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Nucleic acids research, ISSN 1362-4962, 2020, Volume 48, Issue 1, pp. 349 - 358
Modifications at the 5′-end of RNAs play a pivotal role in determining their fate. In eukaryotes, the DXO/Rai1 family of enzymes removes numerous 5′-end RNA... 
PATHWAYS | YEAST | CAP | PROTEIN | RNA | HUMAN-CELLS | BIOCHEMISTRY & MOLECULAR BIOLOGY | NAD(+) | IDENTIFICATION | QUALITY-CONTROL MECHANISM | RNA-Binding Proteins - genetics | Exoribonucleases - genetics | Arabidopsis - enzymology | Chloroplast Proteins - genetics | Saccharomyces cerevisiae - genetics | Exoribonucleases - chemistry | Substrate Specificity | Crystallography, X-Ray | RNA, Messenger - metabolism | Trans-Activators - chemistry | Chloroplast Proteins - chemistry | Arabidopsis Proteins - metabolism | Cloning, Molecular | Escherichia coli - metabolism | Trans-Activators - genetics | Protein Interaction Domains and Motifs | Nuclear Proteins - genetics | Binding Sites | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Arabidopsis Proteins - genetics | Gene Expression | Genetic Vectors - chemistry | RNA, Messenger - genetics | RNA-Binding Proteins - chemistry | Genetic Vectors - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Nuclear Proteins - metabolism | Recombinant Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Nuclear Proteins - chemistry | Arabidopsis - genetics | Animals | Arabidopsis Proteins - chemistry | Protein Conformation, beta-Strand | Escherichia coli - genetics | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Saccharomyces cerevisiae - enzymology | RNA, Messenger - chemistry | Trans-Activators - metabolism | Mice | Chloroplast Proteins - metabolism | Exoribonucleases - metabolism | RNA-Binding Proteins - metabolism | Saccharomyces cerevisiae Proteins - chemistry | nucleic acid enzymes | BASIC BIOLOGICAL SCIENCES | Nucleic Acid Enzymes
Journal Article
PLoS pathogens, ISSN 1553-7374, 2018, Volume 14, Issue 1, p. e1006695
[...]either alteration of Sis1 results in the loss of [URE3], but deletion of the J protein Swa2 results in loss of [URE3] alone [26, 33, 34... 
REQUIREMENTS | APPEARANCE | PSI+ PRION | MICROBIOLOGY | HSP40 FUNCTION | SACCHAROMYCES-CEREVISIAE | PROTEIN DISAGGREGATION | SIS1 | VIROLOGY | IN-VIVO | AUXILIN | PROPAGATION | PARASITOLOGY | Peptide Fragments | Molecular Chaperones - metabolism | Prions - genetics | Saccharomyces cerevisiae - genetics | Vesicular Transport Proteins - metabolism | Protein Multimerization | Molecular Chaperones - chemistry | Phosphoproteins - metabolism | Prion Proteins - metabolism | Phosphoproteins - chemistry | Heat-Shock Proteins - genetics | Glutathione Peroxidase - chemistry | Gene Deletion | HSP70 Heat-Shock Proteins - chemistry | Protein Interaction Domains and Motifs | Prion Proteins - chemistry | HSP40 Heat-Shock Proteins - chemistry | Prion Proteins - genetics | Dimerization | Glutathione Peroxidase - metabolism | Prions - metabolism | HSP40 Heat-Shock Proteins - metabolism | Saccharomyces cerevisiae - physiology | HSP40 Heat-Shock Proteins - genetics | Heat-Shock Proteins - metabolism | Vesicular Transport Proteins - genetics | Molecular Chaperones - genetics | Models, Molecular | HSP70 Heat-Shock Proteins - genetics | Vesicular Transport Proteins - chemistry | Phosphoproteins - genetics | Prions - chemistry | Saccharomyces cerevisiae Proteins - genetics | Glutathione Peroxidase - genetics | HSP70 Heat-Shock Proteins - metabolism | Prions - physiology | Saccharomyces cerevisiae Proteins - metabolism | Saccharomyces cerevisiae - enzymology | Heat-Shock Proteins - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Amino acids | Research | Yeast fungi | Health aspects | Prions | Proteins | Baking yeast | Yeast | Propagation | Mammals
Journal Article
Molecular cell, ISSN 1097-2765, 2017, Volume 67, Issue 5, pp. 837 - 852.e7
.... Architectural proteins insulate compartmental domains by reducing interaction frequencies between neighboring regions in Drosophila, but CTCF loops do not play a distinct role in this organism... 
transcription | Hi-C | TAD | loop | compartment | CTCF | insulator | epigenetics | TOPOLOGY | SYSTEM | PROMOTERS | INITIATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ARCHITECTURE | PROVIDES | DOMAINS | GENOME | CTCF SITES | REVEALS | CELL BIOLOGY | Chromatin - metabolism | Histones - chemistry | Caenorhabditis elegans Proteins - chemistry | Humans | Caenorhabditis elegans Proteins - metabolism | Structure-Activity Relationship | Drosophila Proteins - metabolism | Drosophila melanogaster - genetics | Arabidopsis Proteins - metabolism | Drosophila melanogaster - metabolism | DNA, Plant - chemistry | Computer Simulation | Transcription, Genetic | Nucleic Acid Conformation | DNA, Plant - genetics | Chromatin - chemistry | Arabidopsis Proteins - genetics | Caenorhabditis elegans - metabolism | Chromosomal Proteins, Non-Histone - metabolism | Caenorhabditis elegans - genetics | Chromatin Assembly and Disassembly | DNA - metabolism | Drosophila Proteins - chemistry | DNA, Plant - metabolism | Arabidopsis - metabolism | Chromosomal Proteins, Non-Histone - genetics | Arabidopsis - genetics | DNA - genetics | DNA - chemistry | Animals | Histones - genetics | Arabidopsis Proteins - chemistry | Models, Biological | Protein Conformation | Drosophila Proteins - genetics | Histones - metabolism | Caenorhabditis elegans Proteins - genetics | Chromatin - genetics | Chromosomal Proteins, Non-Histone - chemistry | Arabidopsis thaliana | Chromatin | Epigenetic inheritance
Journal Article
Nature (London), ISSN 1476-4687, 2010, Volume 468, Issue 7322, pp. 400 - 405
Journal Article
Trends in biochemical sciences (Amsterdam. Regular ed.), ISSN 0968-0004, 2016, Volume 41, Issue 4, pp. 338 - 355
...-lactam antibiotics, but is now known to be widely distributed. The MBL core protein fold is present in human enzymes with diverse biological roles, including cell... 
metallo β-lactamase fold protein | β-lactam antibiotic and cancer drug resistance | hydrogen sulphide metabolism | RNA processing | nuclease | DNA repair | HUMAN SNM1A | MYOFIBRILLOGENESIS REGULATOR | CROSS-LINK REPAIR | BIOCHEMISTRY & MOLECULAR BIOLOGY | ANTIBIOTIC-RESISTANCE | NON-KINESIGENIC DYSKINESIA | GLYOXALASE-II | MOLECULAR-CLONING | CANCER SUSCEPTIBILITY GENE | HYDROLYZING PHOSPHOLIPASE-D | N-ACETYLNEURAMINIC ACID | beta-Lactams - metabolism | Arabidopsis - enzymology | Zinc - metabolism | Humans | DNA Repair Enzymes - genetics | Mitochondrial Proteins - genetics | Zinc - chemistry | beta-Lactamases - genetics | Mitochondrial Proteins - metabolism | Nucleocytoplasmic Transport Proteins - chemistry | DNA Repair Enzymes - metabolism | Muscle Proteins - metabolism | Protein Interaction Domains and Motifs | beta-Lactamases - metabolism | Nuclear Proteins - genetics | DNA Repair Enzymes - chemistry | Protein Conformation, alpha-Helical | Gene Expression | Nuclear Proteins - metabolism | Nuclear Proteins - chemistry | Bacteria - genetics | beta-Lactams - chemistry | Nucleocytoplasmic Transport Proteins - genetics | Protein Folding | Arabidopsis - genetics | Hydrolysis | Muscle Proteins - genetics | beta-Lactamases - chemistry | Nucleocytoplasmic Transport Proteins - metabolism | Protein Conformation, beta-Strand | Mitochondrial Proteins - chemistry | Protein Binding | Bacteria - enzymology | Muscle Proteins - chemistry | Thiolester Hydrolases - genetics | Thiolester Hydrolases - metabolism | Thiolester Hydrolases - chemistry | Review
Journal Article
Science (American Association for the Advancement of Science), ISSN 1095-9203, 2019, Volume 364, Issue 6435, pp. eaav5870 - 44
.... We reconstituted an active complex containing the coiled-coil NLR ZAR1, the pseudokinase RKS1, uridylated protein kinase PBL2, and 2′-deoxyadenosine 5′-triphosphate (dATP... 
RUST RESISTANCE PROTEIN | CRYSTAL-STRUCTURE | CASPASE-9 ACTIVATION | MULTIDISCIPLINARY SCIENCES | DOMAIN-LIKE PROTEIN | NUCLEOTIDE-BINDING | COILED-COIL | CRYO-EM STRUCTURE | DISEASE RESISTANCE | CELL-DEATH | PATHOGEN PERCEPTION | Arabidopsis - enzymology | Disease Resistance | Protein Structure, Secondary | Arabidopsis - immunology | Adenosine Diphosphate - chemistry | Phosphoproteins - chemistry | Host-Pathogen Interactions - immunology | NLR Proteins - chemistry | Arabidopsis Proteins - metabolism | Cryoelectron Microscopy | Membrane Proteins | Arabidopsis - microbiology | Arabidopsis Proteins - chemistry | Intracellular Signaling Peptides and Proteins - chemistry | Protein Domains | Bacterial Proteins - metabolism | Carrier Proteins - chemistry | Ligands | Protein-Serine-Threonine Kinases - chemistry | Protein-Serine-Threonine Kinases - metabolism | Xanthomonas campestris - enzymology | Nucleoside-Phosphate Kinase - metabolism | Cell proliferation | Coils | Defensive behavior | Activation | Helices | Biochemistry | Leucine | Kinases | Remodeling | Immunity | Plant cells | Proteins | Disease resistance | Receptors | Microorganisms | Adenosine triphosphate | Pathogens | Hypersensitive response | Immune response | Oligomerization | Filtration | Mortality | Nlr protein | Electron microscopy | Deoxyadenosine | Switching | Domains | Transmission electron microscopy | Microscopy | Mutagenesis | Protein kinase | Cell death | Effectors | Gel filtration | Mustard | Mutation | ATP | Apoptosis
Journal Article
Cellular and Molecular Life Sciences, ISSN 1420-682X, 3/2013, Volume 70, Issue 5, pp. 761 - 775
Protein quality control is vital for all living cells and sophisticated molecular mechanisms have evolved to prevent the excessive accumulation of unfolded proteins... 
Life Sciences | Biochemistry, general | X-ray crystallography | Oligomerization | Life Sciences, general | Molecular switch | Protein quality control | PDZ domain | Biomedicine general | Cell Biology | ENTERICA SEROVAR TYPHIMURIUM | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | CELLULAR STRESS | HEAT-SHOCK-PROTEIN | CELL BIOLOGY | PROTEOLYTIC ACTIVITY | PDZ DOMAINS | STRUCTURAL BASIS | COMPLEX REVEALS | SERINE-PROTEASE | Bacteria - chemistry | Humans | Stress, Physiological | Arabidopsis Proteins - metabolism | Mitochondrial Proteins - metabolism | Plant Proteins - chemistry | Plant Proteins - metabolism | Plants - chemistry | Peptide Hydrolases - metabolism | Bacteria - metabolism | Periplasmic Proteins - chemistry | Heat-Shock Proteins - metabolism | High-Temperature Requirement A Serine Peptidase 1 | Models, Molecular | Escherichia coli Proteins - metabolism | Serine Endopeptidases - chemistry | Peptide Hydrolases - chemistry | Protein Folding | High-Temperature Requirement A Serine Peptidase 2 | Plants - metabolism | Animals | Arabidopsis Proteins - chemistry | Mitochondrial Proteins - chemistry | PDZ Domains | Periplasmic Proteins - metabolism | Serine Endopeptidases - metabolism | Escherichia coli Proteins - chemistry | Heat-Shock Proteins - chemistry | Oligomers | Proteins | Proteases | Quality control | Universities and colleges | Cells | Quality management | Stress analysis
Journal Article
The Plant cell, ISSN 1040-4651, 11/2012, Volume 24, Issue 11, pp. 4465 - 4482
.... Effective coupling of the enzymes in the pathway thus seems to be required. Subcellular localization, mobility, protein... 
Proteins | Enzymes | Lignin | Protein metabolism | Sterols | RESEARCH ARTICLES | Hematocrit | Fluorescence | Cytochromes | Plants | Plant cells | ENDOPLASMIC-RETICULUM MEMBRANE | MOLECULAR-INTERACTIONS | ARABIDOPSIS-THALIANA | BIOCHEMISTRY & MOLECULAR BIOLOGY | CINNAMIC ACID | PHENYLALANINE AMMONIA-LYASE | CYTOCHROME P450 REDUCTASE | PLANT SCIENCES | CELL BIOLOGY | PHENYLPROPANOID PATHWAY | TANDEM AFFINITY PURIFICATION | ENZYME COMPLEXES | BINDING PROTEIN-1 | Green Fluorescent Proteins | Protein Multimerization | Cytochrome P-450 Enzyme System - metabolism | Endoplasmic Reticulum - metabolism | Trans-Cinnamate 4-Monooxygenase - genetics | Acyltransferases - metabolism | Recombinant Fusion Proteins | Coenzyme A Ligases - metabolism | Arabidopsis Proteins - metabolism | Trans-Cinnamate 4-Monooxygenase - metabolism | Lignin - metabolism | Plants, Genetically Modified | Membrane Proteins - metabolism | Transgenes | Acyl Coenzyme A - metabolism | Arabidopsis Proteins - genetics | Hydroxylation | Hydroxybenzoates - metabolism | Membrane Proteins - genetics | Tobacco - metabolism | Arabidopsis - metabolism | Protein Interaction Mapping | Arabidopsis - genetics | Plant Leaves - genetics | Plant Leaves - metabolism | Tobacco - genetics | Cytochrome P-450 Enzyme System - genetics | Phytochemistry | Physiological aspects | Biosynthesis | Research | Protein-protein interactions | Membrane proteins | Life Sciences | Molecular biology | Cellular Biology | Biochemistry, Molecular Biology
Journal Article
PloS one, ISSN 1932-6203, 2012, Volume 7, Issue 8, p. e41922
To improve our understanding of uranium toxicity, the determinants of uranyl affinity in proteins must be better characterized... 
SPECTROSCOPY | AMINO-ACIDS | PROTEIN-KINASE CK2 | COMPLEXES | CALCIUM | BIOLOGY | GAS-PHASE | COORDINATION | URANYL-ION | SPECTRA | AQUEOUS-SOLUTION | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Calmodulin - genetics | Arabidopsis Proteins - genetics | Phosphorylation | Arabidopsis - chemistry | Calmodulin - metabolism | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Casein Kinase II - genetics | Uranium - metabolism | Arabidopsis - metabolism | Arabidopsis - genetics | Arabidopsis Proteins - metabolism | Uranium - toxicity | Casein Kinase II - chemistry | Arabidopsis Proteins - chemistry | Protein Engineering | Protein Binding | Uranium - chemistry | Calmodulin - chemistry | Casein Kinase II - metabolism | Hydrogen-Ion Concentration | Arabidopsis thaliana | Tyrosine | Uranium | Analysis | Physiological aspects | Fluorescence | Protein kinases | Calmodulin | Protein binding | Protein kinase C | Peptides | Calcium | Toxicity | Physical chemistry | Amino acids | Biochemistry | Kinases | pH effects | Casein kinase II | Proteins | Spectrometry | Hydrogen ions | Calcium-binding protein | Catalysis | Dissociation | Uranium dioxide | Vibration | Threonine | Chromatography | Ion-exchange chromatography | EF-hand | Homogeneity | Affinity | Ligands | Binding sites | Life Sciences | Biomolecules | Environmental Engineering | Biochemistry, Molecular Biology | Environmental Sciences
Journal Article
The Plant cell, ISSN 1532-298X, 2013, Volume 25, Issue 1, pp. 270 - 287
...% protein and up to 40% lignin. These wall polymers interact covalently and noncovalently to form the functional cell wall... 
Proteins | Music analysis | Polysaccharides | Proteoglycans | Cell walls | RESEARCH ARTICLES | Mass spectroscopy | Plants | Xylans | Sugars | Plant cells | BAMBOO SHOOT | ACID | MOLECULAR-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | STRUCTURAL-CHARACTERIZATION | MASS-SPECTROMETRY | CULTURED SYCAMORE CELLS | PLANT SCIENCES | CELL BIOLOGY | RHAMNOGALACTURONAN | POLYSACCHARIDES | PLANTS | RICH EXTENSIN | Models, Structural | Mucoproteins - immunology | Xylans - metabolism | Pectins - metabolism | Glycoproteins - metabolism | Molecular Sequence Data | Biomass | Proteoglycans - chemistry | Arabidopsis Proteins - metabolism | Plant Proteins - chemistry | Glycoproteins - isolation & purification | Polysaccharides - chemistry | Plant Proteins - metabolism | Antibodies, Monoclonal - immunology | Mucoproteins - genetics | Glycoproteins - genetics | Amino Acid Sequence | Arabidopsis Proteins - genetics | Arabidopsis - chemistry | Cell Wall - genetics | Proteoglycans - metabolism | Plant Proteins - immunology | Cell Wall - chemistry | Epitopes | Pectins - chemistry | Arabidopsis - metabolism | Polysaccharides - metabolism | Arabidopsis - genetics | Arabidopsis Proteins - isolation & purification | Plant Proteins - genetics | Xylans - chemistry | Arabidopsis Proteins - chemistry | Mucoproteins - chemistry | Cell Wall - metabolism | Protein Isoforms | Proteomics | Mutation | Mucoproteins - metabolism | Arabidopsis thaliana | Physiological aspects | Genetic aspects | Pectin | Properties
Journal Article
The journal of physical chemistry. B, ISSN 1520-6106, 03/2017, Volume 121, Issue 11, pp. 2407 - 2419
The yellow fluorescent protein (YFP) is frequently used in a protein complementation assay called bimolecular fluorescence complementation (BiFC... 
VISUALIZATION | GFP | SINGLE-MOLECULE SPECTROSCOPY | ROOM-TEMPERATURE | MUTANTS | CHROMOPHORE | STRUCTURAL BASIS | CRYSTAL-STRUCTURE | CHEMISTRY, PHYSICAL | EXCITED-STATE DYNAMICS | CYAN | Transcription Factors - chemistry | Bacterial Proteins - chemistry | Fluorescence | Green Fluorescent Proteins - genetics | Basic-Leucine Zipper Transcription Factors - radiation effects | Luminescent Proteins - radiation effects | Recombinant Fusion Proteins - radiation effects | Light | Luminescent Proteins - chemistry | Bacteria | Green Fluorescent Proteins - chemistry | Peptide Fragments - genetics | Arabidopsis Proteins - genetics | Transcription Factors - radiation effects | Green Fluorescent Proteins - radiation effects | Arabidopsis | Bacterial Proteins - genetics | Bacterial Proteins - radiation effects | Basic-Leucine Zipper Transcription Factors - genetics | Recombinant Fusion Proteins - chemistry | Transcription Factors - genetics | Peptide Fragments - radiation effects | Arabidopsis Proteins - radiation effects | Protein Interaction Mapping | Peptide Fragments - chemistry | Arabidopsis Proteins - chemistry | Basic-Leucine Zipper Transcription Factors - chemistry | Recombinant Fusion Proteins - genetics | Luminescent Proteins - genetics | Mutation | Hydrogen-Ion Concentration | Proteins | Research | Yellow fluorescent proteins | Protein-protein interactions
Journal Article