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Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 35, pp. 14617 - 14624
Using the energy of ATP hydrolysis, ABC transporters catalyze the trans-membrane transport of molecules. In bacteria, these transporters partner with a... 
ANTHRACIS VIRULENCE DETERMINANT | MALTOSE TRANSPORT | BTUCD-F | MECHANISM | YERSINIA-PESTIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | CASSETTE TRANSPORTER | CRYSTAL-STRUCTURES | MULTIDRUG-RESISTANCE | HISTIDINE PERMEASE | Surface Plasmon Resonance | Hemeproteins - genetics | Heme - metabolism | Protein Multimerization | Bacterial Proteins - chemistry | Holoenzymes - chemistry | Recombinant Proteins | Cell Membrane - chemistry | ATP-Binding Cassette Transporters - chemistry | Holoenzymes - metabolism | ATP-Binding Cassette Transporters - genetics | Heme - chemistry | Adenosine Triphosphate - metabolism | Hemeproteins - chemistry | Apoenzymes - metabolism | ATP-Binding Cassette Transporters - metabolism | Carrier Proteins - chemistry | Receptors, Cell Surface - chemistry | Cell Membrane - metabolism | Protein Interaction Domains and Motifs | Dimerization | Immobilized Proteins - chemistry | Yersinia pestis - metabolism | Hemeproteins - metabolism | Immobilized Proteins - genetics | Bacterial Proteins - genetics | Models, Molecular | Receptors, Cell Surface - metabolism | Hydrolysis | Carrier Proteins - genetics | Carrier Proteins - metabolism | Apoenzymes - genetics | Immobilized Proteins - metabolism | Apoenzymes - chemistry | Bacterial Proteins - metabolism | Holoenzymes - genetics | Molecular Docking Simulation | Kinetics | Adenosine Triphosphate - chemistry | Receptors, Cell Surface - genetics | Index Medicus | Membrane Biology | ATPase | membrane protein | protein-protein interaction | surface plasmon resonance (SPR) | ABC transporter | ATP
Journal Article
Protein Expression and Purification, ISSN 1046-5928, 01/2019, Volume 153, pp. 131 - 137
This work describes a novel strategy for the integrated expression and purification of recombinant proteins in cultures. Hydrophobins can be used as fusion... 
Domain III | Hydrophobin | In situ product removal | Pichia pastoris | Dengue virus | POTENTIAL USE | ASSAY | HFBI | BIOCHEMISTRY & MOLECULAR BIOLOGY | INSECT CELLS | BIOCHEMICAL RESEARCH METHODS | AQUEOUS 2-PHASE SYSTEMS | SEROLOGICAL DIAGNOSIS | IMMOBILIZATION | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | RECOMBINANT PROTEINS | PURIFICATION | EXPRESSION | Consensus Sequence | Fungal Proteins - chemistry | Recombinant Fusion Proteins - isolation & purification | Viral Envelope Proteins - isolation & purification | Polyethylene Glycols - chemistry | Recombinant Fusion Proteins - metabolism | Pichia - metabolism | Cloning, Molecular - methods | Viral Envelope Proteins - metabolism | Protein Domains | Culture Media - chemistry | Fungal Proteins - isolation & purification | Amino Acid Sequence | Gene Expression | Viral Envelope Proteins - genetics | Immobilized Proteins - chemistry | Genetic Vectors - chemistry | Immobilized Proteins - isolation & purification | Solid Phase Microextraction - methods | Immobilized Proteins - genetics | Genetic Vectors - metabolism | Trichoderma - genetics | Fungal Proteins - genetics | Recombinant Fusion Proteins - chemistry | Dengue Virus - chemistry | Dengue Virus - genetics | Viral Envelope Proteins - chemistry | Immobilized Proteins - metabolism | Pichia - genetics | Hydrophobic and Hydrophilic Interactions | Recombinant Fusion Proteins - genetics | Dengue Virus - metabolism | Fungal Proteins - metabolism | Trichoderma - metabolism | Viral antibodies | Detergents, Synthetic | Adsorption | Dengue viruses | Antibodies | Fermentation | Recombinant proteins
Journal Article
Journal of Clinical Investigation, ISSN 0021-9738, 06/2013, Volume 123, Issue 6, pp. 2434 - 2446
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 02/2016, Volume 291, Issue 9, pp. 4343 - 4355
A bacterial collagen-like protein Scl2 has been developed as a recombinant collagen model system to host human collagen ligand-binding sequences, with the goal... 
STREPTOCOCCUS-PYOGENES | PROTEIN | PEPTIDES | STABILITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | SITES | TYROSINE KINASES | TRIPLE-HELICES | IDENTIFICATION | CLEAVAGE | DDR2 | Humans | Bacterial Proteins - chemistry | Collagen Type III - metabolism | Collagen - chemistry | Recombinant Fusion Proteins - metabolism | Discoidin Domain Receptors | HEK293 Cells | Protein Engineering | Receptor Protein-Tyrosine Kinases - antagonists & inhibitors | Streptococcus pyogenes | Collagen - genetics | Protein Interaction Domains and Motifs | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Megakaryocytes - cytology | Megakaryocytes - metabolism | Binding Sites | Peptide Fragments - genetics | Peptide Fragments - metabolism | Immobilized Proteins - chemistry | Receptors, Mitogen - antagonists & inhibitors | Immobilized Proteins - genetics | Bacterial Proteins - genetics | Cells, Cultured | Collagen Type III - chemistry | Models, Molecular | Receptors, Mitogen - metabolism | Collagen Type III - genetics | Fetal Blood - cytology | Receptors, Mitogen - chemistry | Recombinant Fusion Proteins - chemistry | Receptor Protein-Tyrosine Kinases - metabolism | Collagen - metabolism | Peptide Fragments - chemistry | Receptor Protein-Tyrosine Kinases - genetics | Immobilized Proteins - metabolism | Recombinant Fusion Proteins - genetics | Bacterial Proteins - metabolism | Ligands | Receptor Protein-Tyrosine Kinases - chemistry | Cell Movement | Receptors, Mitogen - genetics | Index Medicus | discoidin domain receptor | inhibition mechanism | triple-helix | collagen | peptides | binding | Glycobiology and Extracellular Matrices | recombinant protein expression | protein chimera
Journal Article
PLoS ONE, ISSN 1932-6203, 07/2017, Volume 12, Issue 7, pp. e0181171 - e0181171
We examined the movement of an actin filament sliding on a mixture of normal and genetically modified myosin molecules that were attached to a glass surface.... 
REACTIVE THIOL REGION | F-ACTIN | INHIBITION | FORCE GENERATION | MULTIDISCIPLINARY SCIENCES | MOTOR DOMAIN | SURFACE | ACTOMYOSIN | FIXED H-MEROMYOSIN | ATP | G680V | Actins - metabolism | Multiprotein Complexes - genetics | Muscle, Skeletal - metabolism | Protozoan Proteins - genetics | Molecular Motor Proteins - genetics | Recombinant Fusion Proteins - metabolism | Multiprotein Complexes - metabolism | Movement - physiology | Protozoan Proteins - metabolism | Myosin Type II - metabolism | Actins - chemistry | Molecular Motor Proteins - metabolism | Protozoan Proteins - chemistry | Myosin Type II - genetics | Microscopy, Electron, Transmission | Rabbits | Immobilized Proteins - chemistry | Myosin Subfragments - metabolism | Mutant Proteins - genetics | Mutant Proteins - metabolism | Myosin Subfragments - chemistry | Recombinant Fusion Proteins - chemistry | Molecular Motor Proteins - chemistry | Multiprotein Complexes - chemistry | Animals | Mutant Proteins - chemistry | Immobilized Proteins - metabolism | Dictyostelium - genetics | Recombinant Fusion Proteins - genetics | Dictyostelium - metabolism | In Vitro Techniques | Myosin Type II - chemistry | Dictyostelium | Actin | Analysis | Myosin | Muscles | Research | Health aspects | Bioengineering | Biomedical research | Motility | Glass | Sliding | Biochemistry | Copolymerization | Motor task performance | Assaying | ADP | Velocity | Skeletal muscle | Proteins | Musculoskeletal system | Chemistry | Hypotheses | Filaments | Mutation | Fusion protein | Acceleration | In vitro methods and tests | Genetic modification | Index Medicus
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2018, Volume 293, Issue 8, pp. 2640 - 2649
Transglutaminase 2 (TG2) is a ubiquitously expressed, intracellular as well as extracellular protein with multiple modes of post-translational regulation,... 
SELECTIVE-INHIBITION | HUMAN THIOREDOXIN-1 | ACTIVE-SITE | THROMBUS FORMATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ISOMERASE | THIOL-DISULFIDE EXCHANGE | EXTRACELLULAR-MATRIX | QUIESCIN-SULFHYDRYL OXIDASE | TISSUE TRANSGLUTAMINASE | CELIAC-DISEASE | Enzymes, Immobilized - metabolism | Oxidants - pharmacology | Human Umbilical Vein Endothelial Cells - metabolism | Membrane Glycoproteins - metabolism | Glutathione - metabolism | Protein Disulfide-Isomerases - metabolism | GTP-Binding Proteins - antagonists & inhibitors | Humans | Membrane Glycoproteins - chemistry | Oxidants - metabolism | Extracellular Matrix - metabolism | Transglutaminases - genetics | Protein Disulfide-Isomerases - antagonists & inhibitors | Protein Transport - drug effects | GTP-Binding Proteins - genetics | Thioredoxins - genetics | Oxidoreductases Acting on Sulfur Group Donors - chemistry | Protein Processing, Post-Translational - drug effects | RNA Interference | Biocatalysis - drug effects | Human Umbilical Vein Endothelial Cells - cytology | Thioredoxins - metabolism | Peptide Fragments - genetics | Transglutaminases - antagonists & inhibitors | Transglutaminases - chemistry | Allosteric Regulation - drug effects | Oxidoreductases Acting on Sulfur Group Donors - metabolism | Recombinant Proteins - metabolism | Peptide Fragments - metabolism | GTP-Binding Proteins - chemistry | Oxidation-Reduction | Extracellular Matrix - drug effects | Cells, Cultured | Hydrogen Peroxide - pharmacology | Recombinant Proteins - chemistry | Membrane Glycoproteins - genetics | Extracellular Matrix - enzymology | Peptide Fragments - chemistry | Protein Disulfide-Isomerases - genetics | Human Umbilical Vein Endothelial Cells - enzymology | Cystine - metabolism | Transglutaminases - metabolism | Oxidoreductases Acting on Sulfur Group Donors - genetics | Enzymes, Immobilized - antagonists & inhibitors | GTP-Binding Proteins - metabolism | Index Medicus | Editors' Picks | post-translational modification (PTM) | PDIA3 | transglutaminase | thioredoxin | disulfide | oxidation-reduction (redox) | ERp57 | redox switch | celiac disease | transglutaminase 2 | protein disulfide isomerase family A member 3
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 32, pp. 13345 - 13360
Spontaneous activation enables the complement system to respond very rapidly to diverse threats. This activation is efficiently suppressed by complement factor... 
TRANSLATIONAL MINIREVIEW SERIES | HEMOLYTIC-UREMIC SYNDROME | PROTEIN | ALTERNATIVE PATHWAY | C-TERMINUS | STRUCTURAL BASIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | RISK | FUNCTIONAL-CHARACTERIZATION | BINDING-SITES | DECAY ACCELERATION | Complement C3d - genetics | Complement Factor I - chemistry | Complement Activation | Sheep, Domestic | Humans | Bacterial Proteins - chemistry | Erythrocytes - chemistry | Recombinant Fusion Proteins - metabolism | Complement C3d - metabolism | Streptococcus pneumoniae - metabolism | Surface Properties | Complement C3d - chemistry | Protein Interaction Domains and Motifs | Atypical Hemolytic Uremic Syndrome - genetics | Binding Sites | Peptide Fragments - genetics | Hemolysis | Peptide Fragments - metabolism | Complement C3 Convertase, Alternative Pathway - chemistry | Immobilized Proteins - chemistry | Complement C3 Convertase, Alternative Pathway - metabolism | Immobilized Proteins - genetics | Bacterial Proteins - genetics | Solubility | Complement Factor I - genetics | Recombinant Fusion Proteins - chemistry | Macular Degeneration - metabolism | Peptide Fragments - chemistry | Animals | Complement Factor H - metabolism | Macular Degeneration - genetics | Atypical Hemolytic Uremic Syndrome - metabolism | Immobilized Proteins - metabolism | Bacterial Proteins - metabolism | Mutation | Complement Factor H - genetics | Complement Factor I - metabolism | Complement C3 Convertase, Alternative Pathway - genetics | Amino Acid Substitution | Complement Factor H - chemistry | Index Medicus | kidney | Immunology | Streptococcus | innate immunity | complement system | recombinant protein expression | surface plasmon resonance (SPR) | multiple domain | mutagenesis | CCP module | erythrocyte
Journal Article
Biochemical Journal, ISSN 0264-6021, 07/2014, Volume 461, Issue 2, pp. 291 - 304
Gram-negative bacteria use the Type VI secretion system (T6SS) to inject toxic proteins into rival bacteria or eukaryotic cells. However, the mechanism of the... 
Type VI secretion system (T6SS) | Native complex isolation | Bacterial protein secretion | Protein oligomerization | Serratia marcescens | WIDESPREAD | CELLS | INNER MEMBRANE | BIOCHEMISTRY & MOLECULAR BIOLOGY | SERRATIA-MARCESCENS | ENTEROAGGREGATIVE ESCHERICHIA-COLI | VIBRIO-CHOLERAE | EFFECTOR | bacterial protein secretion | native complex isolation | PSEUDOMONAS-AERUGINOSA | TAIL | protein oligomerization | PROTEIN SECRETION | Recombinant Proteins - metabolism | Bacterial Secretion Systems - genetics | Membrane Proteins - genetics | Protein Multimerization | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Molecular Sequence Data | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Serratia marcescens - chemistry | Serratia marcescens - metabolism | Serratia marcescens - genetics | Membrane Proteins - chemistry | Base Sequence | Bacterial Proteins - metabolism | Membrane Proteins - metabolism | Gene Expression Regulation, Bacterial | Index Medicus | AUC, analytical ultracentrifugation | DDM, dodecyl maltoside | IMAC, immobilized ion-affinity chromatography | TEV, tobacco etch virus | T6SS, Type VI secretion system | EAEC, enteroaggregative Escherichia coli | AAA+, ATPase associated with diverse cellular activities | RNAPβ, RNA polymerase β | SEC, size-exclusion chromatography | SE, sedimentation equilibrium | MBP, maltose-binding protein | SV, sedimentation velocity
Journal Article
Applied and Environmental Microbiology, ISSN 0099-2240, 2014, Volume 80, Issue 10, pp. 3062 - 3071
Bacterial inclusion bodies are aggregations of mostly inactive and misfolded proteins. However, previously the in vivo self-assembly of green fluorescent... 
POLYHYDROXYALKANOATE SYNTHASE | PHOSPHOTRIESTERASE | INCLUSIONS | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | ESCHERICHIA-COLI | BACILLUS-LICHENIFORMIS | PURIFICATION | SURFACE | MICROBIOLOGY | N-ACETYLNEURAMINATE LYASE | PARATHION HYDROLASE | ALPHA-AMYLASE | Enzymes, Immobilized - metabolism | Inclusion Bodies - chemistry | Bacterial Proteins - chemistry | Agrobacterium tumefaciens - genetics | Green Fluorescent Proteins - genetics | Recombinant Fusion Proteins - metabolism | alpha-Amylases - genetics | Oxo-Acid-Lyases - genetics | Oxo-Acid-Lyases - metabolism | Agrobacterium tumefaciens - enzymology | Green Fluorescent Proteins - chemistry | Inclusion Bodies - metabolism | Enzymes, Immobilized - chemistry | Green Fluorescent Proteins - metabolism | Phosphoric Monoester Hydrolases - genetics | Escherichia coli - enzymology | Bacterial Proteins - genetics | Enzyme Stability | Bacillus - genetics | alpha-Amylases - metabolism | Recombinant Fusion Proteins - chemistry | Protein Folding | Oxo-Acid-Lyases - chemistry | Inclusion Bodies - genetics | Enzymes, Immobilized - genetics | Bacillus - enzymology | Escherichia coli - genetics | alpha-Amylases - chemistry | Recombinant Fusion Proteins - genetics | Bacterial Proteins - metabolism | Phosphoric Monoester Hydrolases - metabolism | Hydrogen-Ion Concentration | Phosphoric Monoester Hydrolases - chemistry | Fluorescence | Enzymes | Synthesis | Research | Protein folding | Analysis | Proteins | Probiotics | Bioremediation | Biomass | E coli | Index Medicus | Enzymology and Protein Engineering
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 02/2017, Volume 114, Issue 7, pp. E1128 - E1137
Journal Article
Biosensors and Bioelectronics, ISSN 0956-5663, 09/2015, Volume 71, pp. 214 - 221
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Journal Article