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Journal Article
Human Molecular Genetics, ISSN 0964-6906, 2/2008, Volume 17, Issue 3, pp. 345 - 356
Expanded polyglutamine (polyQ) repeats cause neurodegenerative disorders, but their cytotoxic structures remain to be elucidated. Although soluble polyQ... 
NEURONAL INTRANUCLEAR INCLUSIONS | EXPANSION PROTEINS | BIOCHEMISTRY & MOLECULAR BIOLOGY | MUTANT HUNTINGTIN | GENETICS & HEREDITY | AGGREGATE FORMATION | NEURODEGENERATION | TOXICITY | INHIBITORS | FIBRILLOGENESIS | MAMMALIAN-CELLS | PEPTIDE | Humans | Bacterial Proteins - chemistry | Peptides - genetics | Cercopithecus aethiops | DNA Primers - genetics | Green Fluorescent Proteins - genetics | Recombinant Fusion Proteins - metabolism | Nerve Tissue Proteins - chemistry | Peptides - metabolism | Peptides - toxicity | Transfection | Base Sequence | Protein Structure, Quaternary | Fluorescence Resonance Energy Transfer | Luminescent Proteins - chemistry | Neurons - metabolism | Green Fluorescent Proteins - chemistry | Inclusion Bodies - metabolism | Neurons - drug effects | Nuclear Proteins - genetics | Cell Line | Green Fluorescent Proteins - metabolism | Peptides - chemistry | Protein Structure, Secondary | Bacterial Proteins - genetics | Solubility | Models, Molecular | Nuclear Proteins - metabolism | Recombinant Fusion Proteins - chemistry | Nuclear Proteins - chemistry | Nerve Tissue Proteins - genetics | Nerve Tissue Proteins - metabolism | Huntingtin Protein | Animals | Recombinant Fusion Proteins - genetics | Bacterial Proteins - metabolism | Luminescent Proteins - genetics | COS Cells | Luminescent Proteins - metabolism | Index Medicus
Journal Article
The Journal of Physiology, ISSN 0022-3751, 11/2008, Volume 586, Issue 22, pp. 5383 - 5401
Ca 2+ entry through store‐operated Ca 2+ release‐activated Ca 2+ (CRAC) channels initiates key functions such as gene expression and exocytosis of inflammatory... 
PHYSIOLOGY | 2-AMINOETHOXYDIPHENYL BORATE | STIM1 | STROMAL INTERACTION MOLECULE-1 | OPERATED CALCIUM-CHANNELS | ACTIVATED CA2+ CHANNELS | STORE DEPLETION | OLIGOMERIZATION | PLASMA-MEMBRANE | NEUROSCIENCES | CRAC CHANNEL | T-LYMPHOCYTES | Protein Subunits | Calcium Channels - metabolism | Humans | Multiprotein Complexes | Bacterial Proteins - chemistry | Endoplasmic Reticulum - metabolism | Green Fluorescent Proteins - genetics | Neoplasm Proteins - metabolism | Recombinant Fusion Proteins - metabolism | Protein Structure, Quaternary | Fluorescence Resonance Energy Transfer | Luminescent Proteins - chemistry | Severe Combined Immunodeficiency - metabolism | Membrane Proteins - metabolism | Protein Interaction Domains and Motifs | Green Fluorescent Proteins - chemistry | Neoplasm Proteins - genetics | Calcium Channels - genetics | Calcium Signaling | Stromal Interaction Molecule 1 | Cell Line | Green Fluorescent Proteins - metabolism | Mutagenesis, Site-Directed | Membrane Proteins - genetics | Bacterial Proteins - genetics | Neoplasm Proteins - chemistry | Recombinant Fusion Proteins - chemistry | ORAI1 Protein | Severe Combined Immunodeficiency - genetics | Membrane Proteins - chemistry | Calcium Channels - chemistry | Recombinant Fusion Proteins - genetics | Bacterial Proteins - metabolism | Luminescent Proteins - genetics | Protein Conformation | Ion Channel Gating | Luminescent Proteins - metabolism | Fluorescence | Physiological aspects | Gene expression | Index Medicus | Cellular
Journal Article
Journal Article
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 6/2014, Volume 111, Issue 23, pp. 8452 - 8457
Journal Article
Science, ISSN 0036-8075, 5/2005, Volume 308, Issue 5726, pp. 1321 - 1323
The protein complement of cellular membranes is notoriously resistant to standard proteomic analysis and structural studies. As a result, membrane proteomes... 
Proteins | Datasets | Child abuse | Escherichia coli | Fluorescence | Reports | Cell membranes | Topology | Proteomes | Modeling | Membrane proteins | GREEN FLUORESCENT PROTEIN | EVOLUTION | EFFLUX | MULTIDRUG TRANSPORTER EMRE | ANGSTROM | MULTIDISCIPLINARY SCIENCES | X-RAY-STRUCTURE | CONDUCTING CHANNEL | SELECTIVITY | PREDICTION | Gene Duplication | Green Fluorescent Proteins - genetics | Escherichia coli Proteins - physiology | Membrane Proteins - analysis | Recombinant Fusion Proteins | Cell Membrane - chemistry | Membrane Proteins - physiology | Cloning, Molecular | Alkaline Phosphatase - analysis | Periplasm - chemistry | Escherichia coli Proteins - analysis | Cytoplasm - chemistry | Genes, Bacterial | Alkaline Phosphatase - genetics | Green Fluorescent Proteins - analysis | Protein Structure, Secondary | Membrane Proteins - genetics | Computational Biology | Proteome | Escherichia coli - chemistry | Membrane Proteins - chemistry | Escherichia coli - genetics | Escherichia coli Proteins - genetics | Escherichia coli Proteins - chemistry | Escherichia coli - ultrastructure | Gene amplification | Physiological aspects | Genetic aspects | Research | Pathogens | Membranes | Bioinformatics | Genomics | Index Medicus | Green Fluorescent Proteins/analysis/genetics | Periplasm/chemistry | Escherichia coli/chemistry/genetics/ultrastructure | Cytoplasm/chemistry | Alkaline Phosphatase/analysis/genetics | Cloning; Molecular | Protein Structure; Secondary | Escherichia coli Proteins/analysis/chemistry/genetics/physiology | Cell Membrane/chemistry | Membrane Proteins/analysis/chemistry/genetics/physiology | Genes; Bacterial
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2018, Volume 293, Issue 8, pp. 2959 - 2973
Most proteins that reside in the bacterial outer membrane (OM) have a distinctive "beta-barrel" architecture, but the assembly of these proteins is poorly... 
IN-VITRO | GRAM-NEGATIVE BACTERIA | CONFORMATIONAL-CHANGES | BETA-BARREL | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | AUTOTRANSPORTER | BARREL ASSEMBLY MACHINERY | YAET COMPLEX | SECRETION | MOLECULAR-BASIS | Protein Multimerization | Porins - metabolism | Recombinant Fusion Proteins - metabolism | Lipid-Linked Proteins - metabolism | Escherichia coli - metabolism | Serine Endopeptidases - genetics | Porins - chemistry | Protein Interaction Domains and Motifs | Peptide Fragments - genetics | Bacterial Outer Membrane Proteins - genetics | Protein Conformation, alpha-Helical | Peptide Fragments - metabolism | Porins - genetics | Bacterial Outer Membrane Proteins - chemistry | Escherichia coli Proteins - metabolism | Serine Endopeptidases - chemistry | Recombinant Fusion Proteins - chemistry | Escherichia coli - chemistry | Protein Folding | Protein Transport | Peptide Fragments - chemistry | Bacterial Outer Membrane Proteins - metabolism | Protein Conformation, beta-Strand | Escherichia coli Proteins - genetics | Serine Endopeptidases - metabolism | Lipid Bilayers - chemistry | Lipid Bilayers - metabolism | Liposomes | Escherichia coli Proteins - chemistry | Lipid-Linked Proteins - genetics | Lipid-Linked Proteins - chemistry | Index Medicus | outer membrane | molecular chaperone | beta-barrel proteins | Bam complex | protein-lipid interaction | Membrane Biology | membrane protein | protein folding | Gram-negative bacteria
Journal Article
Science, ISSN 0036-8075, 3/2006, Volume 311, Issue 5767, pp. 1600 - 1603
We directly observed real-time production of single protein molecules in individual Escherichia coli cells. A fusion protein of a fast-maturing yellow... 
Proteins | Molecules | Messenger RNA | Lasers | DNA | Cell lines | Cell cycle | Polynesian studies | Fluorescence | Reports | Gene expression | MESSENGER-RNA DEGRADATION | SINGLE-CELL | GREEN FLUORESCENT PROTEIN | OPERATOR | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | TRANSCRIPTION | NOISE | TRANSLATION | REPRESSOR | Molecular Probe Techniques | Recombinant Fusion Proteins - analysis | Bacterial Proteins - analysis | RNA, Messenger - metabolism | Membrane Proteins - analysis | Luminescent Proteins - biosynthesis | Escherichia coli K12 - metabolism | Luminescent Proteins - analysis | Stochastic Processes | Escherichia coli Proteins - biosynthesis | RNA, Bacterial - genetics | Escherichia coli Proteins - analysis | RNA, Bacterial - metabolism | Recombinant Fusion Proteins - biosynthesis | Promoter Regions, Genetic | Gene Expression | Membrane Proteins - genetics | RNA, Messenger - genetics | Bacterial Proteins - genetics | Gene Expression Profiling - methods | Reverse Transcriptase Polymerase Chain Reaction | Blotting, Western | Membrane Proteins - biosynthesis | Escherichia coli Proteins - genetics | Luminescent Proteins - genetics | Poisson Distribution | Bacterial Proteins - biosynthesis | Escherichia coli K12 - genetics | Microscopy, Fluorescence | Research | Molecular biology | Structure | Genes | Analysis | Bacteria | Peptides | Cells | Index Medicus
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2018, Volume 293, Issue 8, pp. 2744 - 2754
Clustered regularly interspaced short palindromic repeats (CRISPRs) and CRISPR-associated (Cas) proteins provide microbial adaptive immunity against... 
INHIBITION | GENETIC ELEMENTS | BIOCHEMISTRY & MOLECULAR BIOLOGY | CRYO-EM STRUCTURES | BACTERIAL IMMUNE-SYSTEM | CLASSIFICATION | MECHANISMS | SURVEILLANCE COMPLEX | REPEATS | VIRAL SUPPRESSORS | PROKARYOTES | Xanthomonas - metabolism | CRISPR-Associated Proteins - chemistry | Species Specificity | Protein Multimerization | Bacterial Proteins - chemistry | Crystallography, X-Ray | Recombinant Fusion Proteins - metabolism | Viral Proteins - metabolism | Xanthomonas - immunology | CRISPR-Associated Proteins - antagonists & inhibitors | RNA, Small Interfering - chemistry | RNA Interference | Clustered Regularly Interspaced Short Palindromic Repeats | Protein Stability | RNA, Bacterial - metabolism | Bacterial Proteins - antagonists & inhibitors | CRISPR-Associated Proteins - genetics | Isoenzymes | Viral Proteins - chemistry | Bacterial Proteins - genetics | Enzyme Stability | Models, Molecular | Viral Proteins - genetics | Recombinant Fusion Proteins - chemistry | RNA Stability | CRISPR-Associated Proteins - metabolism | RNA, Bacterial - chemistry | CRISPR-Cas Systems | Xanthomonas - enzymology | Bacterial Proteins - metabolism | Protein Conformation | Kinetics | Mutation | Amino Acid Substitution | RNA, Small Interfering - metabolism | Index Medicus | X-ray crystallography | Protein Structure and Folding | CRISPR | anti-CRISPR | Cas | crystal structure | protein-protein interaction | protein complex | RNA-protein interaction | crRNA
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2012, Volume 109, Issue 50, pp. 20431 - 20436
Cellulose-degrading enzyme systems are of significant interest from both a scientific and technological perspective due to the diversity of cellulase families,... 
Cantilevers | Proteins | Enzymes | Histograms | Spectroscopy | Calcium | Cellulosomes | Amino acids | Loading rate | Crystal structure | Molecular recognition | Protein unfolding | RECOGNITION | NUCLEIC-ACID | PROTEIN-STRUCTURE | MULTIDISCIPLINARY SCIENCES | IMMUNOGLOBULIN | ADHESION | protein unfolding | ATOMIC-FORCE MICROSCOPY | SPECTROSCOPY | BONDS | molecular recognition | TITIN KINASE | BINDING | Calcium - metabolism | Protein Multimerization | Bacterial Proteins - chemistry | Crystallography, X-Ray | Recombinant Fusion Proteins - metabolism | Cell Cycle Proteins - chemistry | Thermodynamics | Clostridium thermocellum - metabolism | Cell Cycle Proteins - genetics | Microscopy, Atomic Force | Protein Interaction Domains and Motifs | Protein Stability | Mutagenesis, Site-Directed | Chromosomal Proteins, Non-Histone - metabolism | Bacterial Proteins - genetics | Cell Cycle Proteins - metabolism | Models, Molecular | Biophysics | Recombinant Fusion Proteins - chemistry | Unfolded Protein Response | Chromosomal Proteins, Non-Histone - genetics | Multiprotein Complexes - chemistry | Hydrogen Bonding | Recombinant Fusion Proteins - genetics | Bacterial Proteins - metabolism | Clostridium thermocellum - genetics | Chromosomal Proteins, Non-Histone - chemistry | Amino Acid Substitution | Physiological aspects | Research | Molecular biology |