X
Search Filters
Format Format
Format Format
X
Sort by Item Count (A-Z)
Filter by Count
Journal Article (1450) 1450
Publication (364) 364
Book Review (133) 133
Book Chapter (34) 34
Conference Proceeding (12) 12
Book / eBook (2) 2
Dissertation (2) 2
more...
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
index medicus (1389) 1389
biochemistry & molecular biology (897) 897
exoribonucleases - metabolism (847) 847
humans (536) 536
exoribonucleases - genetics (508) 508
cell biology (382) 382
animals (374) 374
rna, messenger - metabolism (350) 350
molecular sequence data (343) 343
rna (287) 287
saccharomyces-cerevisiae (278) 278
exoribonucleases (275) 275
exoribonucleases - chemistry (272) 272
base sequence (255) 255
messenger-rna (246) 246
mutation (239) 239
escherichia-coli (230) 230
degradation (223) 223
amino acid sequence (213) 213
rna stability (213) 213
proteins (209) 209
protein binding (188) 188
article (187) 187
saccharomyces cerevisiae - genetics (178) 178
ribonuclease (174) 174
gene expression (169) 169
research (167) 167
protein (166) 166
rna, messenger - genetics (166) 166
exoribonuclease (158) 158
saccharomyces cerevisiae proteins - metabolism (156) 156
yeast (156) 156
rna - metabolism (144) 144
substrate specificity (144) 144
models, molecular (140) 140
rna processing, post-transcriptional (138) 138
molecular biology (136) 136
messenger rna (133) 133
saccharomyces cerevisiae proteins - genetics (131) 131
ribonucleic acid--rna (130) 130
escherichia coli - genetics (129) 129
endoribonucleases - metabolism (128) 128
saccharomyces cerevisiae - metabolism (127) 127
nucleic acid conformation (126) 126
quality-control (126) 126
complex (124) 124
polynucleotide phosphorylase (124) 124
mice (121) 121
genetic aspects (114) 114
enzymes (113) 113
ribosomal-rna (113) 113
rna-binding proteins - metabolism (113) 113
exosome multienzyme ribonuclease complex (112) 112
gene-expression (112) 112
escherichia coli - enzymology (111) 111
expression (110) 110
gene (107) 107
exosome (102) 102
protein structure, tertiary (101) 101
analysis (100) 100
genes (100) 100
physiological aspects (100) 100
rna precursors - metabolism (100) 100
biophysics (98) 98
identification (97) 97
kinetics (97) 97
microbiology (96) 96
transcription, genetic (96) 96
binding sites (95) 95
decay (95) 95
polyadenylation (95) 95
dna (94) 94
poly polymerase (94) 94
saccharomyces cerevisiae proteins (94) 94
rna, bacterial - metabolism (88) 88
hela cells (84) 84
exonucleases - metabolism (82) 82
exoribonucleases - physiology (81) 81
poly a - metabolism (81) 81
cell line (79) 79
rna, fungal - metabolism (79) 79
biochemistry (78) 78
fungal proteins - metabolism (77) 77
crystal-structure (76) 76
saccharomyces cerevisiae - enzymology (76) 76
transcription (76) 76
deadenylation (75) 75
exonuclease (75) 75
multidisciplinary sciences (75) 75
escherichia coli - metabolism (74) 74
rna-binding proteins - genetics (73) 73
sequence homology, amino acid (73) 73
14-3-3 proteins (72) 72
genetics & heredity (72) 72
research article (72) 72
binding (71) 71
rna interference (71) 71
female (70) 70
models, biological (70) 70
nuclear proteins - metabolism (70) 70
more...
Library Location Library Location
Language Language
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


Advanced Materials, ISSN 0935-9648, 02/2016, Volume 28, Issue 5, pp. 898 - 904
Journal Article
RNA, ISSN 1355-8382, 06/2019, Volume 25, Issue 6, pp. 737 - 746
Human RNA exoribonuclease 2 (Rexo2) is an evolutionarily conserved 3'-to-5' DEDDh-family exonuclease located primarily in mitochondria. Rexo2 degrades small... 
RNA decay | Exonuclease | Protein–RNA interactions | Ribonuclease | Crystal structure | STRANDED-RNA | exonuclease | CRYSTAL-STRUCTURE | DNA | BIOCHEMISTRY & MOLECULAR BIOLOGY | crystal structure | protein-RNA interactions | ribonuclease | OLIGORIBONUCLEASE | FAMILY | Exoribonucleases - genetics | Humans | Protein Multimerization | Exoribonucleases - chemistry | Crystallography, X-Ray | Mitochondrial Proteins - genetics | RNA - genetics | DNA, Single-Stranded - genetics | Oligoribonucleotides - metabolism | Mitochondrial Proteins - metabolism | Cloning, Molecular | Escherichia coli - metabolism | Biomarkers, Tumor - metabolism | Protein Interaction Domains and Motifs | Oligoribonucleotides - chemistry | Mitochondria - chemistry | Binding Sites | 14-3-3 Proteins - genetics | RNA - metabolism | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Gene Expression | Genetic Vectors - chemistry | DNA, Single-Stranded - metabolism | Genetic Vectors - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Magnesium - metabolism | Mitochondria - metabolism | Recombinant Proteins - genetics | RNA - chemistry | DNA, Single-Stranded - chemistry | 14-3-3 Proteins - metabolism | Hydrolysis | Magnesium - chemistry | Cations, Divalent | Protein Conformation, beta-Strand | Escherichia coli - genetics | Mitochondrial Proteins - chemistry | Hydrophobic and Hydrophilic Interactions | Protein Binding | 14-3-3 Proteins - chemistry | Biomarkers, Tumor - genetics | Biomarkers, Tumor - chemistry | Exoribonucleases - metabolism | Oligoribonucleotides - genetics | Mitochondria | Single-stranded DNA | Oligonucleotides | Nucleotides | Magnesium | Hydrophobicity | Ribonucleic acid--RNA | Deoxyribonucleic acid--DNA | protein–RNA interactions
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 02/2016, Volume 291, Issue 7, pp. 3668 - 3681
The intracellular infections of Mycobacterium tuberculosis, which is the causative agent of tuberculosis, are regulated by many cyclic dinucleotide signaling.... 
enzyme degradation | PROTEIN | LONG-TERM SURVIVAL | BIOCHEMISTRY & MOLECULAR BIOLOGY | RESOLUTION | structure-function | GMP | SPORULATION | IDENTIFICATION | Mycobacterium tuberculosis | AFFECT BACTERIAL-GROWTH | phosphodiesterases | LEADS | cyclic diadenosine monophosphate (c-di-AMP) | AMP PHOSPHODIESTERASE | REVEALS | Exoribonucleases - genetics | Bacterial Proteins - chemistry | Exoribonucleases - chemistry | Molecular Sequence Data | Substrate Specificity | Dinucleoside Phosphates - chemistry | Recombinant Fusion Proteins - metabolism | Cyclic AMP - chemistry | Cyclic AMP - analogs & derivatives | Cyclic GMP - analogs & derivatives | Cyclic GMP - chemistry | Conserved Sequence | Cyclic AMP - metabolism | Peptide Fragments - genetics | Recombinant Proteins - metabolism | 3',5'-Cyclic-AMP Phosphodiesterases - metabolism | Amino Acid Sequence | Catalytic Domain | Peptide Fragments - metabolism | Biocatalysis | 3',5'-Cyclic-GMP Phosphodiesterases - genetics | Bacterial Proteins - genetics | Models, Molecular | Recombinant Proteins - chemistry | 3',5'-Cyclic-GMP Phosphodiesterases - chemistry | 3',5'-Cyclic-AMP Phosphodiesterases - genetics | Recombinant Fusion Proteins - chemistry | Dinucleoside Phosphates - metabolism | Peptide Fragments - chemistry | Sequence Alignment | 3',5'-Cyclic-AMP Phosphodiesterases - chemistry | 3',5'-Cyclic-GMP Phosphodiesterases - metabolism | Cyclic GMP - metabolism | Mycobacterium tuberculosis - enzymology | Bacterial Proteins - metabolism | Protein Conformation | Mutation | Exoribonucleases - metabolism | Index Medicus | Enzymology
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 11/2004, Volume 279, Issue 47, pp. 48702 - 48706
Journal Article
Biochemistry, ISSN 0006-2960, 2017, Volume 56, Issue 30, pp. 3972 - 3982
Proteins typically interact with multiple binding partners, and often different parts of their surfaces are employed to establish these protein protein... 
COMPLEX | SMALL-MOLECULE STABILIZATION | INHIBITION | MEMBRANE H+-ATPASE | STRUCTURAL BASIS | YAP/TAZ | BIOCHEMISTRY & MOLECULAR BIOLOGY | HIPPO PATHWAY | PROTON PUMP ATPASE | CANCER | FAMILY | Exoribonucleases - genetics | Phosphorylation | Transcription Factors - chemistry | Humans | Exoribonucleases - chemistry | Crystallography, X-Ray | Peptide Library | Recombinant Fusion Proteins - metabolism | Protein Isoforms - metabolism | Protein Isoforms - chemistry | Gene Deletion | Biomarkers, Tumor - metabolism | Conserved Sequence | Nuclear Magnetic Resonance, Biomolecular | Protein Interaction Domains and Motifs | Binding Sites | Peptide Fragments - genetics | 14-3-3 Proteins - genetics | Recombinant Proteins - metabolism | Amino Acid Sequence | Peptide Fragments - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Fusion Proteins - chemistry | Transcription Factors - genetics | Protein Interaction Mapping | 14-3-3 Proteins - metabolism | Transcription Factors - metabolism | Peptide Fragments - chemistry | 14-3-3 Proteins - chemistry | Ligands | Protein Conformation | Biomarkers, Tumor - genetics | Protein Processing, Post-Translational | Kinetics | Biomarkers, Tumor - chemistry | Exoribonucleases - metabolism | Protein Isoforms - genetics | X-ray crystallography | Usage | Ligand binding (Biochemistry) | Analysis | Research | Nuclear magnetic resonance | Protein-protein interactions | Index Medicus
Journal Article
RNA, ISSN 1355-8382, 11/2012, Volume 18, Issue 11, pp. 2029 - 2040
All arthropod-borne flaviviruses generate a short noncoding RNA (sfRNA) from the viral 3' untranslated region during infection due to stalling of the cellular... 
Virus-host interaction | Noncoding RNA | Flavivirus | mRNA decay | mRNA stability | CELLS | noncoding RNA | DECAY | BIOCHEMISTRY & MOLECULAR BIOLOGY | PSEUDOKNOT | virus-host interaction | ELEMENTS | POLY(RC) BINDING-PROTEINS | P-BODIES | GENE-EXPRESSION | DEGRADATION | SUBGENOMIC RNA | flavivirus | WEST-NILE | Microtubule-Associated Proteins - chemistry | Oligonucleotide Array Sequence Analysis | RNA, Untranslated - metabolism | Microtubule-Associated Proteins - metabolism | Humans | Exoribonucleases - chemistry | Transcriptome | Half-Life | RNA, Messenger - metabolism | RNA, Viral - physiology | Aedes - virology | West Nile virus - genetics | RNA, Untranslated - chemistry | RNA, Untranslated - physiology | RNA, Viral - metabolism | 3' Untranslated Regions | Insect Proteins - metabolism | Cell Line | Cricetinae | West Nile virus - physiology | Saccharomyces cerevisiae Proteins - antagonists & inhibitors | Gene Expression Regulation | Exoribonucleases - antagonists & inhibitors | Microtubule-Associated Proteins - antagonists & inhibitors | RNA Stability | Insect Proteins - antagonists & inhibitors | Host-Pathogen Interactions | Dengue Virus - genetics | Animals | RNA, Viral - chemistry | Insect Proteins - chemistry | Dengue Virus - physiology | RNA, Messenger - chemistry | Aedes - cytology | Exoribonucleases - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Index Medicus | virus–host interaction
Journal Article
Journal Article
Nature, ISSN 0028-0836, 12/2010, Volume 468, Issue 7325, pp. 779 - 783
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 06/2016, Volume 138, Issue 25, pp. 7951 - 7964
Journal Article
Nature Communications, ISSN 2041-1723, 12/2018, Volume 9, Issue 1, pp. 97 - 97
Nuclease and helicase activities play pivotal roles in various aspects of RNA processing and degradation. These two activities are often present in... 
YEAST | COMPLEX | PROTEIN | SMALL-ANGLE SCATTERING | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | GENE-EXPRESSION | EXOSOME | X-RAY-SCATTERING | DEGRADATION | QUATERNARY STRUCTURE | Endoribonucleases - chemistry | RNA Helicases - metabolism | Endoribonucleases - genetics | Exoribonucleases - genetics | Saccharomyces cerevisiae - genetics | Exoribonucleases - chemistry | Multienzyme Complexes - metabolism | Crystallography, X-Ray | Mitochondrial Proteins - genetics | RNA Helicases - chemistry | RNA - genetics | Saccharomyces cerevisiae - metabolism | Mitochondrial Proteins - metabolism | Base Sequence | RNA Helicases - genetics | DEAD-box RNA Helicases - metabolism | Nucleic Acid Conformation | DEAD-box RNA Helicases - chemistry | RNA - metabolism | Amino Acid Sequence | Polyribonucleotide Nucleotidyltransferase - metabolism | Endoribonucleases - metabolism | Polyribonucleotide Nucleotidyltransferase - genetics | Multienzyme Complexes - genetics | Saccharomyces cerevisiae Proteins - genetics | RNA - chemistry | Candida glabrata - metabolism | Multienzyme Complexes - chemistry | Sequence Homology, Amino Acid | DEAD-box RNA Helicases - genetics | RNA, Mitochondrial | Mitochondrial Proteins - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Saccharomyces cerevisiae - enzymology | Protein Conformation | Candida glabrata - genetics | Candida glabrata - enzymology | Exoribonucleases - metabolism | Polyribonucleotide Nucleotidyltransferase - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Biodegradation | Yeast | Nucleic acids | Gene expression | Metabolism | Ribonucleic acid--RNA | DNA helicase | Mitochondria | Enzymatic activity | Nuclease | RNA processing | Crystal structure | Structural analysis | Index Medicus
Journal Article
Structure, ISSN 0969-2126, 02/2017, Volume 25, Issue 2, pp. 305 - 316
By interacting with hundreds of protein partners, 14-3-3 proteins coordinate vital cellular processes. Phosphorylation of the small heat shock protein, HSPB6,... 
14-3-3 proteins | smooth muscle relaxation | small heat shock proteins | regulatory complex | crystal structure | protein-protein interaction | phosphopeptides | conformational change | small-angle X-ray scattering | intrinsically disordered regions | PHOSPHORYLATION | MOLECULE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ALPHA-B-CRYSTALLIN | CELL BIOLOGY | DOMAIN DIMERS | BIOPHYSICS | PURIFICATION | AIRWAY SMOOTH-MUSCLE | BINDING | EXPRESSION | WEB SERVER | HSP20 HSPB6 | Exoribonucleases - genetics | Phosphorylation | Humans | Protein Multimerization | Exoribonucleases - chemistry | Substrate Specificity | Crystallography, X-Ray | HSP20 Heat-Shock Proteins - genetics | Phosphoproteins - metabolism | HSP20 Heat-Shock Proteins - metabolism | Phosphoproteins - chemistry | Cloning, Molecular | Escherichia coli - metabolism | Biomarkers, Tumor - metabolism | Protein Interaction Domains and Motifs | Binding Sites | HSP20 Heat-Shock Proteins - chemistry | 14-3-3 Proteins - genetics | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Gene Expression | Signal Transduction | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Phosphoproteins - genetics | Intrinsically Disordered Proteins - genetics | Amino Acid Motifs | 14-3-3 Proteins - metabolism | Protein Conformation, beta-Strand | Escherichia coli - genetics | Intrinsically Disordered Proteins - chemistry | Protein Binding | 14-3-3 Proteins - chemistry | Biomarkers, Tumor - genetics | Biomarkers, Tumor - chemistry | Exoribonucleases - metabolism | Intrinsically Disordered Proteins - metabolism | Proteins | Fluorescence spectroscopy | Proteolysis | Analysis | Crystals | Fluorescence | Atoms | Heat shock proteins | Molecular biology | Structure | Protein-protein interactions | Index Medicus | small angle X-ray scattering
Journal Article
Cell, ISSN 0092-8674, 2006, Volume 127, Issue 6, pp. 1223 - 1237
The RNA exosome is a multisubunit 3′ to 5′ exoribonuclease complex that participates in degradation and processing of cellular RNA. To determine the activities... 
COMPLEX | PROTEIN | MESSENGER-RNA | YEAST EXOSOME | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | COMPONENTS |