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Nature, ISSN 0028-0836, 2014, Volume 510, Issue 7503, pp. 172 - 175
Previous studies have established that the folding, structure and function of membrane proteins are influenced by their lipid environments(1-7) and that lipids... 
MYCOBACTERIUM-TUBERCULOSIS | ATOM FORCE-FIELD | MOLECULAR-DYNAMICS | MULTIDISCIPLINARY SCIENCES | COMPLEXES | PURIFICATION | ION-CHANNEL | MOBILITY-MASS SPECTROMETRY | MODEL | MSCL | WATER | Apoproteins - chemistry | Cardiolipins - pharmacology | Protein Unfolding - drug effects | Protein Conformation - drug effects | Aquaporins - chemistry | Bacterial Proteins - chemistry | Substrate Specificity | Crystallography, X-Ray | Membrane Lipids - chemistry | Cation Transport Proteins - metabolism | Protein Folding - drug effects | Mass Spectrometry | Mycobacterium tuberculosis - chemistry | Membrane Proteins - metabolism | Ion Channels - chemistry | Phosphatidylglycerols - metabolism | Apoproteins - metabolism | Ammonia - metabolism | Models, Molecular | Aquaporins - metabolism | Escherichia coli Proteins - metabolism | Cardiolipins - metabolism | Escherichia coli - chemistry | Cardiolipins - chemistry | Phosphatidylglycerols - chemistry | Ion Channels - metabolism | Membrane Proteins - chemistry | Protein Stability - drug effects | Membrane Lipids - metabolism | Phosphatidylglycerols - pharmacology | Bacterial Proteins - metabolism | Membrane Lipids - pharmacology | Lipid Bilayers - chemistry | Cation Transport Proteins - chemistry | Escherichia coli Proteins - chemistry | Biological research | Physiological aspects | Lipids | Cooperative binding (Biochemistry) | Research | Structure | Molecular biology | Membrane proteins | Biology, Experimental | Proteins | Studies | Membranes | E coli | Binding sites | Crystal structure | Index Medicus
Journal Article
FEBS Letters, ISSN 0014-5793, 12/2016, Volume 590, Issue 24, pp. 4531 - 4540
Iron–sulfur (Fe–S) clusters are ubiquitously conserved and play essential cellular roles. The mechanism of Fe–S cluster biogenesis involves multiple proteins... 
[2Fe‐2S] cluster transfer | iron–sulfur cluster | Nfu | glutaredoxin | IscU | [2Fe-2S] cluster transfer | HUMAN NFU | iron-sulfur cluster | BIOCHEMISTRY & MOLECULAR BIOLOGY | PROTEIN BIOGENESIS | MATURATION | SACCHAROMYCES-CEREVISIAE | 4FE-4S CLUSTER | CELL BIOLOGY | MONOTHIOL GLUTAREDOXINS | BIOPHYSICS | BIOSYNTHESIS | 2FE-2S CLUSTER | SCAFFOLD PROTEIN | Apoproteins - chemistry | Humans | Bacterial Proteins - chemistry | Iron-Sulfur Proteins - genetics | Iron-Sulfur Proteins - chemistry | Oxidoreductases - chemistry | Saccharomyces cerevisiae - metabolism | Biological Transport | Escherichia coli - metabolism | Carrier Proteins - chemistry | Thermotoga maritima - chemistry | Thermotoga maritima - metabolism | Apoproteins - metabolism | Sulfur - chemistry | Recombinant Proteins - metabolism | Sulfur - metabolism | Gene Expression | Oxidoreductases - metabolism | Oxidoreductases - genetics | Iron - chemistry | Bacterial Proteins - genetics | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Iron - metabolism | Saccharomyces cerevisiae - chemistry | Cytosol - chemistry | Carrier Proteins - genetics | Carrier Proteins - metabolism | Escherichia coli - genetics | Saccharomyces cerevisiae Proteins - metabolism | Apoproteins - genetics | Bacterial Proteins - metabolism | Cytosol - metabolism | Iron-Sulfur Proteins - metabolism | Kinetics | Saccharomyces cerevisiae Proteins - chemistry | Index Medicus
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 05/2012, Volume 287, Issue 19, pp. 15544 - 15556
This study tested whether nonredox metalloenzymes are commonly charged with iron in vivo and are primary targets of oxidative stress because of it. Indeed,... 
OXIDATIVE STRESS | L-THREONINE DEHYDROGENASE | BACILLUS-SUBTILIS | GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | CYTOSINE DEAMINASE | PROTEIN-TYROSINE PHOSPHATASES | CATALYTIC MECHANISM | TRANSCRIPTION FACTOR | Apoproteins - chemistry | Oxidants - pharmacology | Models, Chemical | Alcohol Oxidoreductases - genetics | Cytosine Deaminase - metabolism | Biocatalysis - drug effects | Cation Transport Proteins - metabolism | Cytosine Deaminase - chemistry | Escherichia coli - metabolism | Oxidation-Reduction - drug effects | Cation Transport Proteins - genetics | Cysteine - metabolism | Apoproteins - metabolism | Bacterial Outer Membrane Proteins - genetics | Cytosine Deaminase - genetics | Amidohydrolases - metabolism | Catalytic Domain | Escherichia coli - enzymology | Amidohydrolases - genetics | Iron - chemistry | Hydrogen Peroxide - pharmacology | Bacterial Outer Membrane Proteins - chemistry | Alcohol Oxidoreductases - metabolism | Escherichia coli Proteins - metabolism | Cysteine - chemistry | Manganese - chemistry | Amidohydrolases - chemistry | Iron - metabolism | Blotting, Western | Manganese - metabolism | Bacterial Outer Membrane Proteins - metabolism | Alcohol Oxidoreductases - chemistry | Escherichia coli - genetics | Escherichia coli Proteins - genetics | Kinetics | Mutation | Cation Transport Proteins - chemistry | Escherichia coli Proteins - chemistry | Index Medicus | Oxidative stress | Fenton Reaction | Microbiology | Iron | Metalloenzymes | Peptide Deformylase | Manganese | Sulfhydryl | Sulfhydryl Oxidation
Journal Article
Journal Article
Journal of Proteome Research, ISSN 1535-3893, 06/2008, Volume 7, Issue 6, pp. 2234 - 2245
We considered, on a global scale, the relationship between the predicted fraction of protein disorder and the RNA and protein expression in Escherichia coli.... 
Protein abundance | Disordered proteins | PONDR | CAI | Gene expression | Microarrays | disordered proteins | MOLECULAR RECOGNITION FEATURES | BIOCHEMICAL RESEARCH METHODS | CODON ADAPTATION INDEX | ELONGATION-FACTOR NUSA | ACETYL-COA CARBOXYLASE | microarrays | NATIVELY UNFOLDED PROTEINS | SUGAR PHOSPHOTRANSFERASE SYSTEM | GRAM-NEGATIVE BACTERIA | protein abundance | DEHYDROGENASE MULTIENZYME COMPLEX | N-TERMINAL DOMAIN | CARBOXYL CARRIER PROTEIN | gene expression | Peptidoglycan - metabolism | Peptide Elongation Factors - metabolism | Molecular Chaperones - metabolism | Transcription Factors - chemistry | Oligonucleotide Array Sequence Analysis | Escherichia coli - drug effects | Bacterial Proteins - chemistry | Dihydrolipoyllysine-Residue Acetyltransferase - metabolism | Gene Expression Profiling | Transcriptional Elongation Factors | Glycine Decarboxylase Complex H-Protein - genetics | Dihydrolipoyllysine-Residue Acetyltransferase - genetics | Phosphoenolpyruvate Sugar Phosphotransferase System - genetics | Fatty Acid Synthase, Type II | Bacterial Proton-Translocating ATPases - chemistry | Bacterial Proton-Translocating ATPases - metabolism | Molecular Chaperones - genetics | DNA-Directed RNA Polymerases - genetics | Peptidoglycan - genetics | DNA-Binding Proteins - chemistry | Acyl Carrier Protein - chemistry | Peptide Elongation Factors - chemistry | Bacterial Outer Membrane Proteins - metabolism | Escherichia coli - genetics | Chaperonin 10 - genetics | Prokaryotic Initiation Factor-1 - metabolism | Chaperonin 10 - chemistry | Protein Conformation | Dihydrolipoyllysine-Residue Acetyltransferase - chemistry | DNA-Directed RNA Polymerases - metabolism | Escherichia coli Proteins - chemistry | Gene Expression Regulation, Bacterial | Acetyl-CoA Carboxylase - metabolism | Acetyl-CoA Carboxylase - chemistry | Apoproteins - chemistry | Ribosomal Proteins - chemistry | Lipoproteins - genetics | Peptidoglycan - chemistry | Glycine Decarboxylase Complex H-Protein - chemistry | Molecular Chaperones - chemistry | Acyltransferases - metabolism | Acyltransferases - genetics | Acetyl-CoA Carboxylase - genetics | Ribosomal Proteins - metabolism | DNA-Binding Proteins - metabolism | Chaperonin 10 - metabolism | Escherichia coli - metabolism | Lipoproteins - metabolism | Prokaryotic Initiation Factor-1 - chemistry | Carrier Proteins - chemistry | DNA-Directed RNA Polymerases - chemistry | Glycine Decarboxylase Complex H-Protein - metabolism | Peptide Elongation Factors - genetics | Apoproteins - metabolism | Bacterial Outer Membrane Proteins - genetics | Phosphoenolpyruvate Sugar Phosphotransferase System - chemistry | Ribosomal Proteins - genetics | Acyl Carrier Protein - metabolism | Bacterial Proton-Translocating ATPases - genetics | Bacterial Proteins - genetics | Bacterial Outer Membrane Proteins - chemistry | Escherichia coli Proteins - metabolism | Lipoproteins - chemistry | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Prokaryotic Initiation Factor-1 - genetics | Transcription Factors - metabolism | Carrier Proteins - genetics | Carrier Proteins - metabolism | Acyl Carrier Protein - genetics | Culture Media - pharmacology | Phosphoenolpyruvate Sugar Phosphotransferase System - metabolism | Apoproteins - genetics | Escherichia coli Proteins - genetics | Bacterial Proteins - metabolism | Acyltransferases - chemistry | Index Medicus
Journal Article
Biochemistry, ISSN 0006-2960, 03/2017, Volume 56, Issue 12, pp. 1716 - 1725
The stereochemical course of monoterpene synthase reactions is thought to be determined early in the reaction sequence by selective binding of distinct... 
NERYL PYROPHOSPHATE | ENZYMATIC CONVERSION | BIOSYNTHESIS | DIPHOSPHATE | BIOCHEMISTRY & MOLECULAR BIOLOGY | MONOTERPENE CYCLASES | TERPENOID CYCLASE | 2-METHYLISOBORNEOL SYNTHASE | GLANDULAR TRICHOMES | MENTHA-X-PIPERITA | PRENYL-TRANSFER-REACTION | Apoproteins - chemistry | Intramolecular Lyases - antagonists & inhibitors | Organophosphates - metabolism | Polyisoprenyl Phosphates - chemistry | Intramolecular Lyases - metabolism | Stereoisomerism | Cyclohexenes - chemistry | Crystallography, X-Ray | Citrus sinensis - chemistry | Recombinant Fusion Proteins - metabolism | Citrus sinensis - enzymology | Terpenes - chemistry | Terpenes - metabolism | Plant Proteins - chemistry | Enzyme Inhibitors - chemistry | Plant Proteins - antagonists & inhibitors | Cloning, Molecular | Escherichia coli - metabolism | Protein Domains | Plant Proteins - metabolism | Diterpenes - metabolism | Apoproteins - metabolism | Diterpenes - chemistry | Apoproteins - antagonists & inhibitors | Catalytic Domain | Gene Expression | Enzyme Inhibitors - metabolism | Protein Structure, Secondary | Models, Molecular | Enzyme Assays | Recombinant Fusion Proteins - chemistry | Polyisoprenyl Phosphates - metabolism | Plant Proteins - genetics | Cyclohexenes - metabolism | Intramolecular Lyases - genetics | Escherichia coli - genetics | Apoproteins - genetics | Recombinant Fusion Proteins - genetics | Ligands | Organophosphates - chemistry | Kinetics | Intramolecular Lyases - chemistry | Phosphates | Research | Chemical properties | Orange | Carbenes | Index Medicus
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 33, pp. 13879 - 13889
Viperin (RSAD2) is an interferon-stimulated antiviral protein that belongs to the radical S-adenosylmethionine (SAM) enzyme family. Viperin's iron-sulfur... 
REPLICATION | HEPATITIS-C VIRUS | BIOGENESIS | DNA METABOLISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | WEST NILE VIRUS | MMS19 | IDENTIFICATION | MATURATION | AMPHIPATHIC ALPHA-HELIX | INHIBIT | Apoproteins - chemistry | Immunoprecipitation | Transcription Factors - chemistry | Humans | Iron-Sulfur Proteins - genetics | Iron-Sulfur Proteins - chemistry | Recombinant Fusion Proteins - metabolism | Metallochaperones - chemistry | RNA Interference | HEK293 Cells | Carrier Proteins - chemistry | Protein Interaction Domains and Motifs | Metallochaperones - antagonists & inhibitors | Nuclear Proteins - genetics | Peptide Fragments - genetics | Apoproteins - metabolism | Recombinant Proteins - metabolism | Peptide Fragments - metabolism | Iron - chemistry | Carrier Proteins - antagonists & inhibitors | Recombinant Proteins - chemistry | Nuclear Proteins - metabolism | Transcription Factors - antagonists & inhibitors | Recombinant Fusion Proteins - chemistry | Transcription Factors - genetics | Nuclear Proteins - chemistry | Iron - metabolism | Metallochaperones - genetics | Proteins - genetics | Transcription Factors - metabolism | Carrier Proteins - genetics | Iron Radioisotopes | Peptide Fragments - chemistry | Carrier Proteins - metabolism | Proteins - metabolism | Models, Biological | Nuclear Proteins - antagonists & inhibitors | Apoproteins - genetics | Iron-Sulfur Proteins - metabolism | Metallochaperones - metabolism | Mutation | Proteins - chemistry | Amino Acid Substitution | Index Medicus | iron–sulfur protein | molecular cell biology | metal biology | iron | sulfur | Cia targeting complex | viperin | biogenesis | interferon | Cell Biology | Basic Medicine | Medical and Health Sciences | Microbiology in the medical area | Mikrobiologi inom det medicinska området | Medicin och hälsovetenskap | Medicinska och farmaceutiska grundvetenskaper
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 08/2006, Volume 281, Issue 33, pp. 23567 - 23578
Journal Article
Biochemistry, ISSN 0006-2960, 10/2013, Volume 52, Issue 43, pp. 7628 - 7640
Succinate dehydrogenase (SDH) is an important respiratory enzyme that plays a critical role in the generation of energy in the majority of eukaryotes,... 
FLAVIN | COVALENT ATTACHMENT | MUTAGENESIS | CIRCULAR-DICHROISM | PROTEIN | COMPLEX-II | GENE | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | FLAVOPROTEIN | NMR STRUCTURE | Apoproteins - chemistry | Flavin-Adenine Dinucleotide - chemistry | Flavoproteins - chemistry | Transcription Factors - chemistry | Bacterial Proteins - chemistry | Holoenzymes - chemistry | Isoenzymes - chemistry | Succinate Dehydrogenase - chemistry | Protein Subunits - metabolism | Flavin-Adenine Dinucleotide - metabolism | Holoenzymes - metabolism | Isoenzymes - metabolism | Escherichia coli - metabolism | Conserved Sequence | Protein Stability | Peptide Fragments - genetics | Serratia - enzymology | Apoproteins - metabolism | Protein Subunits - genetics | Recombinant Proteins - metabolism | Peptide Fragments - metabolism | Escherichia coli - enzymology | Flavoproteins - metabolism | Mutagenesis, Site-Directed | Flavoproteins - genetics | Isoenzymes - genetics | Bacterial Proteins - genetics | Models, Molecular | Recombinant Proteins - chemistry | Escherichia coli Proteins - metabolism | Mutant Proteins - metabolism | Recombinant Proteins - genetics | Transcription Factors - genetics | Protein Folding | Amino Acid Motifs | Transcription Factors - metabolism | Peptide Fragments - chemistry | Succinate Dehydrogenase - genetics | Mutant Proteins - chemistry | Serratia - metabolism | Apoproteins - genetics | Escherichia coli Proteins - genetics | Bacterial Proteins - metabolism | Succinate Dehydrogenase - metabolism | Holoenzymes - genetics | Protein Subunits - chemistry | Escherichia coli Proteins - chemistry | Bacteria | Succinate dehydrogenase complex | Chemical properties | Research | Index Medicus
Journal Article
Journal of Mathematical Biology, ISSN 0303-6812, 8/2009, Volume 59, Issue 2, pp. 193 - 231
Journal Article
Journal Article