 95.e3
The CXXC domain, first identified as the reader of unmodified CpG dinucleotide, plays important roles in epigenetic regulation by targeting various activities... 
histone methylation | DNMT1 | KDM2A | DNA methylation | TET1 | CFP1 | CpG island | MLL | CXXC domain | epigenetics | HOMEODOMAIN | METHYLATION | METHYLTRANSFERASE | CHROMATIN-STRUCTURE | 5-METHYLCYTOSINE | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSCRIPTION | BINDING DOMAIN | CELL BIOLOGY | BIOPHYSICS | GENES | DIOXYGENASE | CPG ISLANDS | Epigenesis, Genetic | Humans | Crystallography, X-Ray | Mixed Function Oxygenases - metabolism | Mixed Function Oxygenases - chemistry | Proto-Oncogene Proteins - chemistry | Neoplasm Proteins - metabolism | DNA-Binding Proteins - metabolism | Protein Isoforms - metabolism | Protein Isoforms - chemistry | Cloning, Molecular | Escherichia coli - metabolism | Jumonji Domain-Containing Histone Demethylases - chemistry | Protein Interaction Domains and Motifs | Neoplasm Proteins - genetics | Binding Sites | Proto-Oncogene Proteins - metabolism | Recombinant Proteins - metabolism | Amino Acid Sequence | Protein Conformation, alpha-Helical | Gene Expression | Genetic Vectors - chemistry | F-Box Proteins - metabolism | F-Box Proteins - chemistry | Genetic Vectors - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Neoplasm Proteins - chemistry | Proto-Oncogene Proteins - genetics | Recombinant Proteins - genetics | DNA - metabolism | DNA-Binding Proteins - genetics | DNA-Binding Proteins - chemistry | Jumonji Domain-Containing Histone Demethylases - genetics | DNA - genetics | Sequence Homology, Amino Acid | DNA - chemistry | Sequence Alignment | Protein Conformation, beta-Strand | Escherichia coli - genetics | CpG Islands | Protein Binding | Mixed Function Oxygenases - genetics | F-Box Proteins - genetics | Jumonji Domain-Containing Histone Demethylases - metabolism | Protein Isoforms - genetics | Epigenetic inheritance | Chromatin | Methyltransferases | DNA | Crystals | Physiological aspects | Genetic research | Nucleotide sequencing | Methylation | Structure | Protein binding | DNA sequencing
Journal Article
EMBO reports, ISSN 1469-3178, 2009, Volume 11, Issue 1, pp. 45 - 51
.... Recent evidence indicates that autophagy mediates selective removal of protein aggregates, organelles and microbes in cells... 
mitophagy | Nix | LC3 | GABARAP | selective autophagy | Selective autophagy | Mitophagy | APOPTOSIS | PROTEIN | RETICULOCYTE MATURATION | UBIQUITIN | BNIP3 | BIOCHEMISTRY & MOLECULAR BIOLOGY | E3 | CELL-DEATH | CELL BIOLOGY | STRUCTURAL BASIS | DEGRADATION | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Humans | Cercopithecus aethiops | Molecular Sequence Data | Substrate Specificity | Autophagy - physiology | Mitochondrial Proteins - genetics | Proto-Oncogene Proteins - chemistry | Mitochondrial Proteins - metabolism | Tumor Suppressor Proteins - chemistry | Tumor Suppressor Proteins - genetics | Membrane Proteins - metabolism | Binding Sites | Proto-Oncogene Proteins - metabolism | Amino Acid Sequence | Tumor Suppressor Proteins - metabolism | Membrane Proteins - genetics | Cells, Cultured | Ubiquitin-Protein Ligases - metabolism | Proto-Oncogene Proteins - genetics | Mitochondria - metabolism | Saccharomyces cerevisiae Proteins - genetics | Blotting, Western | Amino Acid Motifs | Autophagy-Related Protein 8 Family | Animals | Membrane Proteins - chemistry | Reticulocytes - cytology | Mitochondrial Proteins - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Mice | Receptors, GABA-A - metabolism | COS Cells | Proteins | Mitochondria | Cellular biology | Cytoplasm | Scientific Report
Journal Article