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PLoS Pathogens, ISSN 1553-7366, 07/2013, Volume 9, Issue 7, p. e1003508
Bacterial populations co-ordinate gene expression collectively through quorum sensing (QS), a cell-to-cell communication mechanism employing diffusible signal... 
ANALYSIS REVEALS | CRYSTALLIZATION | MICROBIOLOGY | QUINOLONE SIGNAL SYNTHESIS | VIRULENCE | MOLECULES | TRANSCRIPTIONAL REGULATOR | VIROLOGY | GENES | LYSR-TYPE REGULATOR | BENM | CELL | PARASITOLOGY | Virulence - drug effects | Transcription Factors - chemistry | Molecular Conformation | Bacterial Proteins - chemistry | Pseudomonas aeruginosa - physiology | Quinolones - pharmacology | Structure-Activity Relationship | Alkylation | Quinolones - chemistry | Pseudomonas aeruginosa - pathogenicity | Anti-Bacterial Agents - chemistry | Drug Design | Protein Interaction Domains and Motifs | Binding Sites | Mutant Proteins - antagonists & inhibitors | Biofilms - drug effects | Recombinant Proteins - metabolism | Bacterial Proteins - antagonists & inhibitors | Peptide Fragments - metabolism | Quorum Sensing - drug effects | Quinolones - metabolism | Recombinant Proteins - chemistry | Anti-Bacterial Agents - metabolism | Mutant Proteins - metabolism | Transcription Factors - antagonists & inhibitors | Pseudomonas aeruginosa - drug effects | Bacterial Proteins - agonists | Transcription Factors - metabolism | Peptide Fragments - chemistry | Signal Transduction - drug effects | Peptide Fragments - agonists | Peptide Fragments - antagonists & inhibitors | Mutant Proteins - chemistry | Bacterial Proteins - metabolism | Ligands | Anti-Bacterial Agents - pharmacology | Transcription Factors - agonists | Gene Expression Regulation, Bacterial | Mutant Proteins - agonists | Pseudomonas aeruginosa | Genetic aspects | Quorum sensing | Research | Bacterial genetics | Gene expression | Health aspects | Microbiology | Population | Bacteria | Antimicrobial agents | Biosynthesis | Nosocomial infections | Bacteriology
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 02/2016, Volume 291, Issue 7, pp. 3385 - 3394
The adhesion G protein-coupled receptors (aGPCRs) are a large yet poorly understood family of seven-transmembrane proteins. A defining characteristic of the... 
MIGRATION | ACTIVATION | COLLAGEN | signal transduction | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRAFFICKING | TETHERED AGONIST | SUBUNITS | arrestin | MYOBLAST FUSION | receptor structure-function | ubiquitylation (ubiquitination) | APOPTOTIC CELLS | G protein-coupled receptor (GPCR) | GPCR | NUCLEAR FACTOR | proteolysis | Angiogenic Proteins - agonists | Angiogenic Proteins - genetics | Arrestins - chemistry | Receptors, G-Protein-Coupled - metabolism | Allosteric Regulation | Humans | NFATC Transcription Factors - agonists | Arrestins - genetics | Receptors, G-Protein-Coupled - agonists | Arrestins - metabolism | Recombinant Fusion Proteins - metabolism | Ubiquitination | Proteolysis | HEK293 Cells | Conserved Sequence | Protein Interaction Domains and Motifs | Transforming Growth Factor alpha - metabolism | Peptide Fragments - genetics | Genes, Reporter | Recombinant Proteins - metabolism | Peptide Fragments - metabolism | Signal Transduction | Transforming Growth Factor alpha - chemistry | NFATC Transcription Factors - metabolism | Models, Molecular | Recombinant Proteins - chemistry | NFATC Transcription Factors - chemistry | Recombinant Fusion Proteins - chemistry | Transforming Growth Factor alpha - genetics | Angiogenic Proteins - chemistry | Point Mutation | Peptide Fragments - chemistry | Peptide Fragments - agonists | beta-Arrestins | Ligands | Protein Conformation | Receptors, G-Protein-Coupled - genetics | Angiogenic Proteins - metabolism | Receptors, G-Protein-Coupled - chemistry | Amino Acid Substitution | NFATC Transcription Factors - genetics
Journal Article
Diabetes, Obesity and Metabolism, ISSN 1462-8902, 08/2014, Volume 16, Issue 8, pp. 711 - 718
Aims: This work explored the effects of irisin on metabolism, gene expression and mitochondrial content in cultured myocytes. Methods: C2C12 myocytes were... 
FNDC5 | | UCP3 | III | domain containing protein 5 | myokine | mitochondrial uncoupling protein 3 | PGC | fibronectin type | peroxisome proliferator‐activated receptor γ coactivator‐1α | Myokine | Fibronectin type III domain containing protein 5 (FNDC5) | Peroxisome proliferator-activated receptor γ coactivator-1α (PGC-1α) | Mitochondrial uncoupling protein 3 (UCP3) | peroxisome proliferator-activated receptor gamma coactivator-1 alpha (PGC-1 alpha) | fibronectin type III domain containing protein 5 (FNDC5) | CELLS | COACTIVATOR | MITOCHONDRIAL BIOGENESIS | TISSUE | NUCLEAR RESPIRATORY FACTORS | OBESITY | NRF-1 | ENDOCRINOLOGY & METABOLISM | PGC-1 | FAT | mitochondrial uncoupling protein 3 (UCP3) | Humans | Mitochondria, Muscle - metabolism | Muscle Fibers, Skeletal - drug effects | Muscle Fibers, Skeletal - metabolism | Glycolysis - drug effects | Nuclear Respiratory Factor 1 - genetics | DNA-Binding Proteins - metabolism | Oxidative Phosphorylation - drug effects | DNA-Binding Proteins - agonists | Nuclear Respiratory Factor 1 - agonists | Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha | High Mobility Group Proteins - agonists | Muscle Proteins - metabolism | Nuclear Respiratory Factor 1 - metabolism | Fibronectins - agonists | Cell Line | Cell Survival - drug effects | Fibronectins - pharmacology | High Mobility Group Proteins - metabolism | Recombinant Proteins - pharmacology | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Fibronectins - metabolism | Gene Expression Regulation - drug effects | Muscle Proteins - genetics | Transcription Factors - metabolism | Muscle Proteins - agonists | Mitochondrial Turnover - drug effects | Animals | Muscle Fibers, Skeletal - cytology | Cell Proliferation - drug effects | Fibronectins - genetics | Mice | Mitochondria, Muscle - drug effects | Kinetics | Transcription Factors - agonists | High Mobility Group Proteins - genetics | Fibronectins | Glucose metabolism | Muscles | Biosynthesis | Chemical properties | Glucose | Gene expression | Dextrose | Protein binding | Medical research | Metabolism | Rodents
Journal Article
Biochemical Pharmacology, ISSN 0006-2952, 09/2016, Volume 116, pp. 63 - 72
Apelin peptide analogues displaying bias towards G protein signalling pathways have beneficial cardiovascular actions compared with the native peptide in... 
In vivo | G protein coupled receptor | Cardiovascular | Biased agonism | Apelin | CHRONIC HEART-FAILURE | CONTRACTILITY | RATS | IDENTIFICATION | GENETIC ALGORITHM | PRESSURE | PEPTIDE APELIN | DISEASE | PHARMACOLOGY & PHARMACY | ORPHAN RECEPTOR APJ | LIGAND | Cricetulus | Receptors, G-Protein-Coupled - metabolism | Amino Acids, Branched-Chain - metabolism | Cardiotonic Agents - metabolism | Humans | Half-Life | Intercellular Signaling Peptides and Proteins - chemistry | Myocardial Contraction - drug effects | Male | Receptors, G-Protein-Coupled - agonists | Benzimidazoles - chemistry | Intercellular Signaling Peptides and Proteins - metabolism | Binding Sites | CHO Cells | Binding, Competitive | Recombinant Proteins - metabolism | Cardiotonic Agents - pharmacokinetics | Benzimidazoles - pharmacokinetics | Models, Molecular | Rats | Recombinant Proteins - chemistry | Cardiotonic Agents - chemistry | Cardiotonic Agents - pharmacology | Random Allocation | Rats, Sprague-Dawley | Amino Acids, Branched-Chain - chemistry | Intercellular Signaling Peptides and Proteins - agonists | Animals | Amino Acids, Branched-Chain - pharmacokinetics | Intercellular Signaling Peptides and Proteins - pharmacology | Apelin Receptors | Benzimidazoles - metabolism | Amino Acids, Branched-Chain - pharmacology | Benzimidazoles - pharmacology | Heart Ventricles - metabolism | Mice | Molecular Docking Simulation | Receptors, G-Protein-Coupled - genetics | Structural Homology, Protein | Receptors, G-Protein-Coupled - chemistry | Heart Ventricles - drug effects | G proteins
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 02/2016, Volume 291, Issue 9, pp. 4523 - 4536
Inhibiting class I histone deacetylases (HDACs) increases energy expenditure, reduces adiposity, and improves insulin sensitivity in obese mice. However, the... 
WHITE FAT | PROTEIN | GENE | BEIGE | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSCRIPTION | EPIGENETIC REGULATION | UPSTREAM ENHANCER | INSULIN SENSITIVITY | EXPRESSION | ADIPOSE-TISSUE | Polycomb Repressive Complex 2 - antagonists & inhibitors | Polycomb Repressive Complex 2 - agonists | Polycomb Repressive Complex 2 - genetics | Adipocytes, Brown - metabolism | Polycomb Repressive Complex 1 - metabolism | Humans | Ion Channels - genetics | Ubiquitin-Protein Ligases - antagonists & inhibitors | Mitochondrial Proteins - genetics | Mitochondrial Proteins - agonists | Adrenergic beta-3 Receptor Agonists - pharmacology | Promoter Regions, Genetic - drug effects | Polycomb Repressive Complex 1 - genetics | Adipocytes, Brown - enzymology | Protein Processing, Post-Translational - drug effects | RNA Interference | Mitochondrial Proteins - metabolism | Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha | Polycomb Repressive Complex 1 - antagonists & inhibitors | Histone Deacetylase 1 - antagonists & inhibitors | Lysine - metabolism | Histone Deacetylase 1 - genetics | Recombinant Proteins - metabolism | Adipocytes, Brown - drug effects | Mitochondrial Proteins - antagonists & inhibitors | Ubiquitin-Protein Ligases - metabolism | Recombinant Proteins - chemistry | Transcription Factors - antagonists & inhibitors | Transcription Factors - genetics | Mice, Inbred Strains | Enhancer of Zeste Homolog 2 Protein | Ion Channels - antagonists & inhibitors | Gene Expression Regulation - drug effects | Polycomb Repressive Complex 1 - agonists | Transcription Factors - metabolism | Acetylation - drug effects | Animals | Ion Channels - metabolism | Methylation - drug effects | Ion Channels - agonists | Histones - metabolism | Thermogenesis - drug effects | Transcription Factors - agonists | Uncoupling Protein 1 | Polycomb Repressive Complex 2 - metabolism | Ubiquitin-Protein Ligases - genetics | Cell Line, Transformed | Histone Deacetylase 1 - metabolism | histone methylation | thermogenesis | brown adipocytes | UCP1 | histone deacetylation | H3K27 | Metabolism | epigenetics | obesity | histone deacetylase 1 (HDAC1) | uncoupling protein
Journal Article
PLoS Pathogens, ISSN 1553-7366, 04/2015, Volume 11, Issue 4, p. e1004794
Monoamines, such as 5-HT and tyramine (TA), paralyze both free-living and parasitic nematodes when applied exogenously and serotonergic agonists have been used... 
BIOACTIVITY | INFECTIONS | INDUCED PARALYSIS | FUNCTIONAL RECONSTITUTION | MICROBIOLOGY | GATED CHLORIDE CHANNEL | HAEMONCHUS-CONTORTUS | VIROLOGY | PROTEIN-COUPLED RECEPTOR | IN-VIVO | RESISTANCE | SEROTONIN | PARASITOLOGY | GTP-Binding Protein alpha Subunits - chemistry | Humans | Receptors, Biogenic Amine - genetics | Caenorhabditis elegans Proteins - metabolism | Motor Activity - drug effects | Serotonin 5-HT1 Receptor Agonists - pharmacology | Drug Discovery - methods | Drosophila Proteins - agonists | Drosophila Proteins - metabolism | Caenorhabditis elegans Proteins - agonists | Behavior, Animal - drug effects | Helminth Proteins - metabolism | Recombinant Proteins - metabolism | Caenorhabditis elegans - metabolism | GTP-Binding Protein alpha Subunits - metabolism | Caenorhabditis elegans - genetics | Chloride Channel Agonists - pharmacology | Nerve Tissue Proteins - agonists | Interneurons - drug effects | Recombinant Proteins - chemistry | GTP-Binding Protein alpha Subunits - genetics | Helminth Proteins - genetics | Recombinant Proteins - genetics | Hypotonic Solutions - toxicity | Animals, Genetically Modified - metabolism | Nerve Tissue Proteins - genetics | Nerve Tissue Proteins - metabolism | Animals | Caenorhabditis elegans - drug effects | Interneurons - metabolism | Animals, Genetically Modified - genetics | Anthelmintics - pharmacology | Receptors, Biogenic Amine - metabolism | Haemonchus | Helminth Proteins - agonists | Drosophila Proteins - genetics | Caenorhabditis elegans Proteins - genetics | Drosophila melanogaster | Receptors, Biogenic Amine - agonists | Proteins | Nematodes | Parasites | Mutation | Permeability | Worms
Journal Article
Neuropharmacology, ISSN 0028-3908, 10/2012, Volume 63, Issue 5, pp. 905 - 915
Mu-opioid and CB1-cannabinoid agonists produce analgesia; however, adverse effects limit use of drugs in both classes. Additive or synergistic effects... 
Analgesia | Morphine | Marijuana | G-protein | Adenylyl cyclase | CB1 receptors | AGONIST MORPHINE | ACTIVATION | PROTEIN-KINASE | CB1 CANNABINOID RECEPTOR | SYNERGISTIC INTERACTIONS | NEUROSCIENCES | INHIBITION | KAPPA | FULL AGONIST | ADENYLYL-CYCLASE | PHARMACOLOGY & PHARMACY | RAT-BRAIN | Pyrazoles - therapeutic use | Receptor, Cannabinoid, CB2 - agonists | Humans | Analgesics, Opioid - pharmacology | Receptors, Opioid, mu - agonists | Piperidines - pharmacology | Cannabinoid Receptor Agonists - therapeutic use | Recombinant Proteins - antagonists & inhibitors | Piperidines - metabolism | Receptors, Opioid, mu - metabolism | Morpholines - metabolism | Analgesics, Non-Narcotic - metabolism | Drug Inverse Agonism | Mice | Analgesics, Opioid - metabolism | Kinetics | Receptor, Cannabinoid, CB1 - antagonists & inhibitors | Analgesics, Opioid - antagonists & inhibitors | Cannabinoid Receptor Agonists - metabolism | Cricetulus | Analgesics, Non-Narcotic - pharmacology | Cannabinoid Receptor Agonists - pharmacology | Receptor, Cannabinoid, CB2 - genetics | Analgesics, Opioid - adverse effects | Narcotic Antagonists - metabolism | Receptor, Cannabinoid, CB1 - agonists | Analgesics, Non-Narcotic - adverse effects | Cannabinoid Receptor Agonists - adverse effects | Morpholines - adverse effects | CHO Cells | Pyrazoles - adverse effects | Pyrazoles - pharmacology | Binding, Competitive | Recombinant Proteins - metabolism | Cricetinae | Morpholines - pharmacology | Narcotic Antagonists - adverse effects | Recombinant Proteins - agonists | Analgesics, Non-Narcotic - therapeutic use | Pyrazoles - metabolism | Mice, Inbred Strains | Receptors, Opioid, mu - antagonists & inhibitors | Receptor, Cannabinoid, CB1 - metabolism | Receptor, Cannabinoid, CB2 - metabolism | Animals | Narcotic Antagonists - therapeutic use | Piperidines - therapeutic use | Narcotic Antagonists - pharmacology | Piperidines - adverse effects | Receptors, Opioid, mu - genetics | Index Medicus | Drugs | Pain perception | Opioid receptors | Cyclic AMP | Opioid receptors (type mu) | Antagonists | Cannabinoid CB1 receptors | Guanine nucleotide-binding protein | Antagonism | Cell activation | Side effects | Inverse agonists | CB1 Receptors | Adenylyl Cyclase
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 6/2010, Volume 107, Issue 24, pp. 11110 - 11115
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 50, pp. 20354 - 20361
In the yeast Saccharomyces cerevisiae, the exposure to mating pheromone activates a prototypic mitogen-activated protein kinase (MAPK) cascade and triggers a... 
differentiation | SPECIFICITY | PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | mitogen-activated protein kinase (MAPK) | PROLIFERATION | SIGNALING DYNAMICS | yeast mating response | imaging | SACCHAROMYCES-CEREVISIAE | cell fate decision | PATHWAY | cell signaling | GROWTH | GENE-EXPRESSION | pheromone | FEEDBACK | single-cell analysis | Cytoskeletal Proteins - genetics | Mating Factor - agonists | Saccharomyces cerevisiae - drug effects | Green Fluorescent Proteins - genetics | Mating Factor - metabolism | Protein Transport - drug effects | Cytoskeletal Proteins - agonists | Recombinant Fusion Proteins - metabolism | Mitogen-Activated Protein Kinases - chemistry | Gene Deletion | Cytoskeletal Proteins - metabolism | Membrane Proteins - metabolism | Green Fluorescent Proteins - chemistry | Single-Cell Analysis | Peptide Fragments - genetics | Recombinant Proteins - metabolism | Green Fluorescent Proteins - metabolism | Peptide Fragments - metabolism | Saccharomyces cerevisiae - physiology | Pheromones - pharmacology | Membrane Proteins - genetics | Recombinant Proteins - chemistry | Cytoskeletal Proteins - chemistry | Recombinant Fusion Proteins - chemistry | Saccharomyces cerevisiae Proteins - genetics | Enzyme Activation - drug effects | Membrane Proteins - agonists | Gene Expression Regulation, Bacterial - drug effects | Peptide Fragments - chemistry | MAP Kinase Signaling System - drug effects | Membrane Proteins - chemistry | Peptide Fragments - agonists | Saccharomyces cerevisiae Proteins - metabolism | Saccharomyces cerevisiae - enzymology | Genes, Reporter - drug effects | Mitogen-Activated Protein Kinases - genetics | Kinetics | Mutation | Saccharomyces cerevisiae Proteins - agonists | Saccharomyces cerevisiae - growth & development | Amino Acid Substitution | Mitogen-Activated Protein Kinases - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Accelerated Communications
Journal Article
Journal of Pharmacology and Experimental Therapeutics, ISSN 0022-3565, 05/2008, Volume 325, Issue 2, pp. 577 - 587
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 1/2004, Volume 101, Issue 1, pp. 396 - 401
Journal Article
FEBS Journal, ISSN 1742-464X, 10/2015, Volume 282, Issue 20, pp. 3959 - 3970
The specific cochaperonin, chloroplast chaperonin (Cpn)20, consisting of two tandem Gro ES ‐like domains, is present abundantly in plant and algal... 
Rubisco | GroEL | chaperonin | folding | Cpn60 | ARABIDOPSIS-THALIANA | PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | CHLOROPLAST | CPN20 | CPN10 | PURIFICATION | BINDING | SUBUNIT | Rhodospirillum rubrum - metabolism | Molecular Weight | Protein Multimerization | Bacterial Proteins - chemistry | Ribulose-Bisphosphate Carboxylase - genetics | Chlamydomonas - metabolism | Recombinant Fusion Proteins - metabolism | Arabidopsis Proteins - metabolism | Group I Chaperonins - agonists | Chaperonin 10 - metabolism | Escherichia coli - metabolism | Algal Proteins - genetics | Chaperonin 10 - agonists | Escherichia coli Proteins - agonists | Rhodospirillum rubrum - enzymology | Chaperonin 60 - metabolism | Recombinant Proteins - metabolism | Chaperonin 60 - chemistry | Ribulose-Bisphosphate Carboxylase - chemistry | Arabidopsis Proteins - agonists | Arabidopsis Proteins - genetics | Chaperonin 60 - agonists | Chaperonin 60 - genetics | Algal Proteins - chemistry | Group I Chaperonins - metabolism | Bacterial Proteins - genetics | Protein Refolding | Algal Proteins - agonists | Models, Molecular | Recombinant Proteins - chemistry | Escherichia coli Proteins - metabolism | Recombinant Fusion Proteins - chemistry | Chloroplasts - metabolism | Arabidopsis - metabolism | Bacterial Proteins - agonists | Ribulose-Bisphosphate Carboxylase - metabolism | Arabidopsis Proteins - chemistry | Group I Chaperonins - chemistry | Chaperonin 10 - genetics | Escherichia coli Proteins - genetics | Bacterial Proteins - metabolism | Chaperonin 10 - chemistry | Escherichia coli Proteins - chemistry | Group I Chaperonins - genetics | Algal Proteins - metabolism | Oligomers | Analysis | Escherichia coli | Chloroplasts | Microbiology | Enzymes
Journal Article