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Many plants produce enzymes collectively known as ribosome-inactivating proteins (RIPs). RIPs catalyze the removal of an adenine residue from a conserved loop in the large ribosomal RNA. The adenine residue removed by this depurination is crucial for the binding of elongation factors. Ribosomes modified in this way are no longer able to carry out protein synthesis. Most RIPs exist as single polypeptides (Type 1 RIPs) which are largely non-toxic to mammalian cells because they are unable to enter them and thus cannot reach their ribosomal substrate. In some instances, however, the RIP forms part of a heterodimer where its partner polypeptide is a lectin (Type 2 RIPs). These heterodimeric RIPs are able to bind to and enter mammalian cells. Their ability to reach and modify ribosomes in target cells means these proteins are some of the most potently cytotoxic poisons found in nature, and are widely assumed to play a protective role as part of the host plant’s defenses. RIPs are able to further damage target cells by inducing apoptosis. In addition, certain plants produce lectins lacking an RIP component but which are also cytotoxic. This book focuses on the structure/function and some potential applications of these toxic plant proteins.
Plant proteins. --- Polypeptides. --- Plant proteins --- Polypeptides --- Plant Proteins --- Lectins --- N-Glycosyl Hydrolases --- Proteins --- Glycoside Hydrolases --- Plant Lectins --- Ribosome Inactivating Proteins --- Amino Acids, Peptides, and Proteins --- Hydrolases --- Enzymes --- Chemicals and Drugs --- Enzymes and Coenzymes --- Botany --- Earth & Environmental Sciences --- Plant Physiology --- Life sciences. --- Plant biochemistry. --- Cell biology. --- Plant science. --- Botany. --- Plant physiology. --- Life Sciences. --- Plant Biochemistry. --- Cell Biology. --- Plant Physiology. --- Plant Sciences. --- Biopolymers --- Peptides --- Plant polymers --- Biochemistry. --- Cytology. --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Biology --- Chemistry --- Medical sciences --- Botanical science --- Phytobiology --- Phytography --- Phytology --- Plant biology --- Plant science --- Natural history --- Plants --- Physiology --- Cell biology --- Cellular biology --- Cells --- Cytologists --- Composition --- Floristic botany --- Phytochemistry --- Plant biochemistry --- Plant chemistry --- Biochemistry --- Phytochemicals --- Plant biochemical genetics
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*** This series does not include back cover copy. ***.
Electronic books. -- local. --- Hydrolases. --- Paraoxonase -- Physiological effect. --- Paraoxonase --- Aryldialkylphosphatase --- Physiology --- Biological Science Disciplines --- Phosphoric Triester Hydrolases --- Natural Science Disciplines --- Esterases --- Disciplines and Occupations --- Hydrolases --- Enzymes --- Enzymes and Coenzymes --- Chemicals and Drugs --- Animal Biochemistry --- Medical Research --- Cytology --- Biology --- Human Anatomy & Physiology --- Medicine --- Health & Biological Sciences --- Physiological effect --- Physiological effect. --- Hydrolytic enzymes --- Aromatic esterase --- Arylesterase --- Life sciences. --- Pharmacology. --- Cardiology. --- Medical biochemistry. --- Cell biology. --- Life Sciences. --- Cell Biology. --- Pharmacology/Toxicology. --- Medical Biochemistry. --- Medical biochemistry --- Pathobiochemistry --- Pathological biochemistry --- Biochemistry --- Pathology --- Cell biology --- Cellular biology --- Cells --- Cytologists --- Heart --- Internal medicine --- Drug effects --- Medical pharmacology --- Medical sciences --- Chemicals --- Chemotherapy --- Drugs --- Pharmacy --- Biosciences --- Sciences, Life --- Science --- Diseases --- Cytology. --- Toxicology. --- Biochemistry. --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Chemistry --- Pharmacology --- Poisoning --- Poisons --- Composition --- Toxicology --- Los Angeles (Calif.)
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The Rho GTPases in Cancer is the first volume to collect and summarize the current understanding of the Rho GTPases and their involvement in the progression of human cancer. The critical role of the Rho GTPases, their regulatory proteins, and their effectors in cancer progression has become increasingly evident over the past decade. As translational research increases on these proteins, their importance as keystone molecules in vital cellular process is highlighted. Thus, these molecules represent a major class of potential therapeutic targets that could be exploited clinically. This aspect of Rho GTPase biology is developing, therefore the contents of The Rho GTPases in Cancer should prove of interest to clinicians and members of the cancer research community wishing to develop new treatments for cancer.
Cancer -- Etiology. --- Rho GTPases --- Cancer --- Monomeric GTP-Binding Proteins --- Diseases --- rho GTP-Binding Proteins --- Neoplasms --- GTP-Binding Proteins --- Intracellular Signaling Peptides and Proteins --- GTP Phosphohydrolases --- Peptides --- Proteins --- Carrier Proteins --- Amino Acids, Peptides, and Proteins --- Acid Anhydride Hydrolases --- Chemicals and Drugs --- Hydrolases --- Enzymes --- Enzymes and Coenzymes --- Medicine --- Human Anatomy & Physiology --- Oncology --- Animal Biochemistry --- Health & Biological Sciences --- Etiology --- Rho GTPases. --- G proteins. --- GTP-binding proteins --- GTP regulatory proteins --- Guanine nucleotide-binding proteins --- Guanine nucleotide regulatory proteins --- Rho G proteins --- Rho GTP-binding proteins --- Medicine. --- Cancer research. --- Pharmacology. --- Cell biology. --- Biomedicine. --- Cancer Research. --- Cell Biology. --- Pharmacology/Toxicology. --- Membrane proteins --- G proteins --- Guanosine triphosphatase --- Oncology. --- Cytology. --- Toxicology. --- Chemicals --- Pharmacology --- Poisoning --- Poisons --- Cell biology --- Cellular biology --- Biology --- Cells --- Cytologists --- Tumors --- Toxicology --- Drug effects --- Medical pharmacology --- Medical sciences --- Chemotherapy --- Drugs --- Pharmacy --- Cancer research --- Physiological effect
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Ribonuclease P (RNaseP), a ribonucleoprotein, is an essential tRNA processing enzyme found in all living organisms. Since its discovery almost 40 years ago, research on RNase P has led to the discovery of the catalytic properties of RNA, and of the only known, naturally occurring RNA enzymes, RNase P catalytic RNA. The description of the catalytic properties of RNA has provided fundamental insight into the RNA world and these catalytic properties are being harnessed as therapeutic and prevention strategies for acquired and inherited diseases. Ribonuclease P is the first book to provide a comprehensive collection covering all aspects of current research on RNase P. The topics include kinetic and structural analysis, mechanism of catalysis, and its regulation and biogenesis in prokaryotes, eukaryotes, and organelles. Furthermore, research progresses on developing RNase P as a potential drug target for antimicrobial development and as a gene-targeting tool for anti-infective and anticancer therapy are also included. This book should be of general interests to molecular biologists and biochemists in both the academic section and pharmaceutical industry.
Gene silencing. --- Ribonucleases. --- RNA. --- Small interfering RNA -- Therapeutic use. --- RNA --- Ribonucleases --- Ribonucleoproteins --- Endoribonucleases --- RNA, Catalytic --- Nucleic Acids --- Ribonuclease P --- Enzymes --- RNA-Binding Proteins --- Nucleic Acids, Nucleotides, and Nucleosides --- Nucleoproteins --- Carrier Proteins --- Chemicals and Drugs --- Enzymes and Coenzymes --- Esterases --- Proteins --- Hydrolases --- Amino Acids, Peptides, and Proteins --- Human Anatomy & Physiology --- Chemistry --- Biochemistry --- Animal Biochemistry --- Physical Sciences & Mathematics --- Health & Biological Sciences --- Proteins. --- Proteids --- RNases --- Life sciences. --- Proteomics. --- Life Sciences. --- Molecular biology --- Biosciences --- Sciences, Life --- Science --- Biomolecules --- Polypeptides --- Proteomics --- Nucleases
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The diversity of RNAs inside living cells is amazing. We have known of the more “classic” RNA species: mRNA, tRNA, rRNA, snRNA and snoRNA for some time now, but in a steady stream new types of molecules are being described as it is becoming clear that most of the genomic information of cells ends up in RNA. To deal with the enormous load of resulting RNA processing and degradation reactions, cells need adequate and efficient molecular machines. The RNA exosome is arising as a major facilitator to this effect. Structural and functional data gathered over the last decade have illustrated the biochemical importance of this multimeric complex and its many co-factors, revealing its enormous regulatory power. By gathering some of the most prominent researchers in the exosome field, it is the aim of this volume to introduce this fascinating protein complex as well as to give a timely and rich account of its many functions. The exosome was discovered more than a decade ago by Phil Mitchell and David Tollervey by its ability to trim the 3’end of yeast, S. cerevisiae, 5. 8S rRNA. In a historic account they laid out the events surrounding this identification and the subsequent birth of the research field. In the chapter by Kurt Januszyk and Christopher Lima the structural organization of eukaryotic exosomes and their evolutionary counterparts in bacteria and archaea are discussed in large part through presentation of structures.
Ribonucleases. --- Ribosomes. --- RNA -- Metabolism. --- Ribonucleases --- RNA --- Ribosomes --- Metabolic Phenomena --- Biochemical Phenomena --- Nucleic Acids --- Exonucleases --- Chemical Phenomena --- Esterases --- Phenomena and Processes --- Nucleic Acids, Nucleotides, and Nucleosides --- Chemicals and Drugs --- Hydrolases --- Enzymes --- Enzymes and Coenzymes --- Exoribonucleases --- Metabolism --- RNA Stability --- Human Anatomy & Physiology --- Health & Biological Sciences --- Animal Biochemistry --- Metabolism. --- Ribonucleoprotein particles --- Ribonucleic acid metabolism --- RNases --- Medicine. --- Molecular biology. --- Biomedicine. --- Biomedicine general. --- Molecular Medicine. --- Molecular biochemistry --- Molecular biophysics --- Biochemistry --- Biophysics --- Biomolecules --- Systems biology --- Clinical sciences --- Medical profession --- Human biology --- Life sciences --- Medical sciences --- Pathology --- Physicians --- Cell organelles --- Microsomes --- Nucleoproteins --- Protoplasm --- Nucleases --- Health Workforce --- Biomedicine, general.
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Vascular smooth muscle (VSM) constitutes most of the tunica media in blood vessels and plays an important role in the control of vascular tone. Ca2+ is a major regulator of VSM contraction and is strictly regulated by an intricate system of Ca2+ mobilization and Ca2+ homeostatic mechanisms. The interaction of a physiological agonist with its plasma membrane receptor stimulates the hydrolysis of membrane phospholipids and increases the generation of inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG). IP3 stimulates Ca2+ release from the intracellular stores in the sarcoplasmic reticulum. Agonists also stimulate Ca2+ influx from the extracellular space via voltage-gated, receptor-operated, and store-operated channels. Ca2+ homeostatic mechanisms tend to decrease the intracellular free Ca2+ concentration ([Ca2+]i) by activating Ca2+ extrusion via the plasmalemmal Ca2+ pump and the Na+/Ca2+ exchanger and the uptake of excess Ca2+ by the sarcoplasmic reticulum and possibly the mitochondria. A threshold increase in [Ca2+]i activates Ca2+-dependent myosin light chain (MLC) phosphorylation, stimulates actin-myosin interaction, and initiates VSM contraction. The agonist-induced maintained increase in DAG also activates specific protein kinase C (PKC) isoforms, which in turn cause phosphorylation of cytoplasmic substrates that increase the contractile myofilaments force sensitivity to Ca2+ and thereby enhance VSM contraction. Agonists could also activate Rho kinase (ROCK), leading to inhibition of MLC phosphatase and further enhancement of the myofilaments force sensitivity to Ca2+. The combined increases in [Ca2+]i, PKC and ROCK activity cause significant vasoconstriction and could also stimulate VSM hypertrophy and hyperplasia. The protracted and progressive activation of these processes could lead to pathological vascular remodeling and vascular disease.
Muscle contraction. --- Vascular diseases. --- Vascular smooth muscle. --- Ion Channels --- Muscle Proteins --- Microfilament Proteins --- Hemodynamics --- Muscle, Smooth --- Molecular Motor Proteins --- Cardiovascular Diseases --- Blood Vessels --- Diseases --- Muscles --- Contractile Proteins --- Cardiovascular Physiological Processes --- Cardiovascular System --- Adenosine Triphosphatases --- Membrane Glycoproteins --- Biopolymers --- Membrane Transport Proteins --- Cytoskeletal Proteins --- Polymers --- Tissues --- Carrier Proteins --- Acid Anhydride Hydrolases --- Proteins --- Cardiovascular Physiological Phenomena --- Membrane Proteins --- Anatomy --- Musculoskeletal System --- Amino Acids, Peptides, and Proteins --- Circulatory and Respiratory Physiological Phenomena --- Macromolecular Substances --- Hydrolases --- Chemicals and Drugs --- Phenomena and Processes --- Enzymes --- Enzymes and Coenzymes --- Myosins --- Muscle, Smooth, Vascular --- Vasoconstriction --- Calcium Channels --- Vascular Diseases --- Human Anatomy & Physiology --- Health & Biological Sciences --- Physiology --- Vascular resistance. --- Blood pressure. --- Vascular smooth muscle --- Physiology. --- physiology. --- Signal transduction --- Calcium --- Blood pressure --- AngII, angiotensin II --- ATP, adenosine triphosphate --- CPI-17, PKC-potentiated phosphatase inhibitor protein-17 kDa --- CAM, calmodulin --- DAG, diacylglycerol --- ET-1, endothelin --- IP3, inositol 1,4,5-trisphosphate --- MAPK, mitogen-activated protein kinase --- MARCKs, myristoylated alanine-rich C-kinase substrate --- MEK, MAPK kinase --- MLC, myosin light chain --- NCX, Na+-Ca2+ exchanger --- PDBu, phorbol 12,13-dibutyrate; PIP2, phosphatidylinositol 4,5-bisphosphate --- PKC, protein kinase C --- PMA, phorbol myristate acetate --- RACKs, receptors for activated C-kinase --- ROCK, Rho-kinase --- VSMC, vascular smooth muscle cell
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