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Journal Article
Nature, ISSN 0028-0836, 05/2016, Volume 534, Issue 7605, pp. 133 - 137
Ribosome biogenesis is a highly complex process in eukaryotes, involving temporally and spatially regulated ribosomal protein (r-protein... 
REFINEMENT | COMPLEX | RNA | BIOGENESIS | INITIATION | MULTIDISCIPLINARY SCIENCES | RESOLUTION | MATURATION | IDENTIFICATION | ASSOCIATION | SUBUNIT | RNA, Fungal - ultrastructure | GTP Phosphohydrolases - ultrastructure | Saccharomyces cerevisiae - ultrastructure | DNA, Ribosomal Spacer - metabolism | RNA, Ribosomal - genetics | GTP Phosphohydrolases - chemistry | Saccharomyces cerevisiae - metabolism | Cell Nucleus - metabolism | Ribosome Subunits, Large, Eukaryotic - metabolism | DNA, Ribosomal Spacer - genetics | Base Sequence | DNA, Ribosomal Spacer - ultrastructure | Ribosome Subunits, Large, Eukaryotic - chemistry | Models, Molecular | Ribonucleoproteins - metabolism | Nuclear Proteins - chemistry | Saccharomyces cerevisiae - chemistry | RNA, Ribosomal - ultrastructure | Saccharomyces cerevisiae - cytology | Ribosomal Proteins - isolation & purification | GTP Phosphohydrolases - metabolism | Saccharomyces cerevisiae Proteins - metabolism | GTP-Binding Proteins - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Ribosomal Proteins - chemistry | Ribosome Subunits, Large, Eukaryotic - ultrastructure | Nuclear Proteins - ultrastructure | Molecular Sequence Data | Cytoplasm - metabolism | Ribosomal Proteins - metabolism | Ribosomal Proteins - ultrastructure | Saccharomyces cerevisiae Proteins - isolation & purification | RNA, Fungal - genetics | Active Transport, Cell Nucleus | Ribonucleoproteins - chemistry | Saccharomyces cerevisiae Proteins - ultrastructure | Catalytic Domain | GTP-Binding Proteins - chemistry | RNA, Ribosomal - metabolism | Nuclear Proteins - metabolism | GTP-Binding Proteins - ultrastructure | DNA, Ribosomal Spacer - chemistry | Cell Nucleus - ultrastructure | Rotation | RNA, Fungal - metabolism | Cryoelectron Microscopy | Protein Binding | Cell Nucleus - chemistry | Ribonucleoproteins - ultrastructure | Nucleolus organizer region | Protein research | Research | Ribosomes | Protein binding | Genetic research | Proteins | G proteins | Ribosomal RNA | Adenosine triphosphatase | Protein biosynthesis | Cell research | Polypeptides | Molecular structure | Ribonucleic acid--RNA
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 | CARBOXY-TERMINAL DOMAINS | INTRINSIC DISORDER | disordered proteins | BACTERIAL PHOSPHOTRANSFERASE SYSTEM | MOLECULAR RECOGNITION FEATURES | BIOCHEMICAL RESEARCH METHODS | CODON ADAPTATION INDEX | ACETYL-COA CARBOXYLASE | microarrays | ACYL CARRIER PROTEIN | NATIVELY UNFOLDED PROTEINS | protein abundance | DEHYDROGENASE MULTIENZYME COMPLEX | gene expression | RNA-POLYMERASE | 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
Journal Article
Journal of Proteome Research, ISSN 1535-3893, 04/2006, Volume 5, Issue 4, pp. 888 - 898
Regions of conserved disorder prediction (CDP) were found in protein domains from all available InterPro member databases, although with varying frequency... 
Intrinsic disorder | PONDR | Protein structure-function | Disorder prediction | UNSTRUCTURED PROTEINS | protein structure-function | CRYSTAL-STRUCTURE | SHIKIMATE KINASE | BIOCHEMICAL RESEARCH METHODS | disorder prediction | NATIVELY UNFOLDED PROTEINS | PRION PROTEIN | LARGE RIBOSOMAL-SUBUNIT | ENTEROPATHOGENIC ESCHERICHIA-COLI | ADHESION MOLECULE CD2 | intrinsic disorder | SEQUENCE COMPLEXITY | RATE HETEROGENEITY | Ribosomal Proteins - chemistry | RNA-Binding Proteins - genetics | Archaeal Proteins - chemistry | Bacterial Proteins - chemistry | Molecular Sequence Data | Structure-Activity Relationship | Viral Proteins - metabolism | Ribosomal Proteins - metabolism | DNA-Binding Proteins - metabolism | Databases, Protein | Conserved Sequence | Archaeal Proteins - genetics | Insect Proteins - metabolism | Archaeal Proteins - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Ribosomal Proteins - genetics | Viral Proteins - chemistry | RNA-Binding Proteins - chemistry | Bacterial Proteins - genetics | Insect Proteins - genetics | Viral Proteins - genetics | Plants | DNA-Binding Proteins - genetics | DNA-Binding Proteins - chemistry | Proteins - genetics | Sequence Homology, Amino Acid | Animals | Proteins - metabolism | Insect Proteins - chemistry | Bacterial Proteins - metabolism | Kinetics | Proteins - chemistry | RNA-Binding Proteins - metabolism | Evolution, Molecular
Journal Article
Nature chemical biology, ISSN 1552-4469, 2014, Volume 10, Issue 12, pp. 1066 - 1072
Chemical probes that form a covalent bond with a protein target often show enhanced selectivity, potency and utility for biological studies... 
DESIGN | PLACEBO | LIGANDS | BIOCHEMISTRY & MOLECULAR BIOLOGY | REACTIVITY | OPTIMIZATION | GENERATION | INHIBITORS | COORDINATE | CYSTEINES | PREDICTION | Small Molecule Libraries - pharmacology | Humans | Bacterial Proteins - chemistry | Molecular Probes - pharmacology | Janus Kinase 3 - antagonists & inhibitors | Protein Kinase Inhibitors - chemistry | beta-Lactamases - genetics | Janus Kinase 3 - chemistry | Ribosomal Protein S6 Kinases, 90-kDa - antagonists & inhibitors | Cysteine - metabolism | Bacterial Proteins - antagonists & inhibitors | Bacterial Proteins - genetics | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Cysteine - chemistry | beta-Lactamase Inhibitors - pharmacology | Ribosomal Protein S6 Kinases, 90-kDa - chemistry | Serine - chemistry | Drug Discovery | Serine - metabolism | Gram-Negative Bacteria - enzymology | Gram-Negative Bacteria - drug effects | Small Molecule Libraries - chemistry | beta-Lactamases - chemistry | Molecular Probes - chemistry | Animals | Ribosomal Protein S6 Kinases, 90-kDa - genetics | Gram-Negative Bacteria - growth & development | Janus Kinase 3 - genetics | Hydrophobic and Hydrophilic Interactions | Protein Binding | Ligands | Molecular Docking Simulation | Protein Kinase Inhibitors - pharmacology | COS Cells | beta-Lactamase Inhibitors - chemistry | Proteins | Chemical bonds | Biochemistry | Crystal structure | Life Sciences | boronic acid | covalent virtual screening | JAK3 kinase | covalent fragments | covalent inhibition | beta-lactamase | RSK2 kinase | cyanoacrylamide | reversible covalent | covalent electrophile | MSK1 kinase
Journal Article
Nature (London), ISSN 1476-4687, 2013, Volume 497, Issue 7448, pp. 217 - 223
The mammalian target of rapamycin (mTOR), a phosphoinositide 3-kinase-related protein kinase, controls cell growth in response to nutrients and growth factors and is frequently deregulated in cancer... 
MAMMALIAN TARGET | RAPAMYCIN | RAPTOR | BINDING PARTNER | RAG GTPASES | RHEB | PATHWAY | TOR | MULTIDISCIPLINARY SCIENCES | CELL-GROWTH | P70 S6 KINASE | Adaptor Proteins, Signal Transducing - chemistry | Catalytic Domain - drug effects | TOR Serine-Threonine Kinases - metabolism | Pyridines - chemistry | Furans - pharmacology | Humans | Crystallography, X-Ray | Structure-Activity Relationship | Pyrimidines - chemistry | TOR Serine-Threonine Kinases - antagonists & inhibitors | Indoles - metabolism | Furans - chemistry | Adenosine Triphosphate - metabolism | Indoles - pharmacology | Tacrolimus Binding Protein 1A - pharmacology | Naphthyridines - chemistry | Ribosomal Protein S6 Kinases, 70-kDa - metabolism | Purines - metabolism | Purines - pharmacology | MTOR Associated Protein, LST8 Homolog | Tacrolimus Binding Protein 1A - chemistry | Models, Molecular | Magnesium - metabolism | Pyrimidines - pharmacology | Sirolimus - metabolism | Sirolimus - pharmacology | Magnesium - chemistry | Purines - chemistry | TOR Serine-Threonine Kinases - chemistry | Tacrolimus Binding Protein 1A - metabolism | Pyridines - pharmacology | Sirolimus - chemistry | Adaptor Proteins, Signal Transducing - metabolism | Adenosine Triphosphate - chemistry | Indoles - chemistry | Naphthyridines - pharmacology | Naphthyridines - metabolism | Protein Structure, Tertiary - drug effects | Proteins | Enzymes | Kinases | Crystal structure
Journal Article
Molecular and Cellular Biology, ISSN 0270-7306, 10/2007, Volume 27, Issue 19, pp. 6581 - 6592
Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
YEAST | GENE | ATPASE | NUCLEAR EXPORT | GLOBAL ANALYSIS | REQUIRES | MATURATION | RIBOSOMAL-SUBUNIT BIOGENESIS | SACCHAROMYCES-CEREVISIAE | PRE-RIBOSOME | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL BIOLOGY | Ribosomes - metabolism | Cytoplasm - metabolism | Phosphoproteins - metabolism | GTP-Binding Proteins - genetics | Recombinant Fusion Proteins - metabolism | Ribosome Subunits, Large, Eukaryotic - metabolism | Intermediate Filament Proteins - genetics | Nuclear Proteins - genetics | Ribosome Subunits, Large, Eukaryotic - genetics | Protein Precursors - genetics | Ribosomes - chemistry | Adenosine Triphosphatases - metabolism | Nuclear Proteins - metabolism | Phosphoproteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Protein Precursors - metabolism | Peptide Initiation Factors - metabolism | Carrier Proteins - genetics | Peptide Initiation Factors - genetics | Carrier Proteins - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Recombinant Fusion Proteins - genetics | Saccharomyces cerevisiae - enzymology | Adenosine Triphosphatases - genetics | Biological Transport - physiology | Intermediate Filament Proteins - metabolism | GTP-Binding Proteins - metabolism | Ribosomal Proteins | Quantitative Methods | Peptide Initiation Factors | Biochemistry, Molecular Biology | Ribosomes | Cellular Biology | Recombinant Fusion Proteins | Nuclear Proteins | Life Sciences | Biological Transport | Adenosine Triphosphatases | Phosphoproteins | Protein Precursors | Saccharomyces cerevisiae Proteins | Ribosome Subunits, Large, Eukaryotic | Genetics | GTP-Binding Proteins | Subcellular Processes | Molecular biology | Saccharomyces cerevisiae | Intermediate Filament Proteins | Cytoplasm | Carrier Proteins
Journal Article
Scientific reports, ISSN 2045-2322, 2018, Volume 8, Issue 1, pp. 6805 - 11
The content of intrinsically disordered protein (IDP) is related to organism complexity, evolution, and regulation... 
UNSTRUCTURED PROTEINS | CONDITIONAL DISORDER | CP12 | TERMINAL DOMAINS | PHOSPHORYLATION | GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE | MULTIDISCIPLINARY SCIENCES | STRUCTURAL DISORDER | POSTTRANSLATIONAL MODIFICATIONS | PLANT DEVELOPMENT | CHAPERONE | Ribosomal Proteins - chemistry | Phosphorylation | Histones - chemistry | Intrinsically Disordered Proteins - classification | Molecular Chaperones - chemistry | Phosphoproteins - chemistry | Ribosomal Proteins - classification | Chlamydomonas reinhardtii - genetics | Flagella - chemistry | Algal Proteins - genetics | Chlamydomonas reinhardtii - metabolism | Flagella - genetics | Protein Stability | Gene Ontology | Gene Expression | Intrinsically Disordered Proteins - isolation & purification | Algal Proteins - chemistry | Histones - classification | Molecular Chaperones - classification | Ribosomal Proteins - genetics | Molecular Sequence Annotation | Molecular Chaperones - genetics | Hot Temperature | Phosphoproteins - genetics | Algal Proteins - classification | Intrinsically Disordered Proteins - genetics | Phosphoproteins - classification | Histones - isolation & purification | Chlamydomonas reinhardtii - chemistry | Ribosomal Proteins - isolation & purification | Flagella - metabolism | Histones - genetics | Intrinsically Disordered Proteins - chemistry | Phosphoproteins - isolation & purification | Algal Proteins - isolation & purification | Molecular Chaperones - isolation & purification | Proteins | Databases | Ribosomal proteins | Protein folding | Amino acid composition | Histones | Mass spectroscopy | Chaperones | Nucleic acids | Flagella | Life Sciences | Biochemistry, Molecular Biology | Vegetal Biology
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 05/2005, Volume 280, Issue 19, pp. 18717 - 18727
...). Recent work demonstrated the importance of the tuberous sclerosis protein TSC2 for regulation of mTOR by insulin... 
ACTIVATION | ELONGATION-FACTOR-2 KINASE | RHEB | 4E-BINDING PROTEIN-1 | BIOCHEMISTRY & MOLECULAR BIOLOGY | GENE-PRODUCTS | INITIATION-FACTOR 4E | TRANSLATION | BINDING | PHOSPHORYLATION SITE | MTOR | Humans | Multienzyme Complexes - metabolism | Immunoblotting | Ras Homolog Enriched in Brain Protein | Elongation Factor 2 Kinase | AMP-Activated Protein Kinases | Phosphoproteins - chemistry | Time Factors | Guanosine Triphosphate - chemistry | Guanosine Diphosphate - chemistry | Protein Synthesis Inhibitors - pharmacology | Transgenes | Protein-Serine-Threonine Kinases - metabolism | Repressor Proteins - metabolism | Fibroblasts - metabolism | Tumor Suppressor Proteins - metabolism | Signal Transduction | Neuropeptides - metabolism | Tumor Suppressor Proteins - physiology | Adaptor Proteins, Signal Transducing | Models, Biological | Monomeric GTP-Binding Proteins - chemistry | Glucose - chemistry | Mice | TOR Serine-Threonine Kinases | Mutation | Neuropeptides - chemistry | Protein Kinases - metabolism | Monomeric GTP-Binding Proteins - physiology | Phosphorylation | Immunoprecipitation | Amino Acids - chemistry | Neuropeptides - physiology | Dose-Response Relationship, Drug | Repressor Proteins - physiology | Amino Acids - metabolism | Carrier Proteins - chemistry | Guanine - chemistry | Protein Structure, Tertiary | Cell Line | Cells, Cultured | Gene Expression Regulation | Hydrogen Peroxide - pharmacology | Cycloheximide - pharmacology | Hydrolysis | Animals | Monomeric GTP-Binding Proteins - metabolism | Ribosomal Protein S6 - metabolism | Adenosine Triphosphate - chemistry | Calcium-Calmodulin-Dependent Protein Kinases - metabolism | Sorbitol - pharmacology
Journal Article
International Journal of Molecular Sciences, ISSN 1661-6596, 07/2018, Volume 19, Issue 7, p. 1857
The LrtA protein of Synechocystis sp. PCC 6803 intervenes in cyanobacterial post-stress survival and in stabilizing 70S ribosomal particles... 
Spectroscopy | Protein stability | Conformational plasticity | Ribosomal protein | Folding | Disordered protein | disordered protein | BIOCHEMISTRY & MOLECULAR BIOLOGY | folding | LIGHT-REPRESSED TRANSCRIPT | ribosomal protein | SINGLE-STRANDED-DNA | IONIZABLE GROUPS | protein stability | CHEMISTRY, MULTIDISCIPLINARY | conformational plasticity | spectroscopy | SERVER | REGIONS | SECONDARY STRUCTURE ANALYSES | PK VALUES | BINDING | STRUCTURE PREDICTION | Ribosomal Proteins - chemistry | Protein Multimerization | Bacterial Proteins - chemistry | Ribosomes - metabolism | Synechocystis - chemistry | Ribosomal Proteins - metabolism | Thermodynamics | Solutions | Cloning, Molecular | Escherichia coli - metabolism | Protein Interaction Domains and Motifs | Protein Stability | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Gene Expression | Genetic Vectors - chemistry | Ribosomal Proteins - genetics | Bacterial Proteins - genetics | Ribosomes - chemistry | Genetic Vectors - metabolism | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Molecular Dynamics Simulation | Protein Folding | Amino Acid Motifs | Protein Conformation, beta-Strand | Escherichia coli - genetics | Bacterial Proteins - metabolism | Synechocystis - metabolism | Residues | Nuclear magnetic resonance--NMR | Self-association | Computer simulation | Fluorescence | Amino acid sequence | Molecular dynamics | Protein biosynthesis | Secondary structure | Circular dichroism | Proteins | Nanoparticles | Organic chemistry | Protein synthesis | Protein folding | Dichroism | Protein structure
Journal Article
Genes & development, ISSN 0890-9369, 2017, Volume 31, Issue 8, pp. 802 - 815
... its specificity for rDNA-associated proteins and show that this region binds directly to the rDNA-associated protein Csm1... 
Monopolin | RENT complex | STUbL | Sumoylation | RDNA silencing | Cohibin | Desumoylation | rDNA silencing | sumoylation | cohibin | DEVELOPMENTAL BIOLOGY | GENOME STABILITY | MONOPOLIN COMPLEX | IDENTIFICATION | SACCHAROMYCES-CEREVISIAE | CELL BIOLOGY | SUMOYLATED PROTEINS | YEAST | REPLICATION | monopolin | PATHWAY | GENETICS & HEREDITY | PROMOTES | desumoylation | DNA, Ribosomal - metabolism | Intracellular Signaling Peptides and Proteins - metabolism | Cell Cycle Proteins - chemistry | Endopeptidases - chemistry | Proteolysis | Cell Nucleolus - metabolism | Protein Structure, Quaternary | Cell Cycle Proteins - genetics | Protein Stability | Nuclear Proteins - genetics | Endopeptidases - metabolism | Small Ubiquitin-Related Modifier Proteins - metabolism | Cell Cycle Proteins - metabolism | Crystallization | Gene Silencing | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Nuclear Proteins - metabolism | Saccharomyces cerevisiae Proteins - genetics | Nuclear Proteins - chemistry | Ubiquitin-Protein Ligases - chemistry | Amino Acid Motifs | Endopeptidases - genetics | Intracellular Signaling Peptides and Proteins - chemistry | Small Ubiquitin-Related Modifier Proteins - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Ubiquitin-Protein Ligases - genetics | Saccharomyces cerevisiae Proteins - chemistry | Ubiquitin | Post-translational modification | Gene silencing | Ligases | Research | Genetic regulation | Protein-protein interactions | Research Paper
Journal Article