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Analytical Chemistry, ISSN 0003-2700, 09/2003, Volume 75, Issue 18, pp. 4740 - 4746
The creation and characterization of histidine-tagged fusion protein arrays using nitrilotriacetic acid (NTA) capture probes on gold thin films for the study... 
CHEMISTRY, ANALYTICAL | FILMS | MALTOSE-BINDING PROTEIN | SPR | RECOMBINANT PROTEINS | TATA BOX | PURIFICATION | TIME SAMPLING ELECTRONICS | MICROARRAYS | MONOLAYERS | IMMOBILIZATION | Proteins - chemistry | Recombinant Fusion Proteins - chemistry | Histidine - chemistry | Base Sequence | Proteins | Nitrilotriacetic acid | Research
Journal Article
Biochemical Journal, ISSN 0264-6021, 05/2015, Volume 468, Issue 1, pp. 145 - 158
The immediate early gene product Arc (activity-regulated cytoskeleton-associated protein) is posited as a master regulator of long-term synaptic plasticity and... 
Presenilin-1 | Arc | Oligomerization | Protein purification | Synaptic plasticity | Protein stability | Biophysical characterization | IMMEDIATE-EARLY GENE | CYTOSKELETON-ASSOCIATED PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | protein purification | INTRINSICALLY UNSTRUCTURED PROTEINS | ARC/ARG3.1 | biophysical characterization | protein stability | CONSOLIDATION | oligomerization | DENDRITIC SPINE | DIFFERENTIAL SCANNING FLUOROMETRY | SEQUENCE ALIGNMENTS | synaptic plasticity | LONG-TERM POTENTIATION | presenilin-1 | Cytoskeletal Proteins - genetics | Humans | Protein Multimerization | Molecular Sequence Data | Genetic Variation | Nerve Tissue Proteins - chemistry | Neuronal Plasticity - physiology | Protein Structure, Quaternary | Cytoskeletal Proteins - physiology | Protein Stability | Protein Structure, Tertiary | Amino Acid Sequence | Cell Line | Nerve Tissue Proteins - physiology | Biophysical Phenomena | Protein Structure, Secondary | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Cytoskeletal Proteins - chemistry | Microscopy, Electron | Nerve Tissue Proteins - genetics | Sequence Homology, Amino Acid | Presenilin-1 - metabolism | Protein Binding | Amino Acid Substitution | WT, wild-type | Dh, hydrodynamic diameter | HCA, hydrophobic cluster analysis | TBST, Tris-buffered saline | F-actin, filamentous actin | Aβ, amyloid β-peptide | hArc, human Arc | RT, room temperature | DSC, differential scanning calorimetry | DSF, differential scanning fluorimetry | AMPA, α-amino-3-hydroxy-5-methyl isoxazole-4-propionic acid | LTD, long-term depression | RU, response units | LTP, long-term potentiation | TEV, tobacco etch virus | DLS, dynamic light scattering | 0.1% Tween 20 | Ni-NTA, Ni2+-nitrilotriacetate | Trx, thioredoxin | Arc, activity-regulated cytoskeleton-associated protein | MBP, maltose-binding protein | PS1, presenilin-1 | SPR, surface plasmon resonance | APP, amyloid precursor protein
Journal Article
Journal Article
PLoS ONE, ISSN 1932-6203, 11/2012, Volume 7, Issue 11, p. e49589
Journal Article
Protein Science, ISSN 0961-8368, 08/2016, Volume 25, Issue 8, pp. 1535 - 1544
Manipulating single molecules and systems of molecules with mechanical force is a powerful technique to examine their physical properties. Applying force... 
magnetic tweezers | forced unfolding | optical tweezers | membrane protein | SpyTag | protein folding | SpyCatcher | Membrane protein | Optical tweezers | Protein folding | Magnetic tweezers | Forced unfolding | NSF | FORCE SPECTROSCOPY | PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | SNARE COMPLEX | BOND | PEPTIDE TAG | Staining and Labeling - methods | Protein Engineering - methods | Magnets | Recombinant Fusion Proteins - metabolism | DNA-Binding Proteins - metabolism | Endopeptidases - chemistry | Peptides - chemical synthesis | Peptides - metabolism | Cloning, Molecular | Escherichia coli - metabolism | Maltose-Binding Proteins - chemistry | Membrane Proteins - metabolism | Optical Tweezers | Maltose-Binding Proteins - genetics | Amino Acid Sequence | Endopeptidases - metabolism | Gene Expression | Peptides - chemistry | Membrane Proteins - genetics | Escherichia coli Proteins - metabolism | Maltose-Binding Proteins - metabolism | Recombinant Fusion Proteins - chemistry | DNA-Binding Proteins - genetics | DNA-Binding Proteins - chemistry | Protein Folding | Biomechanical Phenomena | DNA - chemistry | Endopeptidases - genetics | Membrane Proteins - chemistry | Escherichia coli - genetics | Escherichia coli Proteins - genetics | Recombinant Fusion Proteins - genetics | Lipid Bilayers - chemistry | Escherichia coli Proteins - chemistry | Dimyristoylphosphatidylcholine - chemistry | Proteins | Genetic research | Analysis | DNA | Methods | Deoxyribonucleic acid--DNA | Methods and Applications
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2009, Volume 106, Issue 34, pp. 14403 - 14407
The mitochondrial intermembrane space (IMS) contains many small cysteine-bearing proteins, and their passage across the outer membrane and subsequent folding... 
Proteins | Oxidases | Yeasts | Numberings | Mitochondria | Cell growth | Disulfides | Cytochromes | Oxidation | Crystal structure | Disulfide bond trasfer | Protein import | CYTOCHROME-C | RESPIRATORY-CHAIN | DISULFIDE RELAY SYSTEM | PATHWAY | MULTIDISCIPLINARY SCIENCES | crystal structure | ERV1 | protein import | IDENTIFICATION | MIA40 | disulfide bond trasfer | Saccharomyces cerevisiae - genetics | Immunoblotting | Genetic Complementation Test | Recombinant Fusion Proteins - metabolism | Cysteine - genetics | Mitochondrial Membrane Transport Proteins - genetics | Saccharomyces cerevisiae - metabolism | Disulfides - chemistry | X-Ray Diffraction | Carrier Proteins - chemistry | Cysteine - metabolism | Binding Sites | Maltose-Binding Proteins | Protein Structure, Tertiary | Mitochondrial Membrane Transport Proteins - chemistry | Mitochondrial Membrane Transport Proteins - metabolism | Protein Structure, Secondary | Crystallization | Models, Molecular | Cysteine - chemistry | Recombinant Fusion Proteins - chemistry | Saccharomyces cerevisiae Proteins - genetics | Static Electricity | Mitochondrial Membranes - metabolism | Carrier Proteins - genetics | Carrier Proteins - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Hydrophobic and Hydrophilic Interactions | Recombinant Fusion Proteins - genetics | Protein Conformation | Mutation | Saccharomyces cerevisiae - growth & development | Saccharomyces cerevisiae Proteins - chemistry | Cysteine | Yeast fungi | Physiological aspects | Research | Chemical properties | Structure | Protein binding | Biological Sciences
Journal Article
Biochemical and Biophysical Research Communications, ISSN 0006-291X, 02/2017, Volume 483, Issue 3, pp. 972 - 977
Signal peptides direct proteins from the cytoplasm to the periplasm. These N-terminal peptides are cleaved upon entry to the periplasm by either signal... 
Signal peptide | Signal peptidase I | Cleavage site | Secretion | Amino acid bias | TRANSLOCATION | MEMBRANE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | EXPORT | PREDICTION | GRAM-NEGATIVE BACTERIA | BIOPHYSICS | MALTOSE-BINDING PROTEIN | BACILLUS-SUBTILIS | PERIPLASM | RESIDUES | Saccharomyces cerevisiae - genetics | Archaeal Proteins - chemistry | Bacterial Proteins - chemistry | Bacillus subtilis - genetics | Serine Endopeptidases - genetics | Archaeal Proteins - genetics | Membrane Proteins - metabolism | Archaeal Proteins - metabolism | Amino Acid Sequence | Escherichia coli - enzymology | Membrane Proteins - genetics | Bacterial Proteins - genetics | Catalytic Domain - genetics | Escherichia coli Proteins - metabolism | Serine Endopeptidases - chemistry | Bacillus subtilis - enzymology | Saccharomyces cerevisiae Proteins - genetics | Amino Acid Motifs | Membrane Proteins - chemistry | Protein Sorting Signals - genetics | Escherichia coli - genetics | Saccharomyces cerevisiae Proteins - metabolism | Escherichia coli Proteins - genetics | Saccharomyces cerevisiae - enzymology | Bacterial Proteins - metabolism | Protein Processing, Post-Translational | Serine Endopeptidases - metabolism | Escherichia coli Proteins - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Proteins | Histidine | Proteases | Lysine | Analysis | Genomics
Journal Article
PLoS ONE, ISSN 1932-6203, 05/2016, Volume 11, Issue 5, p. e0155410
Sialyltransferases (STs) are disulfide-containing, type II transmembrane glycoproteins that catalyze the transfer of sialic acid to proteins and lipids and... 
CLONING | MULTIDISCIPLINARY SCIENCES | PURIFICATION | DISULFIDE BOND | GLYCOSYLATION | PROTEINS | GLYCOSYLTRANSFERASES | CHARGE | ALPHA-2,3-SIALYLTRANSFERASE | SOLUBILITY | REVEALS | Molecular Chaperones - metabolism | Protein Disulfide-Isomerases - metabolism | Humans | Substrate Specificity | Molecular Chaperones - chemistry | Antigens, CD - genetics | Oxidoreductases - chemistry | Recombinant Fusion Proteins - metabolism | Antigens, CD - metabolism | Sialyltransferases - chemistry | Cloning, Molecular | Escherichia coli - metabolism | Maltose-Binding Proteins - chemistry | Protein Engineering | Antigens, CD - chemistry | Protein Interaction Domains and Motifs | Maltose-Binding Proteins - genetics | Binding Sites | Gene Expression | Oxidoreductases - metabolism | Protein Structure, Secondary | Oxidoreductases - genetics | Molecular Chaperones - genetics | Sialyltransferases - genetics | Solubility | Models, Molecular | Maltose-Binding Proteins - metabolism | Recombinant Fusion Proteins - chemistry | Sialyltransferases - metabolism | Protein Folding | Protein Disulfide-Isomerases - genetics | Escherichia coli - genetics | Hydrophobic and Hydrophilic Interactions | Protein Binding | Recombinant Fusion Proteins - genetics | Protein Disulfide-Isomerases - chemistry | Glucosides - biosynthesis | Kinetics | Mutation | Amino Acid Substitution | Escherichia coli | Physiological aspects | Microbiological synthesis | Genetic aspects | Research | Recombinant proteins | Production processes | Amino acids | Lipids | Hydrophobicity | Sulfhydryl oxidase | Proteins | Synthesis | E coli | Protein folding | Chemical bonds | Bacteria | Folding | Milk | Recombinant | Enzymes | Disulfide bonds | N-acetyllactosamine | Glycoproteins | Maltose-binding protein | Oligosaccharides | Maltose | Sialic acids | Substrates | Lactose | Protein disulfide-isomerase | Cytoplasm | Cancer | Breast milk
Journal Article
Biotechnology and Bioengineering, ISSN 0006-3592, 10/2014, Volume 111, Issue 10, pp. 2019 - 2026
ABSTRACT We describe a new affinity purification tag called Car9 that confers proteins to which it is fused micromolar affinity for unmodified silica. When... 
fusion protein | affinity tag | proteolytic cleavage | purification | silica | Purification | Affinity tag | Fusion protein | Silica | Proteolytic cleavage | ESCHERICHIA-COLI | OMPT | MEMBRANE-PROTEIN | ADSORPTION BEHAVIOR | STRATEGIES | PEPTIDES | REMOVAL | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | FLUORESCENT PROTEIN | EXPRESSION | SURFACES | Recombinant Fusion Proteins - isolation & purification | Peptide Hydrolases - genetics | Peptides - genetics | Green Fluorescent Proteins - genetics | Recombinant Fusion Proteins - metabolism | Silicon Dioxide - metabolism | Peptides - metabolism | Maltose-Binding Proteins - isolation & purification | Escherichia coli - metabolism | Maltose-Binding Proteins - genetics | Bacterial Outer Membrane Proteins - genetics | Chromatography, Affinity - methods | Peptide Hydrolases - metabolism | Green Fluorescent Proteins - isolation & purification | Green Fluorescent Proteins - metabolism | Escherichia coli Proteins - metabolism | Maltose-Binding Proteins - metabolism | Hydrolysis | Peptides - isolation & purification | Bacterial Outer Membrane Proteins - metabolism | Escherichia coli - genetics | Escherichia coli Proteins - genetics | Protein Binding | Recombinant Fusion Proteins - genetics | Luminescent Proteins - genetics | Luminescent Proteins - isolation & purification | Luminescent Proteins - metabolism | Proteins | Adsorption | Proteases | Proteolysis | Escherichia coli | Liquid chromatography | Sugars | Protein binding | Pressure drop | Affinity | Silica gel | Devices | Silicon dioxide
Journal Article