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Adenosine dophosphate-ribolysation --- Adenosine-diphosfaat-ribolisation --- Adénosine diphosphate-ribolysation --- Bacterial toxins --- Bacteriële toxinen --- Toxinen [Bacteriële ] --- Toxines bactériennes --- NAD+ADP-RIBOSYLTRANSFERASE --- Bacterial toxins. --- NAD+ADP-RIBOSYLTRANSFERASE. --- Nad+adp-ribosyltransferase.
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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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Adp-ribosylation. --- Bacterial toxins --- Industrial microorganisms --- Bacterial toxins. --- Guanine nucleotide regulatory protein. --- Poly adp ribose polymerase. --- Signal transduction. --- Adenosinedifosfaat. --- Biologische membranen. --- Stoftransport. --- Bacterial Toxins --- ADP Ribose Transferases --- Receptor-CD3 Complex, Antigen, T-Cell --- Receptor Cross-Talk --- Feedback, Physiological --- Gasotransmitters --- Toxins, Bacterial --- GTP-Binding Proteins --- Signal Transduction --- Receptor Mediated Signal Transduction --- Signal Transduction Pathways --- Signal Transduction Systems --- Receptor-Mediated Signal Transduction --- Signal Pathways --- Pathway, Signal --- Pathway, Signal Transduction --- Pathways, Signal --- Pathways, Signal Transduction --- Receptor-Mediated Signal Transductions --- Signal Pathway --- Signal Transduction Pathway --- Signal Transduction System --- Signal Transduction, Receptor-Mediated --- Signal Transductions --- Signal Transductions, Receptor-Mediated --- System, Signal Transduction --- Systems, Signal Transduction --- Transduction, Signal --- Transductions, Signal --- Cell Communication --- 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 --- ADP-Ribosylation --- physiology --- ADP Ribose Transferases. --- Cellular signal transduction. --- G proteins --- Molecular microbiology --- Physiological effect. --- Genetics --- Congresses. --- Cell Signaling --- Bacterial Toxin --- Toxin, Bacterial --- Fungi. --- Antibiotics --- Lactones --- Streptomyces --- Yeasts
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PARP Inhibitors for Cancer Therapy provides a comprehensive overview of the role of PARP—poly ADP ribose polymerase—in cancer therapy. The volume covers the history of the discovery of PARP and its role in DNA repair. Additionally, it describes the discovery of the PARP family, and includes a discussion of other DNA maintenance-associated PARPs. As well, the volume features a section on the accessible chemistry behind the development of inhibitors. PARP inhibitors—PARPi—are a group of pharmacological inhibitors that are particularly good targets for cancer therapy. PARP plays a pivotal role in DNA repair and may contribute to the therapeutic resistance to DNA-damaging agents used to treat cancer. Researchers have learned a great deal about the biology of PARP and how tumor-specific defects in DNA repair can be exploited by PARPi. The “synthetic lethality” of PARPi is an exciting concept for cancer therapy, and has led to heightened activity in this area.
Biomedicine. --- Cancer Research. --- Drug Resistance. --- Molecular Medicine. --- Medicine. --- Oncology. --- Drug interactions. --- Médecine --- Cancérologie --- Médicaments --- Interaction --- Medicine --- Health & Biological Sciences --- Oncology --- Cancer research. --- Drug resistance. --- Molecular biology. --- Interactions, Drug --- Drugs --- Tumors --- Clinical sciences --- Medical profession --- Human biology --- Life sciences --- Medical sciences --- Pathology --- Physicians --- Side effects --- Health Workforce --- NAD-ADP-ribosyltransferase --- Enzyme inhibitors --- Cancer --- Inhibitors --- Therapeutic use. --- Treatment. --- Cancer therapy --- Cancer treatment --- Antagonists, Enzyme --- Enzyme antagonists --- Enzymes --- Inhibitors, Enzyme --- Metabolic inhibitors --- Chemical inhibitors --- ADP-ribosyltransferase (Polymerizing) --- Poly(ADP-ribose) polymerase --- Poly(ADP-ribose) synthase --- Poly(ADP-ribose) synthetase --- Transferases --- Therapy --- Antagonists --- Molecular biochemistry --- Molecular biophysics --- Biochemistry --- Biophysics --- Biomolecules --- Systems biology --- Resistance to drugs --- Pharmacology --- Cancer research
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Vibrio cholerae, the causative organism of the disease Cholera, colonizes the small intestine and produces several different toxins among which the enterotoxin, or more widely known as cholera toxin (CT), happens to be the major virulence determinant that is responsible for the diarrheal syndrome. This book provides for the first time comprehensive and up-to-date information about all the toxins of Vibrio cholerae, their physical and chemical structures, their biosynthesis and its genetic regulation, their physiology, the molecular biology of their interactions with the host as well as their role in the development of an appropriate and effective cholera vaccine. It also offers relevant and necessary background information on the basic biology of the Vibrio cholerae cell and cholera bacteriophages.
Cholera toxin. --- Cholera toxin --- Bacterial Toxins --- ADP Ribose Transferases --- Enterotoxins --- Toxins, Biological --- Pentosyltransferases --- Biological Factors --- Glycosyltransferases --- Chemicals and Drugs --- Transferases --- Enzymes --- Enzymes and Coenzymes --- Cholera Toxin --- Biology --- Medicine --- Health & Biological Sciences --- Microbiology & Immunology --- Infectious Diseases --- Enterotoxins. --- Enterotoxin --- Cholera enterotoxin --- Cholera exotoxin --- Choleragen --- Choleragenoid --- CT (Cholera toxin) --- CTX (Cholera toxin) --- Procholeragenoid --- Vibrio cholerae enterotoxin --- Medicine. --- Medical microbiology. --- Pharmacology. --- Food --- Biochemistry. --- Cell biology. --- Microbiology. --- Biomedicine. --- Medical Microbiology. --- Food Science. --- Biochemistry, general. --- Cell Biology. --- Pharmacology/Toxicology. --- Biotechnology. --- Bacterial toxins --- NAD-ADP-ribosyltransferase --- Food science. --- Cytology. --- Toxicology. --- Chemicals --- Pharmacology --- Poisoning --- Poisons --- Cell biology --- Cellular biology --- Cells --- Cytologists --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Chemistry --- Medical sciences --- Science --- Microbial biology --- Microorganisms --- Toxicology --- Composition --- Food—Biotechnology. --- Drug effects --- Medical pharmacology --- Chemotherapy --- Drugs --- Pharmacy --- Physiological effect
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