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Nature Communications, ISSN 2041-1723, 12/2019, Volume 10, Issue 1, pp. 353 - 14
Mucosal melanoma is a rare and poorly characterized subtype of human melanoma. Here we perform a cross-species analysis by sequencing tumor-germline pairs from... 
POINT MUTATIONS | CANCER PATIENTS | BREAST-CANCER | MUTATIONAL PROCESSES | ARRAY-CGH | MULTIDISCIPLINARY SCIENCES | COPY NUMBER | TUMOR | OVARIAN-CANCER | MOUSE MODELS | REVEALS | Proto-Oncogene Proteins c-mdm2 - genetics | Cadherins - metabolism | Humans | Carcinogenesis - metabolism | DNA Copy Number Variations | Germ-Line Mutation | Cadherins - genetics | Neoplasm Proteins - genetics | Mouth Neoplasms - genetics | Protein-Serine-Threonine Kinases - metabolism | PTEN Phosphohydrolase - genetics | Tumor Suppressor Proteins - metabolism | Membrane Proteins - genetics | Carcinogenesis - genetics | Cell Cycle Proteins - metabolism | Melanoma - pathology | Mucous Membrane - pathology | GTP Phosphohydrolases - metabolism | GTP Phosphohydrolases - genetics | Microtubule-Associated Proteins - genetics | Species Specificity | Microtubule-Associated Proteins - metabolism | Gene Expression Regulation, Neoplastic | Mouth Neoplasms - metabolism | Receptor-Like Protein Tyrosine Phosphatases, Class 3 - genetics | Neoplasm Proteins - metabolism | Tumor Suppressor Protein p53 - genetics | Melanoma - genetics | BRCA1 Protein - metabolism | Tumor Suppressor Proteins - genetics | Cell Cycle Proteins - genetics | Membrane Proteins - metabolism | Proto-Oncogene Proteins c-mdm2 - metabolism | Melanoma - metabolism | Skin Neoplasms - pathology | Neoplasm Recurrence, Local | Protein-Serine-Threonine Kinases - genetics | Tumor Suppressor Protein p53 - metabolism | PTEN Phosphohydrolase - metabolism | Mucous Membrane - metabolism | Skin Neoplasms - metabolism | Carcinogenesis - pathology | BRCA1 Protein - genetics | Animals | BRCA2 Protein - metabolism | Receptor-Like Protein Tyrosine Phosphatases, Class 3 - metabolism | Skin Neoplasms - genetics | Dogs | Horses | Mouth Neoplasms - pathology | BRCA2 Protein - genetics | BRCA2 protein | MDM2 protein | BRCA1 protein | Copy number | p53 Protein | Mucosa | Melanoma | Data processing | Breast cancer | Metastases | Heterogeneity | Human performance | Tumorigenesis | Mutation | Comparative analysis | Species | PTEN protein | Tumors
Journal Article
Neuron, ISSN 0896-6273, 08/2012, Volume 75, Issue 4, pp. 618 - 632
Mitochondrial abnormalities have been documented in Alzheimer’s disease and related neurodegenerative disorders, but the causal relationship between... 
ALZHEIMERS-DISEASE BRAIN | DOMINANT OPTIC ATROPHY | MITOCHONDRIAL-FUNCTION | MOUSE MODEL | LIGHT-CHAIN | FRONTOTEMPORAL DEMENTIA | AXONAL-TRANSPORT | NEUROSCIENCES | DYNAMIN-RELATED PROTEIN | PHOSPHORYLATION SITES | TRANSGENIC MICE | Neurons - pathology | Microtubule-Associated Proteins - genetics | Tauopathies - genetics | Cytoskeletal Proteins - genetics | Gelsolin - metabolism | Microtubule-Associated Proteins - metabolism | Humans | Actins - metabolism | Tauopathies - pathology | Cytoplasm - metabolism | MicroRNAs - metabolism | Green Fluorescent Proteins - genetics | Mitochondrial Proteins - genetics | Drosophila Proteins - metabolism | GTP-Binding Proteins - genetics | Nerve Degeneration - metabolism | Neurons - ultrastructure | tau Proteins - genetics | Cell Death - genetics | Mitochondria - genetics | Mitochondrial Proteins - metabolism | ATP Synthetase Complexes - metabolism | Cell Cycle Proteins - genetics | Tauopathies - complications | Cytoskeletal Proteins - metabolism | Myosins - metabolism | Cytoplasm - genetics | RNA Interference - physiology | Disease Models, Animal | In Situ Nick-End Labeling | Green Fluorescent Proteins - metabolism | Animals, Genetically Modified | Gene Expression Regulation - genetics | Drosophila | Cell Cycle Proteins - metabolism | Mitochondria - metabolism | Mitochondria - pathology | Mutation - genetics | Animals | GTP Phosphohydrolases - metabolism | Analysis of Variance | GTP Phosphohydrolases - genetics | Gelsolin - genetics | Mice | Drosophila Proteins - genetics | Nerve Degeneration - etiology | Voltage-Dependent Anion Channels - metabolism | GTP-Binding Proteins - metabolism | Nervous system diseases | Actin | Neurons | Utrophin | Myosin | Mitochondrial DNA | Alzheimer's disease | Proteins | Phosphorylation | Mitochondria | Neurotoxicity | Insects | Microscopy | Neurodegeneration | Pathogenesis | Morphology | Mutation | Defects | Neurodegenerative diseases | Tau protein | Cell death | Elongation
Journal Article
Molecular Cell, ISSN 1097-2765, 09/2016, Volume 63, Issue 5, pp. 781 - 795
Mutations in the human autophagy gene EPG5 cause the multisystem disorder Vici syndrome. Here we demonstrated that EPG5 is a Rab7 effector that determines the... 
RAB effector | LC3 | autophagosome maturation | epg-5 | SNARE | MEMBRANE-FUSION | LYSOSOME FUSION | BIOCHEMISTRY & MOLECULAR BIOLOGY | MACHINERY | MECHANISMS | SYNTAXIN 17 | MATURATION | VESICLE | C. ELEGANS | HOPS COMPLEX | CELL BIOLOGY | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Humans | Cataract - pathology | Qb-SNARE Proteins - metabolism | R-SNARE Proteins - metabolism | Caenorhabditis elegans Proteins - metabolism | Qb-SNARE Proteins - genetics | rab GTP-Binding Proteins - genetics | Endosomes - metabolism | Lysosomes - metabolism | Qc-SNARE Proteins - metabolism | Agenesis of Corpus Callosum - genetics | Endosomes - ultrastructure | Qa-SNARE Proteins - genetics | Autophagy - genetics | Synaptosomal-Associated Protein 25 - genetics | rab GTP-Binding Proteins - metabolism | Agenesis of Corpus Callosum - metabolism | Amino Acid Sequence | Caenorhabditis elegans - metabolism | Membrane Fusion | Signal Transduction | Caenorhabditis elegans - genetics | R-SNARE Proteins - genetics | Gene Expression Regulation | Autophagosomes - metabolism | Cataract - metabolism | Agenesis of Corpus Callosum - pathology | Autophagosomes - ultrastructure | Lysosomes - ultrastructure | Proteins - genetics | Sequence Homology, Amino Acid | Sequence Alignment | Animals | Proteins - metabolism | Qa-SNARE Proteins - metabolism | Protein Binding | Qc-SNARE Proteins - genetics | Cataract - genetics | Synaptosomal-Associated Protein 25 - metabolism | HeLa Cells | Caenorhabditis elegans Proteins - genetics | Yuan (China)
Journal Article
The Journal of Cell Biology, ISSN 0021-9525, 2/2002, Volume 156, Issue 3, pp. 437 - 451
Disruption of the function of the A-type Aurora kinase of Drosophila by mutation or RNAi leads to a reduction in the length of astral microtubules in syncytial... 
Larvae | Auroras | Microtubules | Drosophila | Metaphase | Centrosomes | Antibodies | Embryos | Cells | Mitotic spindle apparatus | Microtubule | D-TACC | Mitosis | Aurora A | XENOPUS EGG EXTRACTS | PROTEIN | centrosomes | mitosis | HISTONE H3 PHOSPHORYLATION | CELL BIOLOGY | microtubule | ORGANIZATION | BIPOLAR MITOTIC SPINDLE | BINDS | INCENP | DYNAMICS | CHROMOSOME SEGREGATION | MELANOGASTER | Protein Kinases - metabolism | Protein Kinases - genetics | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Protein-Serine-Threonine Kinases | Adenosine Triphosphate - genetics | Male | Drosophila Proteins - metabolism | Mitosis - genetics | Recombinant Fusion Proteins - metabolism | RNA - genetics | Adenosine Triphosphate - metabolism | Spindle Apparatus - genetics | Drosophila - embryology | Female | Nuclear Proteins - genetics | Drosophila - genetics | RNA - metabolism | Nuclear Proteins - metabolism | Protein Structure, Tertiary - genetics | Aurora Kinases | Binding Sites - genetics | Xenopus Proteins | Mutation - genetics | Cell Compartmentation - physiology | Animals | Centrosome - enzymology | Microtubules - genetics | Microtubules - enzymology | Recombinant Fusion Proteins - genetics | Drosophila - metabolism | Drosophila Proteins - genetics | Cell Cycle Proteins | Spindle Apparatus - enzymology | Pregnancy proteins | Research | D-TACC protein | Aurora-A protein | XMAP215 protein | MSPS protein | RNA | Adenosine Triphosphate | Cellular Biology | Recombinant Fusion Proteins | Spindle Apparatus | Cell Compartmentation | Life Sciences | Binding Sites | Centrosome | Protein Structure, Tertiary | Drosophila Proteins | Microtubule-Associated Proteins | Nuclear Proteins | Protein Kinases | Mutation | Aurora A; D-TACC; mitosis; centrosomes; microtubule
Journal Article
Nature Genetics, ISSN 1061-4036, 07/2017, Volume 49, Issue 7, pp. 1148 - 1151
Through exome sequencing, we identified six individuals with biallelic loss-of-function mutations in TRIP13. All six developed Wilms tumor. Constitutional... 
Developmental Disabilities | M Phase Cell Cycle Checkpoints | Sertoli-Leydig Cell Tumor | Humans | Protein-Serine-Threonine Kinases | Child, Preschool | Aneuploidy | Neoplasms, Multiple Primary | Leukemia, Myeloid, Acute | Microcephaly | Journal Article | DNA, Neoplasm | Female | Ovarian Neoplasms | Carrier Proteins | Seizures | Kidney Neoplasms | ATPases Associated with Diverse Cellular Activities | Chromosome Segregation | Genetic Predisposition to Disease | Microtubule-Associated Proteins | RNA Stability | Nuclear Proteins | Mosaicism | Wilms Tumor | Mutation | Cell Cycle Proteins | CELLS | INSTABILITY | PROTEIN | GENETICS & HEREDITY | AAA-ATPASE | MITOTIC CHECKPOINT | MOSAIC VARIEGATED ANEUPLOIDY | Kidney Neoplasms - genetics | Microcephaly - genetics | Seizures - genetics | Microtubule-Associated Proteins - genetics | Wilms Tumor - genetics | M Phase Cell Cycle Checkpoints - genetics | Developmental Disabilities - genetics | Ovarian Neoplasms - genetics | Cell Cycle Proteins - genetics | Nuclear Proteins - genetics | Neoplasms, Multiple Primary - genetics | Sertoli-Leydig Cell Tumor - genetics | Protein-Serine-Threonine Kinases - genetics | RNA Stability - genetics | Carrier Proteins - genetics | DNA, Neoplasm - genetics | Chromosome Segregation - genetics | Leukemia, Myeloid, Acute - genetics | Sequences | Pipelines | Genes | Impairment | Cell division | Genomes | Carcinogenesis | Proteins | Carcinogens | Microencephaly | Chromosomes | Cancer | Tumors
Journal Article
PLoS ONE, ISSN 1932-6203, 04/2017, Volume 12, Issue 4, p. e0173676
Autophagy is a catabolic mechanism to degrade cellular components to maintain cellular energy levels during starvation, a condition where PPAR alpha may be... 
INSULIN SIGNALING TRANSDUCTION | GLUCOSE-HOMEOSTASIS | FIBROBLAST-GROWTH-FACTOR-21 | DEACETYLATION | METABOLISM | PATHWAY | STEATOSIS | MULTIDISCIPLINARY SCIENCES | RESISTANCE | RECEPTORS | FOXO1 | TOR Serine-Threonine Kinases - metabolism | Autophagy-Related Protein 7 - metabolism | Fibroblast Growth Factors - genetics | Autophagy-Related Protein 5 - genetics | fas Receptor - metabolism | Autophagy - drug effects | Fibroblast Growth Factors - metabolism | TOR Serine-Threonine Kinases - genetics | Liver - drug effects | fas Receptor - genetics | Autophagy - genetics | Proto-Oncogene Proteins c-akt - metabolism | Forkhead Box Protein O1 - metabolism | Signal Transduction | Liver - metabolism | PPAR alpha - genetics | Ubiquitin-Conjugating Enzymes - genetics | Stearoyl-CoA Desaturase - genetics | Mice, Knockout | Triglycerides - metabolism | Sequestosome-1 Protein - genetics | Ubiquitin-Conjugating Enzymes - metabolism | Cysteine Endopeptidases - genetics | Autophagy-Related Protein 5 - metabolism | Beclin-1 - genetics | Stearoyl-CoA Desaturase - metabolism | Mice | PPAR alpha - metabolism | Autophagy-Related Proteins - antagonists & inhibitors | Blood Glucose - metabolism | Autophagy-Related Proteins - metabolism | Forkhead Box Protein O1 - genetics | Autophagy-Related Protein 5 - antagonists & inhibitors | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Proto-Oncogene Proteins c-akt - genetics | Fenofibrate - pharmacology | Cysteine Endopeptidases - metabolism | Autophagy-Related Proteins - genetics | Sequestosome-1 Protein - metabolism | Sterol Regulatory Element Binding Protein 1 - metabolism | Autophagy-Related Protein 7 - antagonists & inhibitors | Mice, Inbred C57BL | Autophagy-Related Protein 7 - genetics | Gene Expression Regulation - drug effects | Animals | Sterol Regulatory Element Binding Protein 1 - genetics | PPAR alpha - agonists | Ubiquitin-Conjugating Enzymes - antagonists & inhibitors | Beclin-1 - metabolism | Transcription factors | Adipose tissue | Liver | Body weight | AKT protein | Biochemistry | Glucose | Assaying | Proteins | Signal transduction | Temperature effects | Fibroblasts | Physiology | Acetylation | Inhibition | Growth factors | Hepatotoxicity | Activation analysis | Methanol | Starvation | Ethanol | AMP | Metabolism | Insulin | Fatty acids | Studies | Acetaminophen | Food intake | Weight reduction | Animal welfare | Circulation | Drugs | Biotechnology | Drug abuse | Laboratories | Centrifugation | Glass | Homeostasis | Activation | Biology | Kinases | AMP-activated protein kinase | Autophagy | Nutrient status | Rodents | Nutrients | Oxidation | Heart diseases | Age | Epinephrine | AKT1 protein | Fasting | Chloroform | Diabetes mellitus | Cardiomyocytes | Acclimatization | Triglycerides | Pharmacology | Nitrogen | Calories | Medicine | Nuclear fuels | Protein kinase | Insulin resistance | Diabetes
Journal Article
Biogerontology, ISSN 1389-5729, 06/2013, Volume 14, Issue 3, pp. 303 - 23
During ageing skeletal muscles undergo a process of structural and functional remodelling that leads to sarcopenia, a syndrome characterized by loss of muscle... 
Forkhead Transcription Factors/physiology | Serpin E2/genetics | Humans | Male | Microtubule-Associated Proteins/genetics | Signal Transduction/physiology | Tripartite Motif Proteins | Young Adult | Aging/physiology | TOR Serine-Threonine Kinases/physiology | Aged, 80 and over | Adult | Female | Mice, Inbred DBA | Models, Animal | Insulin-Like Growth Factor I/physiology | Muscle Proteins/genetics | Mice, Inbred C57BL | Proto-Oncogene Proteins c-akt/physiology | Mice, Transgenic | SKP Cullin F-Box Protein Ligases/genetics | Mice, Knockout | Autophagy-Related Protein 7 | Animals | Sarcopenia/physiopathology | Adolescent | Aged | Forkhead Box Protein O1 | Mice | Muscle, Skeletal/physiology | Ubiquitin-Protein Ligases/genetics | Life Sciences | Sarcopenia | FoxO | Geriatrics/Gerontology | Ageing | mTOR | IGF1 | Akt | Developmental Biology | Cell Biology | LIFE-SPAN | IGF-I | ALPHA-V-BETA-3 INTEGRIN | PLASMINOGEN-ACTIVATOR INHIBITOR-1 | GERIATRICS & GERONTOLOGY | GROWTH-HORMONE | MESSENGER-RNA | GENETIC-DETERMINANTS | FAST-TWITCH | CELL-CYCLE | S6 KINASE | Microtubule-Associated Proteins - genetics | SKP Cullin F-Box Protein Ligases - genetics | SKP Cullin F-Box Protein Ligases - physiology | Forkhead Transcription Factors - physiology | Ubiquitin-Protein Ligases - physiology | TOR Serine-Threonine Kinases - physiology | Muscle Proteins - physiology | Serpin E2 - physiology | Proto-Oncogene Proteins c-akt - physiology | Muscle, Skeletal - physiology | Microtubule-Associated Proteins - physiology | Muscle Proteins - genetics | Sarcopenia - physiopathology | Serpin E2 - genetics | Aging - physiology | Insulin-Like Growth Factor I - physiology | Signal Transduction - physiology | Ubiquitin-Protein Ligases - genetics | Ubiquitin | Muscles | Ligases | Proteolysis | Analysis | SKP Cullin F-Box Protein Ligases | Muscle Proteins | Aging | Serpin E2 | Signal Transduction | Biochemistry, Molecular Biology | Microtubule-Associated Proteins | Insulin-Like Growth Factor I | Proto-Oncogene Proteins c-akt | Ubiquitin-Protein Ligases | TOR Serine-Threonine Kinases | Muscle, Skeletal | Forkhead Transcription Factors | Clinical Medicine | Neurology | Neurologi | Medical and Health Sciences | Medicin och hälsovetenskap | Clinical Neurophysiology | Klinisk neurofysiologi | Klinisk medicin
Journal Article
Nature Neuroscience, ISSN 1097-6256, 05/2010, Volume 13, Issue 5, pp. 551 - 558
Brain structure and size require precise division of neural stem cells (NSCs), which self-renew and generate intermediate neural progenitors (INPs) and... 
HUMAN-CHROMOSOMES | PROTEIN | LIS1 EXPRESSION | LISSENCEPHALY GENE | SECKEL-SYNDROME | NASHI | SPINDLE ORIENTATION | NEUROGENESIS | NEUROSCIENCES | MESSENGER-RNA LOCALIZATION | CEREBRAL CORTICAL SIZE | Brain - embryology | Microcephaly - genetics | Embryo, Mammalian | Homeodomain Proteins - metabolism | Humans | Apoptosis - genetics | Green Fluorescent Proteins - genetics | RNA, Messenger - metabolism | Neurogenesis - genetics | DNA Mutational Analysis | Organ Size - genetics | Repressor Proteins - metabolism | Animals, Newborn | Oligonucleotide Array Sequence Analysis - methods | Repressor Proteins - genetics | Genotype | Mice, Transgenic | In Situ Nick-End Labeling - methods | Mutation - genetics | T-Box Domain Proteins - metabolism | Eye Proteins - metabolism | Brain - pathology | Mice | HeLa Cells | Paired Box Transcription Factors - genetics | Neurons - pathology | Age Factors | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Gene Expression Regulation, Developmental - genetics | Brain - growth & development | Cell Differentiation - genetics | 1-Alkyl-2-acetylglycerophosphocholine Esterase - genetics | Transfection | Microcephaly - pathology | Microcephaly - physiopathology | Bromodeoxyuridine - metabolism | Eye Proteins - genetics | Nuclear Proteins - genetics | RNA Interference - physiology | Cell Division - genetics | Mice, Inbred C57BL | Gene Expression Profiling - methods | Nuclear Proteins - metabolism | PAX6 Transcription Factor | Nerve Tissue Proteins - genetics | T-Box Domain Proteins - genetics | Homeodomain Proteins - genetics | Nerve Tissue Proteins - metabolism | 1-Alkyl-2-acetylglycerophosphocholine Esterase - metabolism | Animals | Stem Cells - physiology | Paired Box Transcription Factors - metabolism | Animal experimentation | Axons | Usage | Brain research | Cell division | Physiological aspects | Causes of | Research | Microcephaly | Mental retardation | Risk factors
Journal Article
Science, ISSN 0036-8075, 12/2001, Volume 294, Issue 5550, pp. 2364 - 2368
In Saccharomyces cerevisiae, more than 80% of the ∼6200 predicted genes are nonessential, implying that the genome is buffered from the phenotypic consequences... 
Yeasts | Microbial genetics | Cell growth | Diploidy | Molecular genetics | Cell walls | DNA | Actins | Reports | Genetic mutation | Genetic screening | MORPHOGENESIS | SCREEN | BUDDING YEAST | SYNTHETIC LETHAL | MULTIDISCIPLINARY SCIENCES | ACTIN CYTOSKELETON | MUTATIONS | SACCHAROMYCES-CEREVISIAE | Cytoskeletal Proteins | Cell Polarity | Mitosis | Saccharomyces cerevisiae - genetics | Microtubule Proteins - physiology | Databases, Genetic | Endodeoxyribonucleases - physiology | Robotics | DNA, Fungal - biosynthesis | Genome, Fungal | RecQ Helicases | Recombination, Genetic | Gene Deletion | Cell Cycle Proteins - genetics | Microtubule Proteins - genetics | DNA Helicases - genetics | Genes, Fungal - physiology | Carrier Proteins - physiology | Saccharomyces cerevisiae - physiology | Computational Biology | Fungal Proteins - genetics | Genetic Markers | Saccharomyces cerevisiae Proteins - genetics | Genetic Techniques | Genes, Essential | Carrier Proteins - genetics | Endodeoxyribonucleases - genetics | Fungal Proteins - physiology | Microfilament Proteins | DNA Repair | Flap Endonucleases | Cytoskeleton - physiology | Saccharomyces cerevisiae Proteins - physiology | Cell Cycle Proteins - physiology | Saccharomyces cerevisiae - growth & development | Crosses, Genetic | DNA Helicases - physiology | Yeast | Gene mutations | Analysis | Genetic research | Genetic aspects | Research | Genetics | Mutation
Journal Article
Biochemical Journal, ISSN 0264-6021, 02/2017, Volume 474, Issue 4, pp. 597 - 609
Cyclic AMP (cAMP)-specific phosphodiesterase-4 (PDE4) enzymes underpin compartmentalised cAMP signalling by localising to distinct signalling complexes. PDE4... 
CELLS | SIGNALING PATHWAYS | ACTIVATION | CAMP-SPECIFIC PHOSPHODIESTERASE | PROTEIN-KINASE | MAP KINASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | A-MEDIATED PHOSPHORYLATION | BETA-ARRESTIN | BINDING-SITES | ROLIPRAM INHIBITION | Humans | Cyclic AMP-Dependent Protein Kinases - chemistry | Intracellular Signaling Peptides and Proteins - metabolism | Cyclic AMP-Dependent Protein Kinases - genetics | Mitogen-Activated Protein Kinase 1 - genetics | Cyclic Nucleotide Phosphodiesterases, Type 4 - metabolism | Cyclic Nucleotide Phosphodiesterases, Type 4 - chemistry | Intracellular Signaling Peptides and Proteins - genetics | 1-Alkyl-2-acetylglycerophosphocholine Esterase - chemistry | Protein-Serine-Threonine Kinases - metabolism | Gene Expression | Mitogen-Activated Protein Kinase 3 - genetics | Signal Transduction | Recombinant Proteins - chemistry | Ubiquitin-Conjugating Enzymes - genetics | Cyclic Nucleotide Phosphodiesterases, Type 4 - genetics | Mitogen-Activated Protein Kinase 3 - metabolism | Ubiquitin-Conjugating Enzymes - metabolism | Molecular Docking Simulation | Protein-Serine-Threonine Kinases - chemistry | src-Family Kinases - genetics | COS Cells | Mitogen-Activated Protein Kinase 1 - metabolism | Microtubule-Associated Proteins - chemistry | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | beta-Arrestins - metabolism | Cercopithecus aethiops | Ubiquitin-Conjugating Enzymes - chemistry | Mitogen-Activated Protein Kinase 1 - chemistry | 1-Alkyl-2-acetylglycerophosphocholine Esterase - genetics | HEK293 Cells | src-Family Kinases - metabolism | Protein Interaction Domains and Motifs | Mitogen-Activated Protein Kinase 3 - chemistry | beta-Arrestins - chemistry | Cyclic AMP-Dependent Protein Kinases - metabolism | Recombinant Proteins - metabolism | Catalytic Domain | Protein Structure, Secondary | Protein-Serine-Threonine Kinases - genetics | Recombinant Proteins - genetics | Amino Acid Motifs | 1-Alkyl-2-acetylglycerophosphocholine Esterase - metabolism | beta-Arrestins - genetics | Animals | Intracellular Signaling Peptides and Proteins - chemistry | Protein Binding | src-Family Kinases - chemistry | protein–protein interactions | cAMP | cyclic nucleotide phosphodiesterases
Journal Article