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The FEBS Journal, ISSN 1742-464X, 01/2017, Volume 284, Issue 2, pp. 338 - 352
At the nuclear envelope, the inner nuclear membrane protein emerin contributes to the interface between the nucleoskeleton and the chromatin. Emerin is an... 
nuclear envelope | nucleoskeleton | lamin | oligomerization | intrinsically disordered region | folding | SUN PROTEINS | BIOCHEMISTRY & MOLECULAR BIOLOGY | BAF | COMPLEXES | LAMIN-A/C | IDENTIFICATION | DNA | ENVELOPE | DREIFUSS MUSCULAR-DYSTROPHY | NUCLEAR-MEMBRANE PROTEIN | MECHANOTRANSDUCTION | Humans | Protein Multimerization | Recombinant Fusion Proteins - metabolism | DNA-Binding Proteins - metabolism | Cloning, Molecular | Escherichia coli - metabolism | Membrane Proteins - metabolism | Protein Interaction Domains and Motifs | Nuclear Proteins - genetics | Binding Sites | Amino Acid Sequence | Protein Conformation, alpha-Helical | Gene Expression | Membrane Proteins - genetics | Models, Molecular | Nuclear Proteins - metabolism | Recombinant Fusion Proteins - chemistry | DNA-Binding Proteins - genetics | Nuclear Proteins - chemistry | DNA-Binding Proteins - chemistry | Sequence Alignment | Membrane Proteins - chemistry | Protein Conformation, beta-Strand | Escherichia coli - genetics | Protein Binding | Recombinant Fusion Proteins - genetics | Kinetics | Mutation | Oligomers | Protein binding | Proteins | Chromatin | Muscular dystrophy | Binding | Self assembly | Residues | Disulfide bonds | Oligomerization | Nuclear magnetic resonance--NMR | Emery-Dreifuss muscular dystrophy | Amino acids | Forming | Mutants | Defects | Membrane proteins | Fragmentation | Bridges | Self-assembly | Filaments | Resonance | Dystrophy | Emery | Structural analysis | Life Sciences
Journal Article
Biochemistry, ISSN 0006-2960, 06/2018, Volume 57, Issue 25, pp. 3460 - 3464
Journal Article
Structure, ISSN 0969-2126, 09/2016, Volume 24, Issue 9, pp. 1573 - 1581
Journal Article
Biochemical Journal, ISSN 0264-6021, 02/2017, Volume 474, Issue 4, pp. 539 - 556
Kindlins co-activate integrins alongside talin. They possess, like talin, a FERM domain (4.1-erythrin-radixin-moiesin domain) comprising F0-F3 subdomains, but... 
PERIPHERAL MEMBRANE-PROTEINS | GRP1 PH DOMAIN | INTEGRIN ALPHA-IIB-BETA-3 | MOLECULAR-DYNAMICS | MODEL MEMBRANES | ACTIVATION | COMPLEX | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | FORCE-FIELD | CELL-ADHESION | Cytoskeletal Proteins - genetics | Crystallography, X-Ray | Phosphatidylcholines - metabolism | Receptors, Cytoplasmic and Nuclear - chemistry | Cloning, Molecular | Escherichia coli - metabolism | Cytoskeletal Proteins - metabolism | Phosphatidylinositols - metabolism | Protein Interaction Domains and Motifs | Binding Sites | Pleckstrin Homology Domains | Recombinant Proteins - metabolism | Amino Acid Sequence | Protein Conformation, alpha-Helical | Gene Expression | Phosphatidylinositols - chemistry | Phosphatidylserines - metabolism | Phosphatidylserines - chemistry | Recombinant Proteins - chemistry | Receptors, Cytoplasmic and Nuclear - genetics | Recombinant Proteins - genetics | Cytoskeletal Proteins - chemistry | Phosphatidylcholines - chemistry | Molecular Dynamics Simulation | Sequence Homology, Amino Acid | Sequence Alignment | Animals | Protein Conformation, beta-Strand | Escherichia coli - genetics | Protein Binding | Mice | Kinetics | Receptors, Cytoplasmic and Nuclear - metabolism | Index Medicus | X-ray crystallography | lipid clustering | molecular dynamics | surface plasmon resonance | PH domain
Journal Article
Journal of Magnetism and Magnetic Materials, ISSN 0304-8853, 11/2019, Volume 489, p. 165420
The effect of torsion-induced acceleration of domain-wall motion has been discovered in magnetic glass-covered microwires. Torsion-stress application causes a... 
Domain wall motion | Magneto-optic Kerr effect | Helical domain structure | Amorphous magnetic microwires | Torsion stress | PHYSICS, CONDENSED MATTER | MATERIALS SCIENCE, MULTIDISCIPLINARY | SENSOR | PROPAGATION | Magnetic structure | Acceleration | Torsion | Domain walls
Journal Article
Structure, ISSN 0969-2126, 08/2018, Volume 26, Issue 8, pp. 1137 - 1143.e3
The kinase associated-1 (KA1) domain is found at the C-terminus of multiple Ser/Thr protein kinases from yeast to humans, and has been assigned autoinhibitory,... 
αD helix | Tau protein | serine/threonine protein kinase | C-terminal domain | structural biology | inhibitory mechanism | autoinhibition | activation segment | MARK1 | ACTIVATION | BIOPHYSICS | POLARITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | AMPK | LKB1 | BINDING | FEATURES | CELL BIOLOGY | Humans | Peptides - genetics | Substrate Specificity | Crystallography, X-Ray | Checkpoint Kinase 1 - chemistry | Thermodynamics | Peptides - metabolism | Cloning, Molecular | Escherichia coli - metabolism | Protein-Serine-Threonine Kinases - antagonists & inhibitors | Protein Interaction Domains and Motifs | Binding Sites | Protein-Serine-Threonine Kinases - metabolism | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Gene Expression | Genetic Vectors - chemistry | Peptides - chemistry | Protein-Serine-Threonine Kinases - genetics | Genetic Vectors - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Checkpoint Kinase 1 - metabolism | Protein Conformation, beta-Strand | Escherichia coli - genetics | Protein Binding | Protein-Serine-Threonine Kinases - chemistry | Structural Homology, Protein | Kinetics | Mutation | Checkpoint Kinase 1 - genetics | Medical colleges | Peptides | Structure | Protein kinases | Alzheimer's disease | Crystals | αD-helix | Serine | threonine protein kinase
Journal Article
The FEBS Journal, ISSN 1742-464X, 10/2017, Volume 284, Issue 19, pp. 3218 - 3229
Bridging integrator 1 (bin1) gene is a genetic determinant of Alzheimer's disease (AD) and has been reported to modulate Alzheimer's pathogenesis through... 
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
Structure, ISSN 0969-2126, 01/2018, Volume 26, Issue 1, pp. 72 - 84.e7
Ubiquitin-specific protease 7 (USP7) deubiquitinase activity is controlled by a number of regulatory factors, including stimulation by intramolecular accessory... 
USP7 | protein engineering | deubiquinating enzymes | molecular dynamics | Rosetta | UBIQUITIN-SPECIFIC PROTEASE | SYSTEM | RECOGNITION | MECHANISM | STABILIZATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | SIMULATION | CELL BIOLOGY | POTENT | BIOPHYSICS | CHEMISTRY | INHIBITORS | USP7/HAUSP | Peptidomimetics - chemical synthesis | Ubiquitin-Specific Peptidase 7 - chemistry | Humans | Substrate Specificity | Crystallography, X-Ray | Enzyme Inhibitors - chemical synthesis | Thermodynamics | Enzyme Inhibitors - chemistry | Cloning, Molecular | Escherichia coli - metabolism | Protein Interaction Domains and Motifs | Recombinant Proteins - metabolism | Amino Acid Sequence | Protein Conformation, alpha-Helical | Catalytic Domain | Gene Expression | Genetic Vectors - chemistry | Ubiquitin-Specific Peptidase 7 - genetics | Genetic Vectors - metabolism | Recombinant Proteins - chemistry | Peptidomimetics - chemistry | Recombinant Proteins - genetics | Ubiquitin-Specific Peptidase 7 - antagonists & inhibitors | Ubiquitin-Specific Peptidase 7 - metabolism | Static Electricity | Molecular Dynamics Simulation | Protein Conformation, beta-Strand | Escherichia coli - genetics | Hydrophobic and Hydrophilic Interactions | Protein Binding | Enzyme Activation | Kinetics | Mutation | Amino Acid Substitution | Ubiquitin | Cysteine | Proteases | Analysis | Crystals | Molecular dynamics | Structure
Journal Article