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Molecular Cell, ISSN 1097-2765, 10/2009, Volume 36, Issue 1, pp. 15 - 27
The multifunctional, stress-inducible molecular chaperone HSP70 has important roles in aiding protein folding and maintaining protein homeostasis. HSP70... 
PROTEINS | CHEMBIO | CELLCYCLE | CANCER-CELLS | HSP70 | CHAPERONE-MEDIATED AUTOPHAGY | NEGATIVE REGULATION | LYSOSOMAL MEMBRANE | BIOCHEMISTRY & MOLECULAR BIOLOGY | HEAT-SHOCK RESPONSE | APAF-1 APOPTOSOME | P53 PROTEINS | P62 | CELL-DEATH | CELL BIOLOGY | HSP70 Heat-Shock Proteins - antagonists & inhibitors | Microtubule-Associated Proteins - metabolism | Sequestosome-1 Protein | Humans | NF-kappa B - metabolism | Cathepsin L - metabolism | Autophagy - drug effects | DNA-Binding Proteins - metabolism | Caspases - metabolism | Lysosomes - metabolism | Protein Binding - drug effects | Lymphoma - pathology | Protein Interaction Domains and Motifs | Cell Death - drug effects | Lysosomes - drug effects | Cell Survival - drug effects | HSP40 Heat-Shock Proteins - metabolism | Tumor Suppressor Protein p53 - metabolism | Ubiquitin-Protein Ligases - metabolism | HSP70 Heat-Shock Proteins - genetics | Mice, Transgenic | Mice, Inbred Strains | Sulfonamides - pharmacology | Apoptotic Protease-Activating Factor 1 - metabolism | HSP70 Heat-Shock Proteins - metabolism | Transcription Factors - metabolism | Animals | Sulfonamides - therapeutic use | Lymphoma - prevention & control | Sulfonamides - metabolism | Cell Line, Tumor | Mice | Adaptor Proteins, Signal Transducing - metabolism | Protein Multimerization - drug effects | Protein Binding - physiology | Proteins | Heat shock proteins | Analysis | Tumors | Index Medicus
Journal Article
Nature, ISSN 0028-0836, 04/2010, Volume 464, Issue 7293, pp. 1357 - 1361
The inflammatory nature of atherosclerosis is well established but the agent(s) that incite inflammation in the artery wall remain largely unknown. Germ-free... 
ATHEROSCLEROTIC LESIONS | CELLS | MASSIVE XANTHOMATOSIS | ACAT INHIBITION | MULTIDISCIPLINARY SCIENCES | LOW-DENSITY-LIPOPROTEIN | HYPERLIPIDEMIC MICE | HYPERCHOLESTEROLEMIA | PROGRESSION | NALP3 INFLAMMASOME | APOLIPOPROTEIN-E | Inflammation - chemically induced | Inflammation - pathology | NLR Family, Pyrin Domain-Containing 3 Protein | Humans | Cathepsin L - metabolism | Phagocytes - pathology | Cytoskeletal Proteins - deficiency | Cholesterol - chemistry | Inflammation - metabolism | Time Factors | Bone Marrow Transplantation | Receptors, LDL - deficiency | Female | Lysosomes - pathology | Phagocytes - physiology | Lysosomes - drug effects | Atherosclerosis - pathology | Peritoneal Cavity - pathology | Phagocytes - drug effects | Atherosclerosis - chemically induced | Mice, Inbred C57BL | Crystallization | Cathepsin B - metabolism | Cholesterol - metabolism | Atherosclerosis - metabolism | Carrier Proteins - genetics | Diet, Atherogenic | Animals | Apoptosis Regulatory Proteins | Carrier Proteins - metabolism | CARD Signaling Adaptor Proteins | Cholesterol - pharmacology | Mice | Interleukin-1 - deficiency | Interleukin-18 - metabolism | Cellular proteins | Complications and side effects | Care and treatment | Hypercholesterolemia | Interleukins | Atherosclerosis | Research | Health aspects | Risk factors | Proteins | Gram-positive bacteria | Bone marrow | Medical research | Membranes | Index Medicus
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 01/2011, Volume 286, Issue 3, pp. 2155 - 2170
The first intron of FTO contains common single nucleotide polymorphisms associated with body weight and adiposity in humans. In an effort to identify the... 
RETINAL DEGENERATION | DNA-BINDING | ENERGY-EXPENDITURE | FTO GENE | CATHEPSIN-L | BIOCHEMISTRY & MOLECULAR BIOLOGY | BARDET-BIEDL-SYNDROME | TRANSCRIPTION FACTOR | GENOME-WIDE ASSOCIATION | PRIMARY CILIA | HOMEODOMAIN PROTEIN | Cathepsin L - genetics | Receptors, Leptin - genetics | Homeodomain Proteins - metabolism | Humans | Alpha-Ketoglutarate-Dependent Dioxygenase FTO | Cathepsin L - metabolism | Obesity - genetics | Mixed Function Oxygenases | Adipose Tissue - metabolism | Phosphorylation - genetics | Protein Isoforms - metabolism | Mice, Mutant Strains | Oxo-Acid-Lyases - genetics | Oxo-Acid-Lyases - metabolism | Nuclear Proteins - genetics | Repressor Proteins - metabolism | STAT3 Transcription Factor - metabolism | Introns - genetics | Response Elements | Signal Transduction | Gene Expression Regulation | Repressor Proteins - genetics | Retinitis Pigmentosa - genetics | Retinitis Pigmentosa - metabolism | Nuclear Proteins - metabolism | Adiposity - genetics | Homeodomain Proteins - genetics | Obesity - metabolism | Animals | Hypothalamus - metabolism | Adaptor Proteins, Signal Transducing - genetics | Alleles | Cell Line, Tumor | Mice | Receptors, Leptin - metabolism | Adaptor Proteins, Signal Transducing - metabolism | Protein Isoforms - genetics | Index Medicus | FTO | Obesity | Neuron | Mouse | CUX1 | Cilium | Leptin | Receptor Recycling | RPGRIP1L | Enzymology | Protease Inhibitor
Journal Article
Journal of Clinical Investigation, ISSN 0021-9738, 10/2011, Volume 121, Issue 10, pp. 3965 - 3980
Journal Article
Journal Article
Journal Article