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biochemistry & molecular biology (308) 308
phosphate-binding proteins (224) 224
animals (198) 198
phosphates - metabolism (194) 194
index medicus (149) 149
amino acid sequence (145) 145
molecular sequence data (145) 145
carrier proteins - metabolism (140) 140
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phosphates (87) 87
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cell biology (64) 64
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rats (58) 58
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phosphate-binding protein (56) 56
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inorganic-phosphate (35) 35
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phosphates - chemistry (31) 31
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phosphate-binding (30) 30
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cloning, molecular (29) 29
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transport (29) 29
adenosine triphosphate - metabolism (28) 28
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phosphorylation (27) 27
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mice (26) 26
phosphate (26) 26
protein structure, tertiary (26) 26
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saccharomyces-cerevisiae (22) 22
substrate specificity (22) 22
mitochondria, liver - metabolism (21) 21
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PLoS Pathogens, ISSN 1553-7366, 07/2017, Volume 13, Issue 7, p. e1006515
We have previously shown that the Mycobacterium tuberculosis universal stress protein Rv2623 regulates mycobacterial growth and may be required for the... 
ABC TRANSPORTER | PHAGOCYTOSIS | MICROBIOLOGY | FHA DOMAIN | SERINE/THREONINE KINASES | IDENTIFICATION | SER/THR PHOSPHORYLATION | VIROLOGY | EMBR | MANNOSIDE BIOSYNTHESIS | MOLECULAR-BASIS | EXPRESSION | PARASITOLOGY | Phosphorylation | Humans | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Tuberculosis - microbiology | Carrier Proteins - genetics | Two-Hybrid System Techniques | ATP-Binding Cassette Transporters - chemistry | Carrier Proteins - metabolism | ATP-Binding Cassette Transporters - genetics | ATP-Binding Cassette Transporters - metabolism | Protein Binding | Protein Domains | Bacterial Proteins - metabolism | Carrier Proteins - chemistry | Mycobacterium tuberculosis - chemistry | Mycobacterium tuberculosis - metabolism | Mycobacterium tuberculosis - genetics | Mycobacterium tuberculosis - growth & development | Phosphate-Binding Proteins | Physiological aspects | Stress (Physiology) | Research | Mycobacterium tuberculosis | Bacterial proteins | Analysis | Bacilli | Yeast | Oligopeptides | Laboratories | Funding | Physicians | Modules | Virulence | Infections | Biochemistry | Biosynthesis | Proteins | Spectrometry | Immunology | Affinity chromatography | Forkhead protein | Bacteria | Chief executive officers | Immune system | Binding | Alanine | Inositol | Immune response | Threonine | Immunomodulation | Migraine | Biophysics | Biological activity | Exports | Medicine | Tuberculosis | Lipooligosaccharides | Glycolipids | Powder injection molding | Appointments & personnel changes | Aberration | Protein interaction | Universal stress protein | ATP | Transporter
Journal Article
Journal Article
Journal Article
Acta Crystallographica Section F, ISSN 2053-230X, 06/2017, Volume 73, Issue 6, pp. 342 - 346
Phosphate‐binding proteins (PBPs) are key proteins that belong to the bacterial ABC‐type phosphate transporters. PBPs are periplasmic (or membrane‐anchored)... 
Polaromonas JS666 | phosphate‐binding protein | phosphate ABC transporter | molecular specificity | phosphate-binding protein | MOLECULAR REPLACEMENT | SPECIFICITY | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | PSTS | BIOCHEMICAL RESEARCH METHODS | RECEPTOR | DIFFRACTION DATA | CRYSTALLOGRAPHY | FEATURES | BIOPHYSICS | SEQUENCE | Comamonadaceae - chemistry | Bacterial Proteins - chemistry | Phosphates - chemistry | Crystallography, X-Ray | Phosphate-Binding Proteins - genetics | Recombinant Fusion Proteins - metabolism | Periplasm - metabolism | X-Ray Diffraction | Cloning, Molecular | Escherichia coli - metabolism | Phosphate-Binding Proteins - chemistry | Periplasm - chemistry | Comamonadaceae - metabolism | Amino Acid Sequence | Gene Expression | Genetic Vectors - chemistry | Bacterial Proteins - genetics | Crystallization | Phosphate-Binding Proteins - metabolism | Genetic Vectors - metabolism | Recombinant Fusion Proteins - chemistry | Sequence Homology, Amino Acid | Phosphates - metabolism | Sequence Alignment | Hydrogen Bonding | Escherichia coli - genetics | Recombinant Fusion Proteins - genetics | Bacterial Proteins - metabolism | Hydrogen-Ion Concentration | Binding | Residues | Purification | Hydrogen | Protein purification | X-ray diffraction | Selectivity | Phasing | Proteins | Anions | Diffraction | Phosphate | Data collection | Collection | Bacteria | Affinity | Environment | Sulfur | Transporter | BASIC BIOLOGICAL SCIENCES
Journal Article
FEBS Letters, ISSN 0014-5793, 2006, Volume 580, Issue 25, pp. 5885 - 5893
Genetically-encoded fluorescence resonance energy transfer (FRET) sensors for phosphate (P i) (FLIPPi) were engineered by fusing a predicted Synechococcus... 
Fluorescence energy transfer | Phosphate starvation | Biosensor | Synechococcus | fluorescent protein | FLIPPi | fluorescence resonance energy transfer | FRET | fluorescent indicator protein for inorganic phosphate | FLUORESCENT NANOSENSORS | RAT-LIVER | biosensor | BIOCHEMISTRY & MOLECULAR BIOLOGY | RESONANCE ENERGY-TRANSFER | INORGANIC-PHOSPHATE | BINDING PROTEIN | COS-7 CELLS | FAMILY | CELL BIOLOGY | fluorescence energy transfer | TRANSPORT | phosphate starvation | BIOPHYSICS | SURFACE | LIVING CELLS | Sequence Deletion | Bacterial Proteins - chemistry | Cercopithecus aethiops | Phosphate-Binding Proteins - genetics | Green Fluorescent Proteins - genetics | Recombinant Fusion Proteins - metabolism | Synechococcus - genetics | Base Sequence | Phosphate-Binding Proteins - chemistry | Protein Engineering | CHO Cells | Green Fluorescent Proteins - metabolism | Cricetinae | Mutagenesis, Site-Directed | Bacterial Proteins - genetics | Phosphate-Binding Proteins - metabolism | Models, Molecular | Binding Sites - genetics | Recombinant Fusion Proteins - chemistry | Phosphates - metabolism | Animals | DNA, Bacterial - genetics | Recombinant Fusion Proteins - genetics | Bacterial Proteins - metabolism | Biosensing Techniques - methods | Fluorescence Resonance Energy Transfer - methods | Luminescent Proteins - genetics | Protein Conformation | Kinetics | COS Cells | Fluorescent Dyes | Luminescent Proteins - metabolism | Synechococcus - metabolism | Phosphates | Analysis | Detectors | Physiological aspects | Fluorescence | Physicians (General practice) | Methods
Journal Article
Journal Article
FEBS Letters, ISSN 0014-5793, 03/2019, Volume 593, Issue 6, pp. 611 - 621
Improving the performance of the key photosynthetic enzyme Ribulose‐1,5‐bisphosphate carboxylase/oxygenase (Rubisco) by protein engineering is a critical... 
assembly | Rubisco | Rubisco activase | molecular chaperones | protein expression | folding | PROTEIN | RBCX | ACTIVASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CARBOXYLASE/OXYGENASE | IDENTIFICATION | CELL BIOLOGY | BIOPHYSICS | ASSEMBLY CHAPERONE | GENE | BIOGENESIS | ENZYMES | PHOTOSYNTHESIS | Recombinant Fusion Proteins - isolation & purification | Arabidopsis - enzymology | Molecular Chaperones - metabolism | Ribulose-Bisphosphate Carboxylase - genetics | Phosphate-Binding Proteins - genetics | Histidine - metabolism | Recombinant Fusion Proteins - metabolism | Protein Subunits - metabolism | Arabidopsis Proteins - metabolism | Protein Isoforms - metabolism | Photosynthesis - genetics | Protein Subunits - isolation & purification | Cloning, Molecular - methods | Escherichia coli - metabolism | Protein Subunits - genetics | Arabidopsis Proteins - genetics | Gene Expression | Carbon Dioxide - metabolism | Genetic Vectors - chemistry | Protein Structure, Secondary | Group I Chaperonins - metabolism | Ribulose-Bisphosphate Carboxylase - isolation & purification | Oligopeptides - genetics | Molecular Chaperones - genetics | Phosphate-Binding Proteins - metabolism | Genetic Vectors - metabolism | Histidine - genetics | Models, Molecular | Oligopeptides - metabolism | Protein Folding | Arabidopsis - genetics | Ribulose-Bisphosphate Carboxylase - metabolism | Escherichia coli - genetics | Recombinant Fusion Proteins - genetics | Kinetics | Group I Chaperonins - genetics | Protein Isoforms - genetics | Communication
Journal Article
The FEBS Journal, ISSN 1742-464X, 09/2013, Volume 280, Issue 18, pp. 4463 - 4473
Ruminococcus albus has the ability to intracellularly degrade cello‐oligosaccharides primarily via phosphorolysis. In this study, the enzymatic characteristics... 
glycoside hydrolase family 94 | cellodextrin phosphorylase | phosphate binding site | acceptor binding site | substrate specificity | glycoside hydrolase family 94 | CELLOBIOSE PHOSPHORYLASE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | glycoside hydrolase family94 | RUMINAL BACTERIUM | REACTION-MECHANISM | PURIFICATION | CLOSTRIDIUM-THERMOCELLUM | 2-EPIMERASE | Bacterial Proteins - chemistry | Substrate Specificity | Phylogeny | Glucosyltransferases - metabolism | Ruminococcus - chemistry | Thermodynamics | Cellulose - chemistry | Phenylalanine - chemistry | Oligosaccharides - chemistry | Escherichia coli - metabolism | Glucosyltransferases - classification | Cellulose - analogs & derivatives | Glucosyltransferases - genetics | Recombinant Proteins - metabolism | Phenylalanine - metabolism | Bacterial Proteins - genetics | Recombinant Proteins - chemistry | Cellobiose - metabolism | Recombinant Proteins - genetics | Oligosaccharides - metabolism | Dextrins - chemistry | Hydrolysis | Cellobiose - chemistry | Escherichia coli - genetics | Phenylalanine - genetics | Glucosyltransferases - chemistry | Bacterial Proteins - metabolism | Bacterial Proteins - classification | Dextrins - metabolism | Kinetics | Mutation | Ruminococcus - enzymology | Cellulose - metabolism | Phosphates | Cytokinins | Glucose metabolism | Enzymes | Phenylalanine | Analysis | Hydrolases | Chemical properties | Glucose | Dextrose | Glutamine | Bacteria | Biochemistry | Biocatalysts
Journal Article
Journal Article