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Nature Chemical Biology, ISSN 1552-4450, 08/2014, Volume 10, Issue 10, pp. 810 - 812
Approximately 25% of cytoplasmic tRNAs in eukaryotic organisms have the wobble uridine (U34) modified at C5 through a process that, according to genetic... 
DOMAIN | PROTEIN | POLYMERASE-II HOLOENZYME | BIOCHEMISTRY & MOLECULAR BIOLOGY | HISTONE ACETYLTRANSFERASE | SACCHAROMYCES-CEREVISIAE | ELONGATOR COMPLEX | EXPRESSION | SAM | Histone Acetyltransferases - chemistry | Archaeal Proteins - chemistry | Histone Acetyltransferases - genetics | Molecular Sequence Data | S-Adenosylmethionine - chemistry | Protein Subunits - metabolism | Nerve Tissue Proteins - chemistry | Histone Acetyltransferases - metabolism | Escherichia coli - metabolism | Conserved Sequence | Free Radicals - metabolism | Archaeal Proteins - genetics | RNA, Transfer - chemistry | Methanocaldococcus - chemistry | Uridine - chemistry | Protein Subunits - genetics | Archaeal Proteins - metabolism | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Amino Acid Sequence | Gene Expression | Biocatalysis | Free Radicals - chemistry | RNA, Transfer - metabolism | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Nerve Tissue Proteins - genetics | Nerve Tissue Proteins - metabolism | Escherichia coli - genetics | Methanocaldococcus - enzymology | Saccharomyces cerevisiae Proteins - metabolism | Uridine - metabolism | Protein Subunits - chemistry | Structural Homology, Protein | S-Adenosylmethionine - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Proteins | Eukaryotes | Biocatalysts | Cytoplasm | Transfer RNA | Index Medicus
Journal Article
Journal of Bacteriology, ISSN 0021-9193, 04/2008, Volume 190, Issue 8, pp. 2987 - 2996
Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
PHOSPHOGLUCOSAMINE MUTASE | GLUCOSAMINE-1-PHOSPHATE ACETYLTRANSFERASE | HYPERTHERMOPHILIC ARCHAEON | N-LINKED GLYCOSYLATION | THERMOSTABLE ENZYME | ESCHERICHIA-COLI | MICROBIOLOGY | ACETYLGLUCOSAMINE 2-EPIMERASE | METHANOCALDOCOCCUS-JANNASCHII | METHANOCOCCUS-MARIPALUDIS | PYROCOCCUS-FURIOSUS | Uridine Triphosphate - metabolism | Archaeal Proteins - isolation & purification | Acetylglucosamine - biosynthesis | Molecular Sequence Data | Glucosamine - metabolism | Methanococcus - genetics | Acetylglucosamine - metabolism | Enzymes - genetics | Cloning, Molecular | Acetylglucosamine - analogs & derivatives | Archaeal Proteins - genetics | Enzymes - metabolism | NAD - metabolism | Uridine Diphosphate N-Acetylglucosamine - metabolism | Archaeal Proteins - metabolism | DNA, Archaeal - genetics | Uridine Diphosphate Sugars - metabolism | Phosphotransferases (Phosphomutases) - genetics | Glucosamine - analogs & derivatives | DNA, Archaeal - chemistry | Enzymes - isolation & purification | Glucose-6-Phosphate - analogs & derivatives | Biosynthetic Pathways | Sequence Analysis, DNA | Glucosephosphates - metabolism | Phosphotransferases (Phosphomutases) - metabolism | Escherichia coli - genetics | Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing) - metabolism | Methanococcus - metabolism | Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing) - genetics | Glucose-6-Phosphate - metabolism | Carbohydrate Epimerases - metabolism | Carbohydrate Dehydrogenases - metabolism | Bacterial proteins | Physiological aspects | Influence | Biosynthesis | Research | Properties | Archaeabacteria | Sugar | Eukaryotes | E coli | Gene expression | Protein synthesis | Index Medicus | Physiology and Metabolism
Journal Article
eLife, ISSN 2050-084X, 05/2016, Volume 5, Issue 2016
The essential process of protein secretion is achieved by the ubiquitous Sec machinery. In prokaryotes, the drive for translocation comes from ATP hydrolysis... 
ATOM FORCE-FIELD | ATP HYDROLYSIS | CONFORMATIONAL-CHANGES | ESCHERICHIA-COLI | BIOLOGY | MEMBRANE-PROTEIN | POLYPEPTIDE TRANSLOCATION | CONDUCTING CHANNEL | NASCENT PEPTIDE | PREPROTEIN TRANSLOCATION | EXPORTED PROTEINS | Bacterial Proteins - chemistry | Substrate Specificity | Adenosine Diphosphate - chemistry | Thermodynamics | Adenosine Triphosphate - metabolism | Escherichia coli - metabolism | Methanocaldococcus - metabolism | Protein Interaction Domains and Motifs | SEC Translocation Channels - chemistry | Binding Sites | Thermotoga maritima - metabolism | SEC Translocation Channels - metabolism | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Gene Expression | Bacterial Proteins - genetics | Adenosine Triphosphatases - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Thermotoga maritima - genetics | Amino Acid Motifs | Protein Transport | SEC Translocation Channels - genetics | Escherichia coli - genetics | Methanocaldococcus - genetics | Protein Binding | Adenosine Triphosphatases - chemistry | Bacterial Proteins - metabolism | Adenosine Triphosphatases - genetics | Adenosine Diphosphate - metabolism | Kinetics | Adenosine Triphosphate - chemistry | Brownian motion | Translocation (Genetics) | Observations | Protein-protein interactions | Hydrolysis | Proteins | Prokaryotes | Secretion | Fluorescence resonance energy transfer | Molecular biology | Protein transport | Binding sites | Index Medicus
Journal Article
Nature Communications, ISSN 2041-1723, 12/2018, Volume 9, Issue 1, pp. 1360 - 12
The proteasome is a sophisticated ATP-dependent molecular machine responsible for protein degradation in all known eukaryotic cells. It remains elusive how... 
20S PROTEASOME | REGULATORY PARTICLE | ANGSTROM RESOLUTION | EUKARYOTIC PROTEASOME | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | MOLECULAR ARCHITECTURE | ELECTRON-MICROSCOPY | METHANOCALDOCOCCUS-JANNASCHII | CRYO-EM STRUCTURE | CONFORMATIONAL STATES | Allosteric Regulation | Humans | Holoenzymes - chemistry | ATPases Associated with Diverse Cellular Activities - chemistry | ATPases Associated with Diverse Cellular Activities - genetics | Nucleotides - chemistry | Arabidopsis Proteins - metabolism | Holoenzymes - metabolism | Proteolysis | ATPases Associated with Diverse Cellular Activities - metabolism | Adenosine Triphosphate - metabolism | Protein Interaction Domains and Motifs | Binding Sites | Amino Acid Sequence | Protein Conformation, alpha-Helical | Arabidopsis Proteins - genetics | Adenosine Triphosphatases - metabolism | Models, Molecular | Proteasome Endopeptidase Complex - chemistry | Saccharomyces cerevisiae Proteins - genetics | Nucleotides - metabolism | Adenosine Triphosphate - analogs & derivatives | Cryoelectron Microscopy | Proteasome Endopeptidase Complex - genetics | Sequence Homology, Amino Acid | Sequence Alignment | Arabidopsis Proteins - chemistry | Protein Conformation, beta-Strand | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Adenosine Triphosphatases - chemistry | Adenosine Triphosphatases - genetics | Holoenzymes - genetics | Kinetics | Proteasome Endopeptidase Complex - metabolism | Adenosine Triphosphate - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Translocation | Allosteric properties | Channel gating | Nucleotides | Gating | ATP | Core particles | Adenosine triphosphatase | Substrates | Adenosine triphosphate | Index Medicus
Journal Article
Journal Article
FEBS Journal, ISSN 1742-464X, 09/2015, Volume 282, Issue 17, pp. 3412 - 3423
The genome of some methanogens contains besides the [Fe]‐hydrogenase (Hmd) a related protein termed Hmd II . We showed by X‐ray and infrared spectroscopic data... 
methanogenic archaea | tetrahydromethanopterin | [Fe]‐hydrogenase | sensor protein | Hmd paralogs | [Fe]-hydrogenase | ACTIVE-SITE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | INFRARED-SPECTROSCOPY | H-2 ACTIVATION | CLUSTER-FREE HYDROGENASE | COMPLETE GENOME SEQUENCE | H-2-FORMING METHYLENETETRAHYDROMETHANOPTERIN DEHYDROGENASE | TRANSFER-RNA SYNTHETASE | ACYL-IRON LIGATION | Pterins - metabolism | Hydrogenase - genetics | Pyridines - chemistry | Archaeal Proteins - chemistry | Iron-Sulfur Proteins - genetics | Crystallography, X-Ray | Holoenzymes - chemistry | Hydrogenase - chemistry | Iron-Sulfur Proteins - chemistry | Coenzymes - metabolism | Hydrogenase - metabolism | Holoenzymes - metabolism | Spectrophotometry, Infrared | Apoenzymes - metabolism | Escherichia coli - metabolism | Archaeal Proteins - genetics | Protein Biosynthesis - genetics | Protein Interaction Domains and Motifs | Pterins - chemistry | Coenzymes - chemistry | Binding Sites | Methanocaldococcus - chemistry | Archaeal Proteins - metabolism | Recombinant Proteins - metabolism | Gene Expression | Protein Structure, Secondary | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Protein Folding | Pyridines - metabolism | Escherichia coli - genetics | Apoenzymes - genetics | Methanocaldococcus - enzymology | Apoenzymes - chemistry | Protein Binding | Holoenzymes - genetics | Iron-Sulfur Proteins - metabolism | Kinetics | Physiological aspects | Protein biosynthesis | Sensors | Aminoacyl-tRNA synthetases | Analysis | Transfer RNA | Enzymes | Biophysics | Protein synthesis | Index Medicus
Journal Article
Journal of Biomolecular Structure and Dynamics, ISSN 0739-1102, 06/2017, Volume 35, Issue 8, pp. 1615 - 1628
The Sm and Sm-like proteins are widely distributed among bacteria, archaea and eukarya. They participate in many processes related to RNA-processing and... 
Lsm proteins | crystal structure | Hfq | translation regulation | RNA-protein interactions | archaea | RNA–protein interactions | COMPLEX | LIGAND-BINDING | RECOGNITION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI HFQ | BIOPHYSICS | MESSENGER-RNA | SURFACE-PLASMON RESONANCE | SM-LIKE PROTEIN | SOLUBLE-RNA | RNA-Binding Proteins - genetics | RNA, Archaeal - chemistry | Archaeal Proteins - chemistry | Crystallography, X-Ray | Poly A - chemistry | RNA, Messenger - metabolism | Host Factor 1 Protein - metabolism | Cloning, Molecular | Escherichia coli - metabolism | Archaeal Proteins - genetics | Methanocaldococcus - metabolism | Protein Interaction Domains and Motifs | RNA, Archaeal - genetics | Binding Sites | Host Factor 1 Protein - genetics | Methanocaldococcus - chemistry | Archaeal Proteins - metabolism | Recombinant Proteins - metabolism | Amino Acid Sequence | Protein Conformation, alpha-Helical | Gene Expression | Genetic Vectors - chemistry | RNA, Messenger - genetics | RNA-Binding Proteins - chemistry | Genetic Vectors - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Sequence Homology, Amino Acid | Poly A - metabolism | Sequence Alignment | Protein Conformation, beta-Strand | Escherichia coli - genetics | RNA, Archaeal - metabolism | Protein Binding | RNA, Messenger - chemistry | Kinetics | RNA-Binding Proteins - metabolism | Host Factor 1 Protein - chemistry | Index Medicus
Journal Article
Scientific Reports, ISSN 2045-2322, 12/2016, Volume 6, Issue 1, pp. 38399 - 38399
The conserved SecYEG protein-conducting channel and the accessory proteins SecDF-YajC and YidC constitute the bacterial holo-translocon (HTL), capable of... 
PERIPLASMIC DOMAIN | COMPLEX | CHANNEL | PARTICLE ELECTRON CRYOMICROSCOPY | ESCHERICHIA-COLI YIDC | SECD | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | EM STRUCTURE DETERMINATION | COMPONENT | MICROSCOPY | Substrate Specificity | Thermus thermophilus - metabolism | Thermus thermophilus - genetics | Membrane Transport Proteins - genetics | Cloning, Molecular | Escherichia coli - metabolism | Membrane Transport Proteins - metabolism | Methanocaldococcus - metabolism | Protein Interaction Domains and Motifs | SEC Translocation Channels - chemistry | Binding Sites | Methanocaldococcus - chemistry | SEC Translocation Channels - metabolism | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Gene Expression | Thermus thermophilus - chemistry | Genetic Vectors - chemistry | Genetic Vectors - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Scattering, Small Angle | Escherichia coli Proteins - metabolism | Recombinant Proteins - genetics | Escherichia coli - chemistry | Membrane Transport Proteins - chemistry | Protein Transport | Cryoelectron Microscopy | SEC Translocation Channels - genetics | Protein Conformation, beta-Strand | Escherichia coli - genetics | Methanocaldococcus - genetics | Escherichia coli Proteins - genetics | Protein Binding | Structural Homology, Protein | Neutron Diffraction | Escherichia coli Proteins - chemistry | Proteins | Neutron scattering | Secretion | Proteolysis | Lipids | Electron microscopy | Membrane proteins | Index Medicus | Life Sciences | Biomolecules | Biochemistry, Molecular Biology
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Journal Article
Journal Article