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Science, ISSN 0036-8075, 03/2017, Volume 355, Issue 6331, pp. 1312 - 1317
Journal Article
Biochemical Journal, ISSN 0264-6021, 02/2012, Volume 441, Issue 3, pp. 803 - 812
PABP1 [poly(A)-binding protein 1] is a central regulator of mRNA translation and stability and is required for miRNA (microRNA)-mediated regulation and... 
Poly(A)-binding-protein- interacting motif 2 (PAM2)-poly(A)-binding protein C-terminal domain (PABC) interaction | Post-translational modification | RNA-binding protein | mRNA translation | Poly(A)-binding protein (PABP) | Post-transcriptional control | post-transcriptional control | METHYLATION | RECOGNITION | PHOSPHORYLATION | STABILITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | BINDING-PROTEIN | post-translational modification | MLLE DOMAIN | LYSINE ACETYLATION | TRANSLATION | poly(A)-binding-protein-interacting motif 2 (PAM2)-poly(A)-binding protein C-terminal domain (PABC) interaction | MESSENGER-RNA | STRUCTURAL BASIS | poly(A)-binding protein (PABP) | Humans | Protein Processing, Post-Translational - genetics | Cells, Cultured | Poly(A)-Binding Protein I - metabolism | Models, Molecular | Structure-Activity Relationship | Protein Methyltransferases - metabolism | Protein Processing, Post-Translational - physiology | Tissue Distribution | Animals | Protein Methyltransferases - physiology | Mice | HeLa Cells | Kinetics | Methylation | Poly(A)-Binding Protein I - genetics | Poly(A)-Binding Protein I - physiology | Arginine - metabolism | Poly(A)-Binding Protein I - chemistry | PTM, post-translational modification | MLLE, methionine-leucine-leucine-glutamate motif-containing domain | PABC, poly(A)-binding protein 1 C-terminal domain | DTT, dithiothrietol | eRF, eukaryotic release factor | PCNA, proliferating cell nuclear antigen | eRF3-N, N-terminal eRF3 | HRP, horseradish peroxidase | RRM, RNA recognition motif | TOB, transducer of ERBB2 | TSA, trichostatin A | GAPDH, glyceraldehyde-3-phosphate dehydrogenase | eIF, eukaryotic initiation factor | PRMT, protein arginine N-methyltransferase | poly(A)-binding-protein-interacting motif 2 (PAM2)–poly(A)binding protein C-terminal domain (PABC) interaction | AdOX, adenosine dialdehyde | G3BP, Ras GAP (GTPase-activating protein) SH3 (Src homology 3) domain-binding protein | MS, tandem MS | SG, stress granule | PAIP, poly(A)-interacting protein | miRNA, microRNA | PAN, poly(A) nuclease | eEF, eukaryotic elongation factor | MEF, mouse embryonic fibroblast | PAM, PABP-interacting motif | posttranscriptional control | PABP, poly(A)-binding protein | TD-NEM, transcription-dependent nuclear export motif
Journal Article
Science, ISSN 0036-8075, 5/2012, Volume 336, Issue 6081, pp. 593 - 597
The telomere end-protection problem is defined by the aggregate of DNA damage signaling and repair pathways that require repression at telomeres. To define the... 
Telomeres | Yeasts | Quantification | Lymphocytes | DNA | DNA damage | REPORTS | Cell cycle | Ataxia telangiectasia | Repression | Chromosomes | JOINING PATHWAY | POT1 PROTEINS | MAMMALIAN TELOMERES | SGS1 | MULTIDISCIPLINARY SCIENCES | DYSFUNCTIONAL TELOMERES | DOUBLE-STRAND BREAKS | HOMOLOGOUS RECOMBINATION | NHEJ | YEAST KU | Telomere - ultrastructure | Antigens, Nuclear - metabolism | Telomeric Repeat Binding Protein 1 - genetics | Telomeric Repeat Binding Protein 1 - metabolism | Homologous Recombination | DNA Breaks, Double-Stranded | DNA Ligases - metabolism | DNA-Binding Proteins - metabolism | Poly-ADP-Ribose Binding Proteins | Telomere-Binding Proteins - genetics | DNA End-Joining Repair | Telomere - metabolism | Telomere-Binding Proteins - metabolism | Protein-Serine-Threonine Kinases - metabolism | Tumor Suppressor Proteins - metabolism | Chromosomal Proteins, Non-Histone - metabolism | Signal Transduction | Cell Cycle Proteins - metabolism | Cells, Cultured | Ataxia Telangiectasia Mutated Proteins | Xenopus Proteins | DNA-Binding Proteins - genetics | Telomere Homeostasis | Mice, Knockout | Poly(ADP-ribose) Polymerases - metabolism | Animals | Antigens, Nuclear - genetics | Cell Cycle | Ku Autoantigen | DNA Repair | DNA Ligase ATP | Telomeric Repeat Binding Protein 2 - metabolism | Mice | Poly (ADP-Ribose) Polymerase-1 | Telomeric Repeat Binding Protein 2 - genetics | Tumor Suppressor p53-Binding Protein 1 | Proteins | Physiological aspects | Research | Health aspects | DNA repair | Telomerase
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2018, Volume 293, Issue 21, pp. 7942 - 7968
In aortic vascular smooth muscle (VSM), the canonical Wnt receptor LRP6 inhibits protein arginine (Arg) methylation, a new component of noncanonical Wnt... 
atherosclerosis | Type 2 diabetes | BONE BIOLOGY | cardiovascular disease | TRANSCRIPTION FACTOR RUNX2 | SINGLETON-MERTEN SYNDROME | CARDIOVASCULAR CALCIFICATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | INHIBITS VASCULAR CALCIFICATION | vascular biology | metabolic syndrome | DIABETES-MELLITUS | Wnt signaling | arteriosclerosis | protein methylation | ATHEROSCLEROTIC CALCIFICATION | IN-VIVO | calcification | ARGININE METHYLATION | vascular smooth muscle cells | CORONARY-ARTERY-DISEASE | Calcinosis - genetics | RNA Helicases - metabolism | Poly-ADP-Ribose Binding Proteins - metabolism | Calcium - metabolism | Humans | Myocytes, Smooth Muscle - pathology | Antiviral Agents - metabolism | Aorta - metabolism | Arteriosclerosis - genetics | Wnt Proteins - metabolism | Wnt Proteins - genetics | RNA Helicases - genetics | Calcinosis - metabolism | RNA Recognition Motif Proteins - metabolism | DNA Helicases - genetics | Myocytes, Smooth Muscle - metabolism | Low Density Lipoprotein Receptor-Related Protein-6 | Signal Transduction | Mice, Inbred C57BL | Cells, Cultured | Poly-ADP-Ribose Binding Proteins - genetics | beta Catenin - metabolism | beta Catenin - genetics | Mice, Knockout | Aorta - pathology | DNA Helicases - metabolism | Adaptor Proteins, Signal Transducing - physiology | Animals | Arteriosclerosis - metabolism | Mice | RNA Recognition Motif Proteins - genetics | Receptors, LDL - physiology | Calcinosis - pathology | Arteriosclerosis - pathology | Molecular Bases of Disease
Journal Article
Cell, ISSN 0092-8674, 03/2017, Volume 168, Issue 6, pp. 1028 - 1040.e19
In eukaryotic cells, diverse stresses trigger coalescence of RNA-binding proteins into stress granules. In vitro, stress-granule-associated proteins can demix... 
membraneless organelle | RNA-binding protein | poly(A)-binding protein | intrinsically disordered protein | quinary structure | stress granules | pH | heat shock | low-complexity region | energy depletion | HEAT-STRESS | MESSENGER-RNAS | TEMPERATURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | SEQUENCE | LIQUID DROPLETS | DISORDERED PROTEINS | TRANSITIONS | SACCHAROMYCES-CEREVISIAE | GRANULES | BINDING | CELL BIOLOGY | Amino Acid Sequence | Saccharomyces cerevisiae - physiology | Poly(A)-Binding Proteins - genetics | Proline - metabolism | Stress, Physiological | Hot Temperature | Saccharomyces cerevisiae Proteins - genetics | Cytoplasmic Granules - chemistry | Proline - analysis | Ribonucleases - metabolism | Saccharomyces cerevisiae - cytology | Sequence Alignment | Mutagenesis | Poly(A)-Binding Proteins - chemistry | Intrinsically Disordered Proteins - chemistry | Poly(A)-Binding Proteins - metabolism | Cytoplasmic Granules - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Hydrophobic and Hydrophilic Interactions | Protein Domains | Saccharomyces cerevisiae - growth & development | Hydrogen-Ion Concentration | Intrinsically Disordered Proteins - metabolism | Saccharomyces cerevisiae Proteins - chemistry | RNA | Physiological aspects | Stress (Physiology) | Sensors | Molecular biology | Binding proteins | Protein binding | Stress (Psychology) | BASIC BIOLOGICAL SCIENCES | 60 APPLIED LIFE SCIENCES | second messenger
Journal Article
PLoS Neglected Tropical Diseases, ISSN 1935-2727, 07/2018, Volume 12, Issue 7, p. e0006679
Poly(A)-binding proteins (PABPs) regulate mRNA fate by controlling stability and translation through interactions with both the poly(A) tail and eIF4F complex.... 
POLY(A) BINDING-PROTEIN | POSTTRANSCRIPTIONAL REGULATION | FUNCTIONALLY DISTINCT | ARABIDOPSIS-THALIANA | TRYPANOSOMA-BRUCEI | GENE-EXPRESSION | POLY(A)-BINDING PROTEINS | CAPPING ENZYME | TRANSLATION INITIATION | SPLICED LEADER RNA | PARASITOLOGY | TROPICAL MEDICINE | Trypanosoma brucei brucei - metabolism | RNA, Messenger - genetics | Poly(A)-Binding Protein I - metabolism | Poly(A)-Binding Protein II - genetics | Eukaryotic Initiation Factor-4E - metabolism | Trypanosoma brucei brucei - genetics | Protozoan Proteins - genetics | RNA, Messenger - metabolism | Trypanosoma brucei brucei - chemistry | Poly(A)-Binding Protein II - metabolism | Protozoan Proteins - metabolism | Poly(A)-Binding Protein II - chemistry | Proteomics | Protein Binding | Protozoan Proteins - chemistry | Poly(A)-Binding Protein I - genetics | Eukaryotic Initiation Factor-4E - genetics | Poly(A)-Binding Protein I - chemistry | Messenger RNA | Genetic aspects | Research | Binding proteins | Trypanosoma brucei | Genetic translation | Poly(A) | RNA | Protein purification | Identification | Proteins | Initiation factors | Poly(A)-binding protein | Life sciences | Polyribosomes | Localization | Water purification | Supervision | Binding | Stresses | Starvation | Translation | Stability | Developmental biology | Translation initiation | Cohorts | Mass spectroscopy | Nucleic acids | Ribonucleic acid--RNA | Gene expression | Stress | RNA-binding protein | Granular materials | Polyadenylation | Granules | Control stability | Interactions | Initiation factor eIF-4E | Mass spectrometry | Potassium | Initiation factor eIF-4G | mRNA stability | Ribonucleic acid
Journal Article