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American Journal of Physiology - Endocrinology and Metabolism, ISSN 0193-1849, 2016, Volume 311, Issue 5, pp. E836 - E849
Alcohol ingestion decreases postexercise rates of muscle protein synthesis, but the mechanism( s) (e.g., increased protein breakdown) underlying this... 
Alcohol | Exercise | Autophagy | Protein | Apoptosis | alcohol | ACTIVATION | PHYSIOLOGY | autophagy | MITOCHONDRIAL BIOGENESIS | INCREASES | exercise | apoptosis | HUMAN SKELETAL-MUSCLE | MTOR | CELL-DEATH | DIRECT PHOSPHORYLATION | P53 | MESSENGER-RNA | RESISTANCE EXERCISE | protein | ENDOCRINOLOGY & METABOLISM | Molecular Chaperones - metabolism | Apoptosis - drug effects | Humans | Male | Autophagy - physiology | Alcohol Drinking | Carrier Proteins - drug effects | Autophagy - drug effects | Electron Transport Complex IV - metabolism | Transcription Factors - drug effects | Central Nervous System Depressants - pharmacology | Mitochondrial Proteins - drug effects | Young Adult | Organelle Biogenesis | Mitochondrial Proteins - metabolism | Dietary Proteins - pharmacology | Nuclear Respiratory Factor 1 - metabolism | Mitochondrial Proton-Translocating ATPases - drug effects | Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha - drug effects | Voltage-Dependent Anion Channel 1 - drug effects | Mitochondrial Degradation - physiology | Mitochondrial Proton-Translocating ATPases - metabolism | Cross-Over Studies | Signal Transduction - drug effects | Mitochondrial Degradation - drug effects | Adolescent | Electron Transport Complex IV - drug effects | Membrane Proteins - drug effects | Exercise - physiology | RNA-Binding Proteins - metabolism | Protein Kinases - metabolism | Muscle Fibers, Skeletal - drug effects | Healthy Volunteers | DNA-Binding Proteins - metabolism | Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha - metabolism | Adult | Molecular Chaperones - drug effects | Membrane Proteins - metabolism | DNA Fragmentation - drug effects | Muscle Fibers, Skeletal - physiology | Proto-Oncogene Proteins - metabolism | Protein Kinases - drug effects | Proto-Oncogene Proteins - drug effects | Dietary Carbohydrates - pharmacology | DNA-Binding Proteins - drug effects | Tumor Suppressor Protein p53 - metabolism | Voltage-Dependent Anion Channel 1 - metabolism | Tumor Suppressor Protein p53 - drug effects | Nuclear Respiratory Factor 1 - drug effects | RNA-Binding Proteins - drug effects | Transcription Factors - metabolism | Basic Helix-Loop-Helix Leucine Zipper Transcription Factors - drug effects | Ethanol - pharmacology | Carrier Proteins - metabolism | Basic Helix-Loop-Helix Leucine Zipper Transcription Factors - metabolism | Apoptosis - physiology | Autophagy (Cytology) | Cell research | Alcoholic beverages | Physiological aspects | Cellular signal transduction | Research
Journal Article
Nature Medicine, ISSN 1078-8956, 07/2016, Volume 22, Issue 7, pp. 800 - 806
Type 2 diabetes (T2D) is among the most common and costly disorders worldwide(1). The goal of current medical management for T2D is to transiently ameliorate... 
MEDICINE, RESEARCH & EXPERIMENTAL | HOMEOSTASIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | MODEL | SUPPRESSION | ASTROCYTES | BALANCE | CELL BIOLOGY | INSULIN | TANYCYTES | METABOLISM | INTRAVENOUS GLUCOSE-TOLERANCE | IN-VIVO | Body Composition | Ependymoglial Cells - metabolism | Injections, Intraventricular | Male | Muscle, Skeletal - metabolism | Diabetes Mellitus, Type 2 - metabolism | Neoplasm Proteins - metabolism | Deoxyglucose | Neoplasm Proteins - drug effects | Brain - metabolism | Adipose Tissue - metabolism | Receptor, Insulin - genetics | Diet, High-Fat | Muscle, Skeletal - drug effects | Myocardium - metabolism | Hypothalamus - drug effects | Diabetes Mellitus, Experimental - metabolism | Real-Time Polymerase Chain Reaction | Disease Models, Animal | Glucose Tolerance Test | Heat-Shock Proteins - drug effects | Heat-Shock Proteins - metabolism | Liver - metabolism | Proto-Oncogene Proteins c-fos - metabolism | Rats | Ependymoglial Cells - drug effects | Receptor, Insulin - antagonists & inhibitors | Remission Induction | Blotting, Western | Proto-Oncogene Proteins c-fos - drug effects | Mice, Knockout | Blood Glucose - drug effects | Brain - drug effects | Hyperglycemia - metabolism | Rats, Zucker | Animals | Hypothalamus - metabolism | Hypothalamus - cytology | Fibroblast Growth Factor 1 - pharmacology | Heart - drug effects | Mice, Obese | Mice | Blood Glucose - metabolism | Adipose Tissue - drug effects | Forkhead Box Protein O1 - genetics | Carbon Radioisotopes | Type 2 diabetes | Molecular targeted therapy | Care and treatment | Innovations | Development and progression | Genetic aspects | Fibroblast growth factors | Health aspects | Fibroblasts | Diabetes | Drug therapy | Rodents | brain | diabetes | fibroblast growth factor
Journal Article
Diabetes, ISSN 0012-1797, 10/2010, Volume 59, Issue 10, pp. 2426 - 2434
OBJECTIVE Branched-chain amino acids, such as leucine and glucose, stimulate protein synthesis and increase the phosphorylation and activity of the mammalian... 
MAMMALIAN TARGET | ENERGY | AMINO-ACID METABOLISM | MALONYL-COA | ENDOCRINOLOGY & METABOLISM | STARVATION | ACETYL-COA CARBOXYLASE | VEIN ENDOTHELIAL-CELLS | KINASE ACTIVATION | SIRT1 | EXERCISE | AMP-Activated Protein Kinases - metabolism | Leucine - pharmacology | Phosphoproteins - drug effects | Phosphorylation | Intracellular Signaling Peptides and Proteins - drug effects | Intracellular Signaling Peptides and Proteins - metabolism | Ribosomal Protein S6 Kinases, 70-kDa - drug effects | Carrier Proteins - drug effects | Phosphoproteins - metabolism | Dose-Response Relationship, Drug | Insulin Resistance - physiology | Adenylate Kinase - metabolism | Muscle, Skeletal - drug effects | Aminoimidazole Carboxamide - metabolism | Protein-Serine-Threonine Kinases - metabolism | Pyruvates - metabolism | Muscle, Skeletal - enzymology | Ribonucleotides - metabolism | Ribosomal Protein S6 Kinases, 70-kDa - metabolism | Rats | Glucose - pharmacology | Down-Regulation - drug effects | Animals | Carrier Proteins - metabolism | Lactates - metabolism | Aminoimidazole Carboxamide - analogs & derivatives | Protein-Serine-Threonine Kinases - drug effects | TOR Serine-Threonine Kinases | Kinetics | Branched chain amino acids | Analysis | Physiological aspects | Insulin resistance | Protein biosynthesis | Research | Diabetes | Protein kinases | Metabolism
Journal Article
American Journal of Physiology - Endocrinology and Metabolism, ISSN 0193-1849, 2017, Volume 312, Issue 1, pp. E27 - E36
Citrulline (CIT) is an endogenous amino acid produced by the intestine. Recent literature has consistently shown CIT to be an activator of muscle protein... 
Protein synthesis | Mammalian target of rapamycin | Mitogen-activated protein kinase | Amino acids | Muscle | Myotube | Phosphatidylinositol 3-kinase | Eukaryotic initiation factor 4E-binding protein 1 | CELLS | PHYSIOLOGY | NITROGEN HOMEOSTASIS | amino acids | RATS | protein synthesis | eukaryotic initiation factor 4E-binding protein 1 | IMPAIRMENT | mitogen-activated protein kinase | CROSS-TALK | SUPPLEMENTATION | SKELETAL-MUSCLE | mammalian target of rapamycin | myotube | METABOLISM | AMINO-ACIDS | muscle | ENDOCRINOLOGY & METABOLISM | LEUCINE | phosphatidylinositol 3-kinase | Phosphoproteins - drug effects | TOR Serine-Threonine Kinases - metabolism | Citrulline - metabolism | Malnutrition - metabolism | Male | Muscle, Skeletal - metabolism | Phosphatidylinositol 3-Kinases - metabolism | Muscle Fibers, Skeletal - drug effects | Muscle Fibers, Skeletal - metabolism | Carrier Proteins - drug effects | Phosphoproteins - metabolism | Mechanistic Target of Rapamycin Complex 1 | Muscle Proteins - biosynthesis | Multiprotein Complexes - metabolism | Muscle, Skeletal - drug effects | Phosphatidylinositol 3-Kinases - drug effects | Flavonoids - pharmacology | Chromones - pharmacology | Proto-Oncogene Proteins c-akt - metabolism | TOR Serine-Threonine Kinases - drug effects | Multiprotein Complexes - drug effects | Signal Transduction | Enzyme Inhibitors - pharmacology | Morpholines - pharmacology | Rats | Muscle Proteins - drug effects | Rats, Sprague-Dawley | Sirolimus - pharmacology | Animals | Carrier Proteins - metabolism | Citrulline - pharmacology | Androstadienes - pharmacology | Protein Kinase Inhibitors - pharmacology | In Vitro Techniques | Mitogen-Activated Protein Kinases - drug effects | Mitogen-Activated Protein Kinases - metabolism | Proto-Oncogene Proteins c-akt - drug effects | Physiological aspects | Protein research | Protein biosynthesis | Citrulline | Research | Life Sciences | Human health and pathology | Endocrinology and metabolism
Journal Article
STEM CELLS, ISSN 1066-5099, 03/2010, Volume 28, Issue 3, pp. 564 - 572
Human mesenchymal stem cells (hMSCs) are multipotent cells that can differentiate into many cell types. Chondrogenesis is induced in hMSCs cultured as a... 
N‐cadherin | Cell shape | Rac1 | Chondrogenesis | Smooth muscle cells | Mesenchymal stem cells | N-cadherin | MYOBLAST FUSION | CELL & TISSUE ENGINEERING | CELL BIOLOGY | ADHESION | ONCOLOGY | MESENCHYMAL PROGENITOR CELLS | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | GENE-EXPRESSION | CYTOSKELETAL TENSION | DIFFERENTIATION | RHO-GTPASES | PROTEINS | HEMATOLOGY | MODULATION | MAMMARY EPITHELIAL-CELLS | Chondrocytes - cytology | Chondrogenesis - drug effects | Cadherins - metabolism | Humans | Extracellular Matrix - metabolism | Antigens, CD - genetics | Cell Lineage - drug effects | Transforming Growth Factor beta3 - metabolism | Antigens, CD - metabolism | Cell Differentiation - genetics | Chondrocytes - drug effects | Mesenchymal Stromal Cells - cytology | Cadherins - genetics | Myocytes, Smooth Muscle - drug effects | Myocytes, Smooth Muscle - cytology | Myocytes, Smooth Muscle - metabolism | Chondrocytes - metabolism | Transforming Growth Factor beta3 - pharmacology | Mesenchymal Stromal Cells - drug effects | Cell Adhesion - genetics | Muscle Development - physiology | Cells, Cultured | Gene Expression Regulation - physiology | Mesenchymal Stromal Cells - metabolism | Up-Regulation - genetics | Antigens, CD - drug effects | Cadherins - drug effects | Cell Adhesion - drug effects | Cell Lineage - physiology | Cell Shape - drug effects | Gene Expression Regulation - drug effects | Up-Regulation - drug effects | Chondrogenesis - physiology | Muscle Development - drug effects | rac1 GTP-Binding Protein - drug effects | Cell Differentiation - drug effects | Cell Shape - physiology | rac1 GTP-Binding Protein - metabolism | rac1 GTP-Binding Protein - genetics
Journal Article
Nature Medicine, ISSN 1078-8956, 02/2016, Volume 22, Issue 2, pp. 154 - 162
Although the lung can undergo self-repair after injury, fibrosis in chronically injured or diseased lungs can occur at the expense of regeneration. Here we... 
MEDICINE, RESEARCH & EXPERIMENTAL | STEM-CELLS | ANGIOGENESIS | MACROPHAGE REGULATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | NOTCH | SIGNALING PROMOTES | CELL BIOLOGY | TO-MESENCHYMAL TRANSITION | ENDOTHELIAL-CELLS | DISEASE | SMOOTH-MUSCLE-CELLS | DIFFERENTIATION | Antibiotics, Antineoplastic - toxicity | Receptors, Notch - metabolism | Humans | Calcium-Binding Proteins - antagonists & inhibitors | Capillaries - drug effects | Hydrochloric Acid - toxicity | Smad3 Protein - metabolism | Pulmonary Circulation - physiology | Intercellular Signaling Peptides and Proteins - metabolism | Pulmonary Artery - metabolism | Receptors, CXCR - metabolism | Serrate-Jagged Proteins | Lung Injury - metabolism | Lung - metabolism | Membrane Proteins - metabolism | Pulmonary Fibrosis - metabolism | Capillaries - metabolism | Endothelial Cells - physiology | Wnt Signaling Pathway | Bleomycin - toxicity | Fibroblasts - metabolism | Jagged-1 Protein | Calcium-Binding Proteins - metabolism | Lung - pathology | Endothelial Cells - metabolism | RNA, Small Interfering - pharmacology | Vascular Endothelial Growth Factor Receptor-1 - metabolism | Pulmonary Artery - drug effects | Lung - physiology | Regeneration - physiology | Macrophages - metabolism | Regeneration - drug effects | Animals | Membrane Proteins - antagonists & inhibitors | Smad3 Protein - drug effects | Fibroblasts - drug effects | Lung - drug effects | Fibrosis | Fluorescent Antibody Technique | Macrophages - drug effects | Mice | Pulmonary Circulation - drug effects | Oligopeptides - pharmacology | Receptors, CXCR - agonists | Endothelial Cells - drug effects | Physiological aspects | Regeneration (Biology) | Lung diseases | Blood vessels | Angiogenesis | Pulmonary fibrosis | Cellular biology
Journal Article
Journal Article
Nature Medicine, ISSN 1078-8956, 10/2016, Volume 22, Issue 10, pp. 1120 - 1130
Cachexia represents a fatal energy-wasting syndrome in a large number of patients with cancer that mostly results in a pathological loss of skeletal muscle and... 
MEDICINE, RESEARCH & EXPERIMENTAL | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | PANCREATIC-CANCER | CELL-DEATH | CELL BIOLOGY | WHOLE-BODY LIPOLYSIS | OBESITY | ADIPOCYTE LIPOLYSIS | METABOLISM | ENERGY HOMEOSTASIS | AICAR | LIPID HOMEOSTASIS | Neoplasms - metabolism | Uncoupling Protein 1 - drug effects | AMP-Activated Protein Kinases - metabolism | Lipolysis - drug effects | AMP-Activated Protein Kinases - pharmacology | Uncoupling Protein 1 - metabolism | Cells, Cultured | Adipose Tissue, White - metabolism | Peptide Fragments - pharmacology | Apoptosis Regulatory Proteins - drug effects | Apoptosis Regulatory Proteins - metabolism | Neoplasms - complications | Adipocytes, White - drug effects | Animals | Lipogenesis - drug effects | Cachexia - etiology | Lipid Metabolism - drug effects | Mice | Thermogenesis - drug effects | In Vitro Techniques | Cachexia - metabolism | Adipocytes, White - metabolism | Adipose Tissue, White - drug effects | Adipose tissues | Peptides | Cachexia | Genetic aspects | Research | Protein kinases | Health aspects | Type 2 diabetes | Muscles | Cancer | Phosphates | Adipose tissue | Deactivation | Preservation | AMP | Homeostasis | Adipocytes | Shielding | Kinases | Inactivation | AMP-activated protein kinase | Skeletal muscle | Proteins | Thermogenesis | Energy | Uncoupling protein 1 | Tumors | Biological Sciences | Basic Medicine | Medical and Health Sciences | Medicin och hälsovetenskap | Medicinsk bioteknologi | Cell and Molecular Biology | Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy) | Medicinsk bioteknologi (med inriktning mot cellbiologi (inklusive stamcellsbiologi), molekylärbiologi, mikrobiologi, biokemi eller biofarmaci) | Medical Biotechnology | Naturvetenskap | Biologiska vetenskaper | Medicinska och farmaceutiska grundvetenskaper | Natural Sciences | Cell- och molekylärbiologi
Journal Article
American Journal of Physiology - Heart and Circulatory Physiology, ISSN 0363-6135, 2015, Volume 309, Issue 10, pp. H1720 - H1730
S-glutathionylation of cardiac myosin-binding protein C (cMyBP-C) induces Ca2+ sensitization and a slowing of cross-bridge kinetics as a result of increased... 
Oxidative stress | Diastolic dysfunction | Cardiac myosin-binding protein C | S-glutathionylation | Sarcomeres | BINDING-PROTEIN-C | MYOFILAMENT RESPONSE | CARDIAC & CARDIOVASCULAR SYSTEMS | PHYSIOLOGY | sarcomeres | TROPONIN-I | CA2 | RECOMMENDATIONS | cardiac myosin-binding protein C | CARDIAC-HYPERTROPHY | MUTATION | diastolic dysfunction | PERIPHERAL VASCULAR DISEASE | ECHOCARDIOGRAPHY | oxidative stress | ALPHA-TROPOMYOSIN | Free Radical Scavengers - pharmacology | Tropomyosin - genetics | Calcium - metabolism | Cardiomyopathy, Hypertrophic, Familial - genetics | Calcium-Binding Proteins - drug effects | Male | Mitogen-Activated Protein Kinase 1 - drug effects | Carrier Proteins - drug effects | Sarcoplasmic Reticulum Calcium-Transporting ATPases - drug effects | Mitogen-Activated Protein Kinase 3 - drug effects | Female | Diastole - drug effects | Phosphorylation - drug effects | Disease Models, Animal | Calcium-Binding Proteins - metabolism | Cardiomyopathy, Hypertrophic, Familial - physiopathology | Myofibrils - drug effects | Sarcoplasmic Reticulum Calcium-Transporting ATPases - metabolism | Cardiomyopathy, Hypertrophic, Familial - metabolism | Mice, Transgenic | Animals | Carrier Proteins - metabolism | Heart Ventricles - physiopathology | Mitogen-Activated Protein Kinase 3 - metabolism | Acetylcysteine - pharmacology | Heart Ventricles - metabolism | Mice | Myofibrils - metabolism | Oxidative Stress - drug effects | Heart Ventricles - drug effects | Mitogen-Activated Protein Kinase 1 - metabolism | Complications and side effects | Care and treatment | Usage | Cardiomyopathy, Hypertrophic | Analysis | Acetylcysteine | Protein C | Influence | Genetic aspects | Genetic engineering | Research | Hypertrophy | Muscle Mechanics and Ventricular Function
Journal Article
Journal of the American Society of Nephrology, ISSN 1046-6673, 09/2013, Volume 24, Issue 9, pp. 1387 - 1398
Journal Article