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The book highlights work from many different labs that taught us abnormal HDACs potentially contribute to the development or progression of many human diseases including immune dysfunctions, heart disease, cancer, memory impairment, aging, and metabolic disorders.

Chemical structure --- Organic spectroscopy --- General biochemistry --- Human biochemistry --- Pharmacology. Therapy --- Semiology. Diagnosis. Symptomatology --- biosynthese --- massaspectrometrie --- klinische chemie --- medische biochemie --- polypeptiden --- medische laboratoriumtechnologie --- protein-engineering --- farmacologie --- biochemie --- toxicologie --- genetische manipulatie --- eiwitten --- moleculaire biologie --- aminozuren --- Histone Deacetylases --- Histone Deacetylase Inhibitors. --- Neoplasms --- Sirtuins --- Histone deacetylase. --- Histone désacétylase --- physiology. --- drug therapy. --- EPUB-LIV-FT LIVBIOLO LIVBIOMO LIVMEDEC SPRINGER-B

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The mechanistic/mammalian target of rapamycin (mTOR), a serine/threonine kinase, is a central regulator for human physiological activity. Deregulated mTOR signaling is implicated in a variety of disorders, such as cancer, obesity, diabetes, and neurodegenerative diseases. The papers published in this Special Issue summarize the current understanding of the mTOR pathway and its role in the regulation of tissue regeneration, regulatory T cell differentiation and function, and different types of cancer including hematologic malignancies, skin, prostate, breast, and head and neck cancer. The findings highlight that targeting mTOR pathway is a promising strategy to fight against certain human diseases.

Medicine --- mTOR --- histone deacetylase --- prostate cancer --- integrins --- adhesion --- invasion --- cell metabolism --- T cells --- Foxp3 --- Acute Lymphoblastic leukemia --- targeted therapy --- metabolism --- cell signalling --- mTOR signalling --- head and neck cancer --- mutant genes --- biomarkers --- targeted therapies --- clinical trials --- cancers --- inhibitors --- photodynamic therapy --- PI3K --- Akt --- skin cancers --- phytochemicals --- melanoma --- basal cell carcinoma --- squamous cell carcinoma --- Merkel cell carcinoma --- TNBC --- eribulin --- PI3K/AKT/mTOR --- everolimus --- combination --- synergy --- mTOR signaling --- tissue regeneration --- neuron --- muscle --- liver --- intestine --- hematologic malignancies --- regulatory T cells --- tumor --- mTOR --- histone deacetylase --- prostate cancer --- integrins --- adhesion --- invasion --- cell metabolism --- T cells --- Foxp3 --- Acute Lymphoblastic leukemia --- targeted therapy --- metabolism --- cell signalling --- mTOR signalling --- head and neck cancer --- mutant genes --- biomarkers --- targeted therapies --- clinical trials --- cancers --- inhibitors --- photodynamic therapy --- PI3K --- Akt --- skin cancers --- phytochemicals --- melanoma --- basal cell carcinoma --- squamous cell carcinoma --- Merkel cell carcinoma --- TNBC --- eribulin --- PI3K/AKT/mTOR --- everolimus --- combination --- synergy --- mTOR signaling --- tissue regeneration --- neuron --- muscle --- liver --- intestine --- hematologic malignancies --- regulatory T cells --- tumor

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Featuring a diverse array of model organisms and scientific techniques, Sirtuins: Methods and Protocols collects detailed contributions from experts in the field addressing this vital family of genes. Opening with methods to generate sirtuin biology tools, the book continues by covering methods to identify sirtuin substrates, to measure sirtuin activity, and to study sirtuin biology. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls.   Comprehensive and easy to use, Sirtuins: Methods and Protocols presents detailed protocols for sirtuin research that can be followed directly or modified to investigate new areas of sirtuin biology.

Sirtuins. --- Proteins. --- Proteins --- Group III Histone Deacetylases --- Intracellular Signaling Peptides and Proteins --- ADP Ribose Transferases --- Histone Deacetylases --- Pentosyltransferases --- Amino Acids, Peptides, and Proteins --- Glycosyltransferases --- Amidohydrolases --- Transferases --- Chemicals and Drugs --- Hydrolases --- Enzymes --- Enzymes and Coenzymes --- Sirtuins --- Human Anatomy & Physiology --- Health & Biological Sciences --- Animal Biochemistry --- Silent Mating Type Information Regulator 2-like Proteins --- Sir2-like Proteins --- Silent Mating Type Information Regulator 2 like Proteins --- Sir2 like Proteins --- Coenzymes and Enzymes --- Biocatalysts --- Transferase --- Glycoside Transferases --- Transferases, Glycoside --- Gene Products, Protein --- Gene Proteins --- Protein Gene Products --- Proteins, Gene --- Class I Histone Deacetylases --- Class II Histone Deacetylases --- HDAC Proteins --- Histone Deacetylase --- Histone Deacetylase Complexes --- Complexes, Histone Deacetylase --- Deacetylase Complexes, Histone --- Deacetylase, Histone --- Deacetylases, Histone --- ADP Ribose Transferase --- ADPRT --- ADPRTs --- ART Transferase --- ART Transferases --- ARTase --- ARTases --- Mono ADP-ribose Transferases --- Mono ADPribose Transferase --- Mono ADPribose Transferases --- Mono(ADP-Ribose) Transferase --- Mono(ADP-Ribosyl)transferase --- Mono(ADPribosyl)transferase --- Mono-ADP-Ribosyltransferase --- MonoADPribosyltransferase --- NAD ADP-Ribosyltransferase --- NAD(+)-L-arginine ADP-D-ribosyltransferase --- NAD-Agmatine ADP-Ribosyltransferase --- NAD-Arginine ADP-Ribosyltransferase --- NADP-ADPRTase --- NADP-Arginine ADP-Ribosyltransferase --- ADP-Ribosyltransferase --- Mono(ADP-Ribose) Transferases --- NAD(P)(+)-Arginine ADP-Ribosyltransferase --- NAD+ ADP-Ribosyltransferase --- ADP Ribosyltransferase --- ADP-Ribosyltransferase, NAD --- ADP-Ribosyltransferase, NAD+ --- ADP-Ribosyltransferase, NAD-Agmatine --- ADP-Ribosyltransferase, NAD-Arginine --- ADP-Ribosyltransferase, NADP-Arginine --- ADP-ribose Transferases, Mono --- ADPribose Transferase, Mono --- ADPribose Transferases, Mono --- Mono ADP Ribosyltransferase --- Mono ADP ribose Transferases --- NAD ADP Ribosyltransferase --- NAD Agmatine ADP Ribosyltransferase --- NAD Arginine ADP Ribosyltransferase --- NAD+ ADP Ribosyltransferase --- NADP ADPRTase --- NADP Arginine ADP Ribosyltransferase --- Ribose Transferase, ADP --- Ribose Transferases, ADP --- Transferase, ADP Ribose --- Transferase, ART --- Transferase, Mono ADPribose --- Transferases, ADP Ribose --- Transferases, ART --- Transferases, Mono ADP-ribose --- Transferases, Mono ADPribose --- Intracellular Signaling Peptides --- Intracellular Signaling Proteins --- Peptides, Intracellular Signaling --- Proteins, Intracellular Signaling --- Signaling Peptides, Intracellular --- Signaling Proteins, Intracellular --- Proteids --- Amidases --- NAD-Dependent Histone Deacetylases --- Sir2-like Deacetylases --- Sirtuin Histone Deacetylases --- Deacetylases, NAD-Dependent Histone --- Deacetylases, Sir2-like --- Histone Deacetylases, NAD-Dependent --- NAD Dependent Histone Deacetylases --- Sir2 like Deacetylases --- Life sciences. --- Proteomics. --- Animal genetics. --- Life Sciences. --- Animal Genetics and Genomics. --- Genetics --- Molecular biology --- Biosciences --- Sciences, Life --- Science

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The book highlights work from many different labs that taught us abnormal HDACs potentially contribute to the development or progression of many human diseases including immune dysfunctions, heart disease, cancer, memory impairment, aging, and metabolic disorders.

Chemical structure --- protein-engineering --- biosynthese --- biochemie --- toxicologie --- General biochemistry --- massaspectrometrie --- genetische manipulatie --- Human biochemistry --- medische biochemie --- medische laboratoriumtechnologie --- polypeptiden --- aminozuren --- eiwitten --- Pharmacology. Therapy --- Semiology. Diagnosis. Symptomatology --- Organic spectroscopy --- Histone Deacetylases --- Histone Deacetylase Inhibitors. --- Neoplasms --- Sirtuins --- Histone deacetylase. --- Histone désacétylase --- physiology. --- drug therapy. --- EPUB-LIV-FT LIVBIOLO LIVBIOMO LIVMEDEC SPRINGER-B --- Physiology. --- Drug therapy. --- Toxicology. --- Medicine. --- Post-translational modification . --- Biochemistry. --- Medical laboratories. --- Medical genetics. --- Pharmacology/Toxicology. --- Biomedicine general. --- Posttranslational Modification. --- Protein Science. --- Laboratory Medicine. --- Gene Function. --- Clinical genetics --- Diseases --- Heredity of disease --- Human genetics --- Medical sciences --- Pathology --- Genetic disorders --- Diagnosis, Laboratory --- Health facilities --- Laboratories --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Biology --- Chemistry --- Co-translational modification --- Cotranslational modification --- Modification, Post-translational --- Post-translation protein modification --- Post-translational protein modification --- Posttranslation protein modification --- Posttranslational modification --- Posttranslational protein modification --- Genetic translation --- Proteins --- Health Workforce --- Chemicals --- Medicine --- Pharmacology --- Poisoning --- Poisons --- Genetic aspects --- Composition --- Synthesis --- Toxicology --- Pharmacology. --- Posttranslational modification. --- Proteins . --- Laboratory medicine. --- Biomedicine, general. --- Clinical medicine --- Clinical pathology --- Diagnostic laboratory tests --- Laboratory diagnosis --- Laboratory medicine --- Medical laboratory diagnosis --- Diagnosis --- Proteids --- Biomolecules --- Polypeptides --- Proteomics --- Drug effects --- Medical pharmacology --- Chemotherapy --- Drugs --- Pharmacy --- Physiological effect --- Histones.

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Tea, made from the leaves of the Camellia senenisis plant, is the second most consumed beverage worldwide after water. Accumulating evidence from cellular, animal, epidemiological and clinical studies have linked tea consumption to various health benefits, such as chemoprevention of cancers, chronic inflammation, heart and liver diseases, diabetes, neurodegenerative diseases, etc. Although such health benefits have not been consistently observed in some intervention trials, positive results from clinical trials have provided direct evidence supporting the cancer-protective effect of green tea. In addition, numerous mechanisms of action have been suggested to contribute to tea’s disease-preventive effects. Furthermore, effects of the processing and storage of tea, as well as additives on tea’s properties have been investigated.

polyphenols --- n/a --- cell cycle arrest and apoptosis --- neuroblastoma --- salivary ?-amylase activity --- cancer apoptosis --- yaupon holly --- bioaccessibility --- fracture --- p53 --- tea --- Liubao tea --- BE(2)-C --- matrix metalloproteinase-1 (MMP-1) --- catechin --- renal stone --- oxalate --- protein expression --- 67LR --- Alzheimer’s disease --- EGCG --- nutraceutical --- diseases --- anti-oxidant --- heme oxygenase-1 --- polyphenol --- anxiety --- matcha --- ERCC1/XPF --- neuro-sphere --- tea consumption --- theanine --- Rosmarinic acid --- yerba mate --- hypercalciuria --- gene expression --- microbiota --- cohort study --- histone deacetylase 2 (HDAC2) --- guayusa --- nuclear factor erythroid 2-related factor 2 (Nrf2) --- DNA repair --- mRNA expression --- caffeine --- chemoprevention --- cisplatin --- 6-OH-11-O-hydroxyphenanthrene --- adrenal hypertrophy --- hepatic damage --- anti-photoaging --- cell death --- green tea --- kudingcha --- suberoylanilide hydroxamic acid (SAHA) --- epigallocatechin gallate (EGCG) --- stress-reduction --- calcium oxalate monohydrate --- Camellia sinensis --- chemoresistance --- tea polyphenols --- green tea polyphenols --- green tea catechins --- N-MYC --- cancer --- epigallocatechin-gallate (EGCG) --- Parkinson’s disease --- Alzheimer's disease --- Parkinson's disease