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2011, Methods in molecular biology, ISBN 9781617379666, Volume 705., xi, 310
Book
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
Annual Review of Biochemistry, ISSN 0066-4154, 6/2016, Volume 85, Issue 1, pp. 715 - 742
Molecular chaperones control the cellular folding, assembly, unfolding, disassembly, translocation, activation, inactivation, disaggregation, and degradation... 
Hsp70 | Hsp60 | unfoldases | Hsp104 | sHsps | protein homeostasis | heat-shock proteins | Hsp110 | small heat-shock proteins | Heat-shock proteins | Small heat-shock proteins | SHsps | Unfoldases | Protein homeostasis | BACTERIOPHAGE-LAMBDA | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | SUBUNIT BINDING-PROTEIN | ALPHA-B-CRYSTALLIN | QUALITY-CONTROL | RIBULOSEBISPHOSPHATE-CARBOXYLASE | HEAT-SHOCK-PROTEIN | ATP HYDROLYSIS | LAMBDA-DNA-REPLICATION | RIBULOSE-BISPHOSPHATE CARBOXYLASE | Protein Aggregates | Rhodospirillum rubrum - metabolism | Protein Unfolding | Humans | Mitochondrial Proteins - genetics | HSP110 Heat-Shock Proteins - chemistry | Mitochondrial Proteins - metabolism | Adenosine Triphosphate - metabolism | Escherichia coli - metabolism | Protein Structure, Quaternary | Chaperonin 60 - metabolism | HSP70 Heat-Shock Proteins - chemistry | Rhodospirillum rubrum - chemistry | Chaperonin 60 - chemistry | Chaperonin 60 - genetics | Gene Expression | Heat-Shock Proteins, Small - chemistry | Heat-Shock Proteins, Small - metabolism | Models, Molecular | HSP70 Heat-Shock Proteins - genetics | Escherichia coli - chemistry | Protein Folding | HSP70 Heat-Shock Proteins - metabolism | HSP110 Heat-Shock Proteins - genetics | Heat-Shock Proteins, Small - genetics | Mitochondrial Proteins - chemistry | Adenosine Triphosphate - chemistry | HSP110 Heat-Shock Proteins - metabolism | Molecular chaperones | Observations | Protein folding | Health aspects
Journal Article
Nature, ISSN 0028-0836, 07/2015, Volume 523, Issue 7562, pp. 555 - 560
Journal Article
Journal Article
Nucleic Acids Research, ISSN 0305-1048, 02/2018, Volume 46, Issue 3, pp. 1470 - 1485
Abstract In Pseudomonas aeruginosa the RNA chaperone Hfq and the catabolite repression control protein (Crc) act as post-transcriptional regulators during... 
POSTTRANSCRIPTIONAL REGULATION | RPOS MESSENGER-RNA | CHAPERONE HFQ | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | CROSS-LINKING | GLOBAL REGULATOR | SOLUBLE-RNA | BINDING | SIGNAL-TRANSDUCTION PATHWAY | MASS-SPECTROMETRY | RNA Prot Comp
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 12/2010, Volume 285, Issue 52, pp. 40573 - 40580
Secretion of the Escherichia coli toxin hemolysin A (HlyA) is catalyzed by the membrane protein complex HlyB-HlyD-TolC and requires a secretion sequence... 
SIGNAL | ANTIFOLDING ACTIVITY | SECB CHAPERONE | TRANSPORTER | MALTOSE-BINDING PROTEIN | MEMBRANE TRANSLOCATION | PATHWAY | BIOCHEMISTRY & MOLECULAR BIOLOGY | IN-VIVO | EXPORT | EXPRESSION | Hemolysin Proteins - genetics | Bacterial Proteins - genetics | Escherichia coli Proteins - metabolism | Hemolysin Proteins - secretion | Multiprotein Complexes - genetics | Mutation, Missense | Bacterial Secretion Systems - physiology | Protein Folding | Carrier Proteins - genetics | Multiprotein Complexes - metabolism | Carrier Proteins - metabolism | Bacterial Outer Membrane Proteins - metabolism | Escherichia coli - genetics | Membrane Transport Proteins - genetics | Escherichia coli - metabolism | Escherichia coli Proteins - genetics | Escherichia coli Proteins - secretion | Bacterial Proteins - metabolism | Membrane Transport Proteins - metabolism | Periplasmic Binding Proteins - genetics | Bacterial Outer Membrane Proteins - genetics | Hemolysin Proteins - metabolism | Amino Acid Substitution | Periplasmic Binding Proteins - metabolism | Bacterial Outer Membrane Proteins | Bacterial Secretion Systems | Hemolysin Proteins | Escherichia coli | Multiprotein Complexes | Biochemistry, Molecular Biology | Bacterial Proteins | Life Sciences | Microbiology and Parasitology | Escherichia coli Proteins | Membrane Transport Proteins | Periplasmic Binding Proteins | Carrier Proteins | Membrane Proteins | Fusion Protein | Secretion | Membrane Biology | ABC Transporter
Journal Article
eLife, ISSN 2050-084X, 04/2015, Volume 2015, 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... 
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
Journal Article