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Nature structural & molecular biology, ISSN 1545-9985, 2010, Volume 17, Issue 10, pp. 1247 - 1254
... of genome stability after mutations in proteins that carry out repair through homologous recombination, such as BRCA2 (refs. 2,3). In mammalian cells, homologous... 
POLY(ADP-RIBOSE) POLYMERASE | COMPLEX | BIOCHEMISTRY & MOLECULAR BIOLOGY | DOUBLE-STRAND BREAKS | HISTONE H2AX | FANCONI-ANEMIA | CELL BIOLOGY | RAD51 | BIOPHYSICS | IN-VIVO | SUSCEPTIBILITY GENE | D-LOOP FORMATION | DNA-REPAIR | Recombination, Genetic - physiology | DNA, Neoplasm - metabolism | Humans | Neoplasm Proteins - physiology | DNA Repair - physiology | Molecular Sequence Data | Structure-Activity Relationship | DNA Breaks, Double-Stranded | BRCA2 Protein - physiology | Breast Neoplasms - metabolism | Base Sequence | Tumor Suppressor Proteins - chemistry | Tumor Suppressor Proteins - genetics | Female | Protein Interaction Domains and Motifs | Nuclear Proteins - genetics | Nucleic Acid Conformation | Fanconi Anemia Complementation Group N Protein | Peptide Fragments - metabolism | Neoplasm Proteins - chemistry | Nuclear Proteins - chemistry | Poly(ADP-ribose) Polymerase Inhibitors | Protein Interaction Mapping | Tumor Suppressor Proteins - physiology | Peptide Fragments - chemistry | Apoptosis Regulatory Proteins | Models, Biological | Rad51 Recombinase - chemistry | Rad51 Recombinase - physiology | BRCA2 Protein - chemistry | Nuclear Proteins - physiology | Poly (ADP-Ribose) Polymerase-1 | Breast cancer | Genetic aspects | Research | BRCA mutations | Ovarian cancer | Proteins | Mutation | Molecular biology | Prostate cancer | homologous recombination | BRCA2 | PALB2
Journal Article
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
Journal Article
Science (American Association for the Advancement of Science), ISSN 1095-9203, 2007, Volume 315, Issue 5813, pp. 856 - 859
.... Our results indicate that BH3-only proteins induce apoptosis at least primarily by engaging the multiple pro-survival relatives guarding Bax and Bak. 
Research fellowships | Protein isoforms | Medical research | Myeloid cells | Antibodies | Cytochromes | Ligands | Reports | Grants | Viability | Apoptosis | RESPONSES | FAMILY-MEMBERS | X-L | MULTIDISCIPLINARY SCIENCES | BIM | HELIX | MITOCHONDRIAL-MEMBRANE | PUMA | DOMAINS | BH3-ONLY PROTEINS | CELL-DEATH | bcl-2-Associated X Protein - chemistry | Humans | BH3 Interacting Domain Death Agonist Protein - genetics | Proto-Oncogene Proteins - chemistry | Neoplasm Proteins - metabolism | bcl-2 Homologous Antagonist-Killer Protein - metabolism | Proto-Oncogene Proteins c-bcl-2 - metabolism | Bcl-2-Like Protein 11 | Tumor Suppressor Proteins - genetics | BH3 Interacting Domain Death Agonist Protein - chemistry | Apoptosis Regulatory Proteins - genetics | bcl-Associated Death Protein - metabolism | Membrane Proteins - metabolism | BH3 Interacting Domain Death Agonist Protein - metabolism | Protein Structure, Tertiary | Proto-Oncogene Proteins - metabolism | Cell Line | Tumor Suppressor Proteins - metabolism | Membrane Proteins - genetics | Apoptosis Regulatory Proteins - chemistry | Cells, Cultured | bcl-2-Associated X Protein - metabolism | Proto-Oncogene Proteins - genetics | Apoptosis Regulatory Proteins - metabolism | Mice, Knockout | Animals | Proteins - metabolism | Membrane Proteins - chemistry | Models, Biological | Myeloid Cell Leukemia Sequence 1 Protein | Mice | Mutation | bcl-X Protein - metabolism | Research | Peptides | Analysis
Journal Article
Science (American Association for the Advancement of Science), ISSN 0036-8075, 9/2006, Volume 313, Issue 5795, pp. 1968 - 1972
In higher eukaryotes, a multiprotein exon junction complex is deposited on spliced messenger RNAs. The complex is organized around a stable core, which serves... 
Hydrolysis | Proteins | Molecules | Messenger RNA | Double stranded RNA | RNA | Exons | Adenosine triphosphatases | Reports | Nucleotides | Binding sites | EIF4A | MESSENGER-RNA | DECAY | HELICASE ACTIVITY | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | DISTINCT | MOLECULAR INSIGHTS | TRANSLATION | MAMMALIAN-CELLS | BINDING | RNA Helicases - metabolism | Humans | Molecular Sequence Data | Crystallography, X-Ray | RNA Helicases - chemistry | Drosophila Proteins - metabolism | Neoplasm Proteins - metabolism | RNA, Messenger - metabolism | Adenosine Triphosphate - metabolism | Eukaryotic Initiation Factor-4A - chemistry | Nucleic Acid Conformation | Dimerization | Protein Structure, Tertiary | Amino Acid Sequence | DEAD-box RNA Helicases | Poly U - chemistry | Protein Structure, Secondary | RNA-Binding Proteins - chemistry | Models, Molecular | Neoplasm Proteins - chemistry | Nuclear Proteins - metabolism | Poly U - metabolism | Drosophila Proteins - chemistry | Nuclear Proteins - chemistry | Adenosine Triphosphate - analogs & derivatives | Amino Acid Motifs | Animals | Hydrogen Bonding | Adenylyl Imidodiphosphate - metabolism | Protein Conformation | RNA, Messenger - chemistry | Mutation | Eukaryotic Initiation Factor-4A - metabolism | RNA-Binding Proteins - metabolism | Exon (Molecular genetics) | Analysis | Research | Eukaryotic Initiation Factor-4A | Adenosine Triphosphate | RNA-Binding Proteins | Life Sciences | RNA Helicases | Neoplasm Proteins | Drosophila Proteins | Biochemistry, Molecular Biology | Nuclear Proteins | Adenylyl Imidodiphosphate | Poly U | Molecular biology | RNA, Messenger
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 39, pp. 16199 - 16210
Tumor cell invasion involves targeted localization of proteins required for interactions with the extracellular matrix and for proteolysis... 
MEMBRANE-FUSION | MIGRATION | GLUT4 TRANSLOCATION | SM PROTEIN | METALLOPROTEINASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | INVOLVEMENT | TRAFFICKING | PLASMA-MEMBRANE | SNARE | VAMP3 | Qb-SNARE Proteins - chemistry | Adenocarcinoma - pathology | Humans | Protein Multimerization | Qb-SNARE Proteins - metabolism | Extracellular Matrix - metabolism | Munc18 Proteins - metabolism | Neoplasm Proteins - antagonists & inhibitors | Green Fluorescent Proteins - genetics | Fibrosarcoma - metabolism | Neoplasm Proteins - metabolism | Vesicle-Associated Membrane Protein 2 - antagonists & inhibitors | Recombinant Fusion Proteins - metabolism | Podosomes - metabolism | Qa-SNARE Proteins - chemistry | Receptor, Epidermal Growth Factor - metabolism | Adenocarcinoma - metabolism | Fibrosarcoma - pathology | Qc-SNARE Proteins - metabolism | RNA Interference | Vesicle-Associated Membrane Protein 2 - chemistry | Munc18 Proteins - chemistry | Qa-SNARE Proteins - genetics | Protein Interaction Domains and Motifs | Neoplasm Proteins - genetics | Peptide Fragments - genetics | Binding, Competitive | Green Fluorescent Proteins - metabolism | Peptide Fragments - metabolism | Munc18 Proteins - genetics | Neoplasm Invasiveness | Neoplasm Proteins - chemistry | Recombinant Fusion Proteins - chemistry | Matrix Metalloproteinase 14 - metabolism | Munc18 Proteins - antagonists & inhibitors | Protein Transport | Podosomes - pathology | Peptide Fragments - chemistry | Qc-SNARE Proteins - chemistry | Qa-SNARE Proteins - metabolism | Cell Line, Tumor | Qc-SNARE Proteins - antagonists & inhibitors | Qb-SNARE Proteins - antagonists & inhibitors | Vesicle-Associated Membrane Protein 2 - metabolism | Extracellular Matrix - pathology | invadopodia | epidermal growth factor receptor (EGFR) | matrix metalloproteinase (MMP) | syntaxin4 | cell invasion | trafficking | Munc18c | Cell Biology
Journal Article
Molecular Cell, ISSN 1097-2765, 09/2010, Volume 39, Issue 6, pp. 963 - 974
... a critical role in tumorigenesis. However, the biochemical and cellular functions of this enigmatic family of proteins have remained elusive... 
NECDIN GENE | EMERGING ROLES | MELANOMA | KAP1 | CANCER/TESTIS ANTIGENS | BIOCHEMISTRY & MOLECULAR BIOLOGY | MDM2 INTERACTION | HOMOLOGOUS RECOMBINATION | CANCER-IMMUNOTHERAPY | CELL-LINES | EXPRESSION | CELL BIOLOGY | Melanoma-Specific Antigens - chemistry | Protein Interaction Domains and Motifs - physiology | Humans | Crystallography, X-Ray | Cytoplasm - metabolism | Intracellular Signaling Peptides and Proteins - metabolism | Neoplasm Proteins - metabolism | RING Finger Domains | Tripartite Motif-Containing Protein 28 | Ubiquitination | Cell Nucleus - metabolism | Transfection | Protein Structure, Quaternary | Antigens, Neoplasm - metabolism | Carrier Proteins - chemistry | Neoplasm Proteins - genetics | Intracellular Signaling Peptides and Proteins - genetics | Repressor Proteins - metabolism | Recombinant Proteins - metabolism | Antigens, Neoplasm - genetics | Cell Line | Biocatalysis | Tumor Suppressor Protein p53 - metabolism | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Repressor Proteins - genetics | Recombinant Proteins - genetics | Ubiquitin-Protein Ligases - chemistry | Carrier Proteins - genetics | Carrier Proteins - metabolism | Intracellular Signaling Peptides and Proteins - chemistry | Melanoma-Specific Antigens - metabolism | Cell Line, Tumor | Ubiquitin-Protein Ligases - genetics | Melanoma-Specific Antigens - genetics | Protein Binding - physiology | Ubiquitin | Antigens | Ligases | Crystals | Melanoma | Structure | Tumor proteins | Protein binding
Journal Article
Proceedings of the National Academy of Sciences - PNAS, ISSN 1091-6490, 2018, Volume 115, Issue 50, pp. E11651 - E11660
NDP52 and TAX1BP1, two SKIP carboxyl homology (SKICH) domain-containing autophagy receptors, play crucial roles in selective autophagy. The autophagic... 
NAP1 | TAX1BP1 | Autophagy receptor | Selective autophagy | NDP52 | STRUCTURAL INSIGHTS | RECRUITMENT | LOCALIZATION | PHOSPHORYLATION | MULTIDISCIPLINARY SCIENCES | OPTINEURIN | TBK1 | UBIQUITIN RECOGNITION | selective autophagy | RECEPTORS | MOLECULAR-BASIS | autophagy receptor | Adaptor Proteins, Signal Transducing - chemistry | Phosphorylation | Humans | Crystallography, X-Ray | Autophagy - physiology | Green Fluorescent Proteins - genetics | Intracellular Signaling Peptides and Proteins - metabolism | Neoplasm Proteins - metabolism | Recombinant Fusion Proteins - metabolism | Protein Structure, Quaternary | Protein Interaction Domains and Motifs | Green Fluorescent Proteins - chemistry | Neoplasm Proteins - genetics | Nuclear Proteins - genetics | Intracellular Signaling Peptides and Proteins - genetics | Protein-Serine-Threonine Kinases - metabolism | Amino Acid Sequence | Green Fluorescent Proteins - metabolism | Protein-Serine-Threonine Kinases - genetics | Models, Molecular | Neoplasm Proteins - chemistry | Nuclear Proteins - metabolism | Recombinant Fusion Proteins - chemistry | Nuclear Proteins - chemistry | Proteins - genetics | Sequence Homology, Amino Acid | Proteins - metabolism | Intracellular Signaling Peptides and Proteins - chemistry | tRNA Methyltransferases | Adaptor Proteins, Signal Transducing - genetics | Recombinant Fusion Proteins - genetics | Protein-Serine-Threonine Kinases - chemistry | HeLa Cells | Proteins - chemistry | Adaptor Proteins, Signal Transducing - metabolism | Autophagy (Cytology) | Cell research | Research | Proteins | Binding | Domains | Receptors | Homology | Kinases | Autophagy | Phagocytosis | Biological Sciences | PNAS Plus
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
Molecular cell, ISSN 1097-2765, 2016, Volume 64, Issue 2, pp. 307 - 319
SF3b is a heptameric protein complex of the U2 small nuclear ribonucleoprotein (snRNP) that is essential for pre-mRNA splicing... 
crystal structure | U2AF65 | SF3b | SF3B1 | cancer-related mutations | pre-mRNA splicing | DNA-DAMAGE RECOGNITION | SITE | U2 SNRNP PROTEINS | COMPLEX | U2AF | BRANCH POINT | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | SEQUENCE | BINDING | PRE-MESSENGER-RNA | CELL BIOLOGY | Oncogene Proteins - genetics | Spliceosomes - chemistry | Baculoviridae - metabolism | Humans | Baculoviridae - genetics | Crystallography, X-Ray | RNA Splicing Factors - chemistry | Moths | Neoplasm Proteins - metabolism | Phosphoproteins - metabolism | Phosphoproteins - chemistry | Protein Subunits - metabolism | RNA Splicing Factors - metabolism | Spliceosomes - metabolism | RNA Splicing | Cloning, Molecular | Protein Interaction Domains and Motifs | Neoplasm Proteins - genetics | Binding Sites | Genes, Tumor Suppressor | Protein Subunits - genetics | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Amino Acid Sequence | Protein Conformation, alpha-Helical | Gene Expression | Oncogene Proteins - chemistry | Oncogene Proteins - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Neoplasm Proteins - chemistry | Recombinant Proteins - genetics | Spliceosomes - ultrastructure | Phosphoproteins - genetics | RNA Splicing Factors - genetics | Splicing Factor U2AF - genetics | Animals | Protein Conformation, beta-Strand | Protein Binding | Splicing Factor U2AF - chemistry | Protein Subunits - chemistry | HeLa Cells | Mutation | Splicing Factor U2AF - metabolism | Crosslinked polymers | RNA | Crystals | Genetic aspects | Structure | Binding proteins | Mass spectrometry | Cancer | Protein binding
Journal Article