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The FEBS Journal, ISSN 1742-464X, 10/2017, Volume 284, Issue 19, pp. 3218 - 3229
.... 1H, 15N spectra showed that the C‐terminal SH3 domain of BIN1 isoform 1 (BIN1Iso1) is not mobile in solution but locked with the core of the protein... 
SH3 domain | nuclear magnetic resonance spectroscopy | protein–protein interaction | Tau | BIN1 | Alzheimer's disease | ALZHEIMERS-DISEASE | NMR-SPECTROSCOPY | BIOCHEMISTRY & MOLECULAR BIOLOGY | PATHOLOGY | MODEL | IDENTIFIES VARIANTS | AMPHIPHYSIN | MEMBRANE CURVATURE | protein-protein interaction | BINDING | EXPRESSION | GENOME-WIDE ASSOCIATION | Adaptor Proteins, Signal Transducing - chemistry | Humans | Peptides - genetics | tau Proteins - metabolism | tau Proteins - chemistry | Peptides - metabolism | Protein Isoforms - metabolism | tau Proteins - genetics | Protein Isoforms - chemistry | Tumor Suppressor Proteins - chemistry | Tumor Suppressor Proteins - genetics | Cloning, Molecular | Escherichia coli - metabolism | Nuclear Magnetic Resonance, Biomolecular | Neurons - metabolism | Protein Interaction Domains and Motifs | Nuclear Proteins - genetics | Binding Sites | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Gene Expression | Tumor Suppressor Proteins - metabolism | Neurons - chemistry | Peptides - chemistry | Models, Molecular | Recombinant Proteins - chemistry | Nuclear Proteins - metabolism | Recombinant Proteins - genetics | Nuclear Proteins - chemistry | Amino Acid Motifs | Sequence Homology, Amino Acid | Sequence Alignment | Protein Conformation, beta-Strand | Escherichia coli - genetics | Adaptor Proteins, Signal Transducing - genetics | Protein Binding | Kinetics | Adaptor Proteins, Signal Transducing - metabolism | Protein Isoforms - genetics | Nuclear magnetic resonance spectroscopy | Neurons | Protein-protein interactions | Spectroscopy | Clathrin | Nuclear magnetic resonance--NMR | Peptides | Neurodegenerative diseases | Pathogenesis | Complexity | Proteins | Magnetic resonance spectroscopy | Tau protein | Spectrum analysis | Isoforms | Alzheimers disease | Binding sites | tau Proteins/metabolism | Nuclear Proteins/chemistry | Protein Isoforms/chemistry | Protein Isoforms/genetics | Adaptor Proteins, Signal Transducing/genetics | Recombinant Proteins/metabolism | Peptides/metabolism | Life Sciences | Recombinant Proteins/chemistry | Adaptor Proteins, Signal Transducing/chemistry | Nuclear Proteins/metabolism | Tumor Suppressor Proteins/chemistry | Nuclear Proteins/genetics | Tumor Suppressor Proteins/metabolism | Protein Isoforms/metabolism | Peptides/chemistry | Recombinant Proteins/genetics | Biochemistry, Molecular Biology | Escherichia coli/genetics | Escherichia coli/metabolism | Adaptor Proteins, Signal Transducing/metabolism | Neurons/chemistry | Tumor Suppressor Proteins/genetics | tau Proteins/genetics | Neurons/metabolism | Peptides/genetics | tau Proteins/chemistry
Journal Article
Molecular cell, ISSN 1097-2765, 2009, Volume 36, Issue 1, pp. 39 - 50
In the largest E3 ligase subfamily, Cul3 binds a BTB domain, and an associated protein-interaction domain such as MATH recruits substrates for ubiquitination... 
PROTEINS | ACTIVATION | PROTEIN | NRF2 | BIOCHEMISTRY & MOLECULAR BIOLOGY | SCF | ADAPTER | DEGRADATION | KEAP1 | DIMERIZATION | BTB DOMAIN | HEDGEHOG | CELL BIOLOGY | Transcription Factors - chemistry | Humans | Crystallography, X-Ray | Drosophila Proteins - metabolism | Mutation - physiology | Protein Multimerization - physiology | Protein Structure, Quaternary - physiology | Ubiquitination - physiology | Peptide Fragments - genetics | Repressor Proteins - metabolism | Amino Acid Sequence | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Repressor Proteins - genetics | Recombinant Fusion Proteins - chemistry | Nuclear Proteins - chemistry | Ubiquitin-Protein Ligases - chemistry | DNA-Binding Proteins - chemistry | Cullin Proteins - chemistry | Peptide Fragments - chemistry | Phosphoprotein Phosphatases - genetics | Consensus Sequence - physiology | Recombinant Fusion Proteins - genetics | Histones - metabolism | Ubiquitin-Protein Ligases - genetics | Drosophila melanogaster | Phosphoprotein Phosphatases - chemistry | Protein Binding - physiology | Adaptor Proteins, Signal Transducing - chemistry | Histones - chemistry | Protein Interaction Domains and Motifs - physiology | Phosphoprotein Phosphatases - metabolism | Recombinant Fusion Proteins - metabolism | DNA-Binding Proteins - metabolism | Cullin Proteins - metabolism | Nuclear Proteins - genetics | Peptide Fragments - metabolism | Repressor Proteins - chemistry | Nuclear Proteins - metabolism | Drosophila Proteins - chemistry | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Cullin Proteins - genetics | Transcription Factors - metabolism | Animals | Histones - genetics | Adaptor Proteins, Signal Transducing - genetics | Drosophila Proteins - genetics | Adaptor Proteins, Signal Transducing - metabolism | Ubiquitin | Chromatin | Phosphatases | Ligases | CHROMATIN | BASIC BIOLOGICAL SCIENCES | SUBSTRATES | FLEXIBILITY | GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE | LIGASES | DIMERS | PHOSPHATASES
Journal Article
Proceedings of the National Academy of Sciences - PNAS, ISSN 1091-6490, 2011, Volume 108, Issue 19, pp. 8003 - 8008
.... By combining cryoelectron microscopy analysis with a characterization of NS1 amphipathic properties, we show that the secreted NS1 hexamer forms a lipoprotein particle with an open-barrel protein... 
Molecules | Lipoproteins | Secretion | Dengue | HDL lipoproteins | Lipids | Triglycerides | Dengue virus | Detergents | Fatty acids | Amphiphilic proteins | Dengue hemorrhagic fever | Arbovirus | amphiphilic proteins | CELLS | RNA | FORM | GLYCOPROTEIN NS1 | MULTIDISCIPLINARY SCIENCES | arbovirus | PATHOGENESIS | dengue hemorrhagic fever | secretion | LIPID PROFILE | ENCEPHALITIS | WEST-NILE | FEVER | REVEALS | Cell Line | Protein Subunits | Recombinant Proteins - ultrastructure | Drosophila | Humans | Protein Multimerization | Dengue Virus - ultrastructure | Cercopithecus aethiops | Models, Molecular | Recombinant Proteins - chemistry | Dengue Virus - chemistry | Cryoelectron Microscopy | Lipoproteins, HDL - ultrastructure | Viral Nonstructural Proteins - chemistry | Animals | Computer Simulation | HEK293 Cells | Protein Structure, Quaternary | Lipoproteins, HDL - chemistry | Nuclear Magnetic Resonance, Biomolecular | Imaging, Three-Dimensional | Viral Nonstructural Proteins - ultrastructure | Vero Cells | Dengue viruses | Genetic aspects | Lipid metabolism | Viral Nonstructural Proteins/ultrastructure | Lipoproteins, HDL/ultrastructure | Life Sciences | Recombinant Proteins/chemistry | Lipoproteins, HDL/chemistry | Viral Nonstructural Proteins/chemistry | Dengue Virus/ultrastructure | Dengue Virus/chemistry | Recombinant Proteins/ultrastructure | Microbiology and Parasitology | Biological Sciences
Journal Article
eLife, ISSN 2050-084X, 2015, Volume 4, Issue 4, pp. 1 - 44
The AAA+ family ATPase TRIP13 is a key regulator of meiotic recombination and the spindle assembly checkpoint, acting on signaling proteins of the conserved HORMA domain family... 
N-Ethylmaleimide-Sensitive Proteins - metabolism | Mad2 Proteins - metabolism | Molecular Chaperones - metabolism | Caenorhabditis elegans Proteins - chemistry | Humans | Crystallography, X-Ray | Phylogeny | N-Ethylmaleimide-Sensitive Proteins - genetics | Amino Acid Sequence | Gene Expression | Caenorhabditis elegans - genetics | Cell Cycle Proteins - metabolism | Molecular Chaperones - genetics | Adenosine Triphosphatases - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Nuclear Proteins - chemistry | Caenorhabditis elegans - classification | Escherichia coli - genetics | Adenosine Triphosphatases - genetics | Escherichia coli Proteins - chemistry | Caenorhabditis elegans Proteins - genetics | Caenorhabditis elegans - enzymology | Adaptor Proteins, Signal Transducing - chemistry | Endopeptidase Clp - chemistry | M Phase Cell Cycle Checkpoints | Caenorhabditis elegans Proteins - metabolism | Molecular Sequence Data | Molecular Chaperones - chemistry | Cell Cycle Proteins - chemistry | Spindle Apparatus - genetics | Escherichia coli - metabolism | Cell Cycle Proteins - genetics | Carrier Proteins - chemistry | Nuclear Proteins - genetics | N-Ethylmaleimide-Sensitive Proteins - chemistry | Protein Structure, Tertiary | Recombinant Proteins - metabolism | ATPases Associated with Diverse Cellular Activities | Endopeptidase Clp - genetics | Escherichia coli Proteins - metabolism | Nuclear Proteins - metabolism | Endopeptidase Clp - metabolism | Mad2 Proteins - chemistry | Recombinant Proteins - genetics | Sequence Homology, Amino Acid | Carrier Proteins - genetics | Sequence Alignment | Animals | Carrier Proteins - metabolism | Adaptor Proteins, Signal Transducing - genetics | Mad2 Proteins - genetics | Escherichia coli Proteins - genetics | Protein Binding | Adenosine Triphosphatases - chemistry | Adaptor Proteins, Signal Transducing - metabolism | Spindle Apparatus - enzymology | Proteins | Medical research | Recombination | Software | Meiosis | Mammals | Chromosomes | DNA repair | Deoxyribonucleic acid--DNA | Adenosine triphosphatase | BASIC BIOLOGICAL SCIENCES
Journal Article
The Journal of biological chemistry, ISSN 1083-351X, 2014, Volume 289, Issue 3, pp. 1402 - 1414
...: We studied the chaperone activity of Hsp70 combined with four different NEFs and four J proteins... 
Protein Complexes | Protein Misfolding | Cochaperones | HIGH-THROUGHPUT SCREEN | MOLECULAR CHAPERONES | BIOCHEMISTRY & MOLECULAR BIOLOGY | QUALITY-CONTROL | Hsp40 | Protein Folding | HSP110 CHAPERONES | HEAT-SHOCK-PROTEIN | NEGATIVE REGULATOR | Isothermal Titration Calorimetry | J-DOMAIN | ATP HYDROLYSIS | STRUCTURAL BASIS | Molecular Chaperone | HSC70 CHAPERONE | ATPases | Protein-Protein Interactions | Adaptor Proteins, Signal Transducing - chemistry | Molecular Chaperones - metabolism | Transcription Factors - chemistry | Humans | Multiprotein Complexes - genetics | Molecular Chaperones - chemistry | DNA-Binding Proteins - metabolism | HSP110 Heat-Shock Proteins - chemistry | Multiprotein Complexes - metabolism | HSP70 Heat-Shock Proteins - chemistry | HSP40 Heat-Shock Proteins - chemistry | Recombinant Proteins - metabolism | HSP40 Heat-Shock Proteins - metabolism | HSP40 Heat-Shock Proteins - genetics | Molecular Chaperones - genetics | Recombinant Proteins - chemistry | HSP70 Heat-Shock Proteins - genetics | Recombinant Proteins - genetics | Transcription Factors - genetics | DNA-Binding Proteins - genetics | DNA-Binding Proteins - chemistry | HSP70 Heat-Shock Proteins - metabolism | Transcription Factors - metabolism | HSP110 Heat-Shock Proteins - genetics | Multiprotein Complexes - chemistry | Apoptosis Regulatory Proteins | Adaptor Proteins, Signal Transducing - genetics | Adaptor Proteins, Signal Transducing - metabolism | HSP110 Heat-Shock Proteins - metabolism | Protein Binding - physiology | Protein Synthesis and Degradation
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
Molecular cell, ISSN 1097-2765, 2019, Volume 74, Issue 6, pp. 1175 - 1188.e9
The condensin protein complex plays a key role in the structural organization of genomes... 
condensin | cohesin | SMC protein complex | ABC ATPase | genome organization | mitotic chromosome | structural biology | DNA loop extrusion | MOLECULAR-REPLACEMENT | FULLY-AUTOMATIC CHARACTERIZATION | STRUCTURE REFINEMENT | DATA-COLLECTION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | COHESIN RING | CHROMOSOME CONDENSATION | PROTEIN COMPLEXES | CRYSTALLOGRAPHY | DNA EXIT GATE | CELL BIOLOGY | Humans | Crystallography, X-Ray | Multiprotein Complexes - genetics | Saccharomyces cerevisiae - metabolism | Multiprotein Complexes - metabolism | Adenosine Triphosphate - metabolism | Binding Sites | Protein Subunits - genetics | Amino Acid Sequence | Gene Expression | Chromosomal Proteins, Non-Histone - metabolism | Adenosine Triphosphatases - metabolism | Models, Molecular | DNA - metabolism | Recombinant Fusion Proteins - chemistry | Saccharomyces cerevisiae Proteins - genetics | Nuclear Proteins - chemistry | DNA-Binding Proteins - chemistry | DNA - chemistry | Multiprotein Complexes - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Recombinant Fusion Proteins - genetics | Adenosine Triphosphatases - genetics | HeLa Cells | Saccharomyces cerevisiae Proteins - chemistry | Saccharomyces cerevisiae - genetics | Protein Multimerization | Recombinant Fusion Proteins - metabolism | Protein Subunits - metabolism | DNA-Binding Proteins - metabolism | Chromosomes - metabolism | Carrier Proteins - chemistry | Protein Interaction Domains and Motifs | Nuclear Proteins - genetics | Protein Conformation, alpha-Helical | Nuclear Proteins - metabolism | DNA-Binding Proteins - genetics | Chaetomium - genetics | Chromosomal Proteins, Non-Histone - genetics | DNA - genetics | Sequence Homology, Amino Acid | Carrier Proteins - genetics | Chaetomium - metabolism | Chromosomes - ultrastructure | Sequence Alignment | Carrier Proteins - metabolism | Protein Binding | Adenosine Triphosphatases - chemistry | Protein Subunits - chemistry | Adenosine Triphosphate - chemistry | Chromosomal Proteins, Non-Histone - chemistry | Proteins | Atoms | Genomics | Cells | Adenosine triphosphatase
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 37, pp. 15287 - 15300
A remarkable property of the machinery for import of peroxisomal matrix proteins is that it can accept already folded proteins as substrates... 
CONSERVED CYSTEINE | HUMAN PTS1 RECEPTOR | DOCKING PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | CYCLING RECEPTOR | MACHINERY | MEMBRANE-PROTEIN | II SECRETION SYSTEM | AAA PEROXINS | TARGETING SIGNAL RECEPTOR | IMPORT RECEPTOR | Humans | Protein Multimerization | Mutation, Missense | Recombinant Fusion Proteins - metabolism | Biological Transport | Gene Deletion | Receptors, Cytoplasmic and Nuclear - chemistry | Membrane Proteins - metabolism | Protein Interaction Domains and Motifs | Peptide Fragments - genetics | Repressor Proteins - metabolism | Recombinant Proteins - metabolism | Peptide Fragments - metabolism | Repressor Proteins - chemistry | Mutagenesis, Site-Directed | Membrane Proteins - genetics | Solubility | Recombinant Proteins - chemistry | Repressor Proteins - genetics | Receptors, Cytoplasmic and Nuclear - genetics | Recombinant Fusion Proteins - chemistry | Peroxisomes - metabolism | Amino Acid Motifs | Peptide Fragments - chemistry | Membrane Proteins - chemistry | Models, Biological | Peroxisome-Targeting Signal 1 Receptor | Endopeptidase K - metabolism | Mutation | Intracellular Membranes - metabolism | Amino Acid Substitution | Hydrogen-Ion Concentration | Receptors, Cytoplasmic and Nuclear - metabolism | ubiquitylation (ubiquitination) | docking | PEX5 | peroxisome | translocation module | protein import | protein sorting | receptor recycling | PEX14 | Cell Biology
Journal Article
Proceedings of the National Academy of Sciences - PNAS, ISSN 1091-6490, 2013, Volume 110, Issue 37, pp. 14942 - 14947
Journal Article