Arginine amino acid [[electronic resource] /] / editor, Nathan L. Jacobs |
Pubbl/distr/stampa | New York, : Nova Science Publishers, c2011 |
Descrizione fisica | 1 online resource (283 p.) |
Disciplina | 612.3/98 |
Altri autori (Persone) | JacobsNathan L |
Collana |
Microbiology research advances
Protein biochemistry, synthesis, structure, and cellular functions |
Soggetto topico |
Arginine
Amino acids |
Soggetto genere / forma | Electronic books. |
ISBN | 1-61122-254-0 |
Formato | Materiale a stampa |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Record Nr. | UNINA-9910461447803321 |
New York, : Nova Science Publishers, c2011 | ||
Materiale a stampa | ||
Lo trovi qui: Univ. Federico II | ||
|
Arginine amino acid [[electronic resource] /] / editor, Nathan L. Jacobs |
Pubbl/distr/stampa | New York, : Nova Science Publishers, c2011 |
Descrizione fisica | 1 online resource (283 p.) |
Disciplina | 612.3/98 |
Altri autori (Persone) | JacobsNathan L |
Collana |
Microbiology research advances
Protein biochemistry, synthesis, structure, and cellular functions |
Soggetto topico |
Arginine
Amino acids |
ISBN | 1-61122-254-0 |
Formato | Materiale a stampa |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Record Nr. | UNINA-9910790032603321 |
New York, : Nova Science Publishers, c2011 | ||
Materiale a stampa | ||
Lo trovi qui: Univ. Federico II | ||
|
Arginine amino acid / / editor, Nathan L. Jacobs |
Edizione | [1st ed.] |
Pubbl/distr/stampa | New York, : Nova Science Publishers, c2011 |
Descrizione fisica | 1 online resource (283 p.) |
Disciplina | 612.3/98 |
Altri autori (Persone) | JacobsNathan L |
Collana |
Microbiology research advances
Protein biochemistry, synthesis, structure, and cellular functions |
Soggetto topico |
Arginine
Amino acids |
ISBN | 1-61122-254-0 |
Formato | Materiale a stampa |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Intro -- ARGININE AMINO ACID -- ARGININE AMINO ACID -- Contents -- Preface -- Chapter 1 Analytical Methods of the Determination of Arginine Amino Acid -- Abstract -- Introduction -- Sources -- Dietary Sources -- Biosynthesis -- Functions and Importance of Arginine -- Methods of Analysis -- Liquid Chromatography -- Ion Exchange Separation -- Reverse-Phase Liquid Chromatography -- Gas Chromatography -- Capillary Electrophoresis -- Nuclear Magnetic Resonance Spectroscopy -- Methodological Considerations Regarding the Quantification of L-Arginine in Biological Matrices -- Derivatization Reagents for LC Analysis -- Ninhydrin -- Dansyl Chloride -- Dabsyl Chloride -- 1-Fluoro-2, 4-Dinitrobenzene -- Phenylisothiocyanate -- Ortho-Phtaldehyde -- 9H-Fluoren-9-Ylmethyl Chloroformate -- Diethyl 2(Ethoxymethylidene)Propanedioate -- 6-Aminoquinolyl-N-Hydroxysuccinimidyl Carbamate -- Conclusion -- References -- Chapter 2 Alternative Metabolic Pathways of Arginine and their Pathophysiological Roles -- Abstract -- Abbreviations -- Introduction - Arginine, a Functional Amino Acid with Several Metabolic Roles -- Nitric Oxide Synthase -- Arginase -- Alternative Pathways of Arginine Metabolism -- Inhibition of NOS and Arginase Isoforms -- NOS Inhibitors -- Arginase Inhibitors -- NOS Isoforms in Diseases -- The Involvement of NOS Isoforms in the Obesity and Metabolic Syndrome -- Nitric Oxide and Preeclampsia -- Arginase in Diseases -- Arginase in Cardiovascular Diseases -- Arginase in Pulmonary Hypertension -- Arginase in Silicosis -- Arginase in Asthma -- Arginase in other Disorders -- Conclusion -- References -- Chapter 3 Free Amino Acid Analysis in Natural Matrices -- Abstract -- Introduction -- Essential Amino Acids -- Nonessential Amino Acids -- 1. Amino Acids Analysis -- 1.1. Derivatization -- Post-Column Derivatization -- Pre-Column Derivatization.
1.2. Separation -- High Performance Liquid Chromatography (HPLC) -- Mass Spectrometry (MS) -- Gas Chromatography (GC) -- Capillary Electrophoresis -- 2. Free Amino Acids in Natural Matrices -- 2.1. Wild Edible Mushroom Species -- 2.2. Brassica oleraceae var. costata DC (Tronchuda Cabbage) -- Internal Leaves -- External Leaves -- 2.3. Red Wine -- Dekkera bruxellensis -- Amino Acids Profile of Dão Red Wine and D. bruxellensis Effects -- 2.4. Quince (Cydonia oblonga Miller) Fruit and Jam -- Quince Fruit -- Quince Jam -- 2.5. Catharanthus roseus -- Conclusion -- Acknowledgments -- References -- Chapter 4 Discovery of Argininosuccinate Synthetase and Argininosuccinate Lyase -- Abstract -- 1. Introduction to Arginine -- 2. History of Arginine Synthesis -- Step 1 -- Step 2 -- 3. The Biochemical Reactions of Arginine Synthesis -- Step 1 -- Step 2 -- Step 2 -- Step 1 -- Step 3 -- Step 1a -- Step 1b -- Step 1 -- Step 2 -- 4. Catalytic, Physical, and Immunological Properties of ASS -- Catalytic Properties -- Physical Properties -- Immunological Properties -- 5. Molecular Aspects of ASS -- 6. Catalytic, Physical, and Immunological Properties of ASL -- Catalytic and Immunological Properties -- Physical Properties -- Comparative Analyses -- 7. Molecular Aspects of ASL -- 8. Tissue Expression of ASS and ASL -- Acknowledgments -- References -- Chapter 5 Expression and Localization of Argininosuccinate Synthetase and Argininosuccinate Lyase in the Female and Male Rat Kidneys -- Abstract -- Introduction -- Material and Methods -- Animals -- Kidney Preparation and Dissection of the Renal Zones -- Protein Extraction and Western Blot Analyses -- Indirect Immunofluorescence -- Calculation and Statistical analyses -- Chemicals -- Results -- Regional Distribution of ASS Protein in the Rat Kidney -- Regional Expression of ASL Protein in the Rat Kidney. Differential Expression of ASS and ASL in the Rat Kidney -- Conclusion -- Acknowledgments -- References -- Chapter 6 Chemical Structure and Toxicity in Arginine-Based Surfactants -- Abstract -- 1. Introduction -- 2. Experimental Methods -- 2.1. Adsorption and Aggregation Properties -- 2.2. Red Blood Cell Assay -- 2.3. Citotoxicity Evaluation -- 3. Single Chain Arginine Surfactants -- 3.1. Adsorption and Aggregation Properties -- 3.2. Toxicity -- 4. Arginine-Based Gemini Surfactants -- 4.1. Adsorption and Aggregation Properties -- 4.2. Toxicity -- 4.2.1 Hemolysis and Potential Ocular Irritation -- 4.2.2 Cytotoxicity -- 5. Glycerolipid-Like Arginine Based Surfactants -- 5.1. Adsorption and Aggregation Properties -- 5.2. Toxicity -- 5.2.1. Hemolysis -- 5.2.2. Cytotoxicity -- Conclusion -- References -- Chapter 7 Arginine: Physico-Chemical Properties, Interactions with Ion-Exchange Membranes, Recovery and Concentration by Electrodialysis -- 1. Introduction -- 2. Experimental -- 3. Results and Discussion -- 3.1. Arginine Sorption by Cation-Exchange Membranes -- 3.2. Hydration of Membranes, Saturated with Arginine -- 3.3. Recovery and Concentration of Arginine in an Electromembrane System -- Conclusion -- Note -- References -- Chapter 8 Central Functions of L-Arginine and its Metabolites for Stress Behavior -- Abstract -- 1. Introduction -- 2. Central Functions of L-Arginine, Nitric Oxide, Agmatine, L-Ornithine and L-Citrulline for Stress Behavior in Chicks -- 3. Central Functions of L-Proline for Stress Response in Chicks -- 4. Central Functions of L-Glutamate for Stress Response in Chicks -- 5. Central Functions of Polyamines for Stress Response in Chicks -- 6. Central Functions of Creatine for Stress Response in Chicks -- Acknowledgments -- References. Chapter 9 Arginine Requirement and Metabolism in Marine Fish Larvae - Review of Recent Findings -- Abstract -- 1. Introduction -- 2. Amino Acid Requirements in Diplodus Sargus and Solea Senegalensis: Comparison of Arginine Levels in Larvae and Live Food -- 3. Metabolism of Arginine -- 4. Supplementation of Arginine in Long Term Trials -- Discussion -- Acknowledgments -- References -- Chapter 10 Arginine-Rich Cell-Penetrating Peptides in Cellular Internalization -- Abstract -- Introduction -- Materials and Methods -- Preparations of Plasmids, Proteins, Peptides and Nanoparticles. -- Mammalian and Plant Cells -- Covalent Protein Transduction (CPT) in Plant Cells -- Noncovalent Protein Transduction (NPT) in Mammalian Cells -- Covalent and Noncovalent Protein Transductions (CNPT) in Mammalian Cells -- Fluorescent and Confocal Microscopy -- Results -- Covalent Protein Transduction (CPT) in Plant Cells -- Noncovalent Protein Transduction (NPT) in Mammalian Cells -- Covalent and Noncovalent Protein Transductions (CNPT) in Mammalian Cells -- Discussion -- Conclusion -- Acknowledgments -- Abbreviations -- References -- Chapter 11 Effects of Deep Sea Water on Changes in Free Amino Acids and Tolerance to Fusarium Root Rot in Mycorrhizal Asparagus Plants -- Abstract -- Introduction -- Materials and Methods -- AMF Inoculation and Growing Plants -- Evaluation of AMF Colonization Level -- Determination of Free Amino Acids in Plants -- Inoculation with Fusarium Proliferatum -- Estimation of Symptoms of Fp -- Results -- Discussion -- Acknowledgments -- References -- Chapter 12 Influence of Arginine-Containing Peptides on the Haemostasis System -- Abstract -- Introduction -- Materials and Methods -- Results -- Discussion -- References -- Chapter 13 Newly Identified Transcriptional Regulation by Mcm1p at ARG1 Promoter -- Abstract. 1. Recruitment of Mcm1p by Gcn4p at ARG1 -- 2. Promoter-Dependent Recruitment of Homodimeric Mcm1p By Activation Domain of Gcn4p -- 3. Collaborative Cooperation for Recruitment Between Mcm1p and Gcn4p At ARG1 -- 4. Mutagenesis of DNA Elements in ARG1 Promoter and Requirement of Mcm1p Binding Site for Gcn4p Recruitment -- 5. Contribution of Mcm1p for Recruitment of Co-Activator SWI/SNF -- 6. Requirement of Mcm1p Binding Site for Growth and ARG1 Transcription in Arginine Starvation -- 7. Additional Requirement of Gcn4p And Mm1p in Synthetic Defined Complete Medium Than in Synthetic Defined Minimal Medium During Arginine Starvation -- 8. Requirement of Mcm1p Binding Sites for Survival in the Absence of Arginine and Gcn4p -- 9. Regulation of Mcm1p Binding Site in ARC2 Through Excess Amino Acids Rather Than Arginine -- 10. Arginine-Dependent Subunit Assembly for Argr/Mcm1p Repressor at ARG1 -- 11. Directions and Applications for Future Work -- References -- Index -- Blank Page. |
Record Nr. | UNINA-9910812237803321 |
New York, : Nova Science Publishers, c2011 | ||
Materiale a stampa | ||
Lo trovi qui: Univ. Federico II | ||
|
Bioactive proteins and peptides as functional foods and nutraceuticals / / Yoshinori Mine, Eunice Li-Chan, and Bo Jiang, editors |
Edizione | [1st ed.] |
Pubbl/distr/stampa | Ames, Iowa, : Wiley-Blackwell, c2010 |
Descrizione fisica | 1 online resource (436 p.) |
Disciplina |
612.3/98
664.01 |
Altri autori (Persone) |
MineYoshinori
Li-ChanEunice JiangBo <1962-> |
Collana | Institute of Food Technologists Series |
Soggetto topico |
Proteins in human nutrition
Functional foods |
ISBN |
1-282-68306-3
9786612683060 0-8138-1132-5 |
Formato | Materiale a stampa |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Bioactive Proteins and Peptides as Functional Foods and Nutraceuticals; Contents; Preface; Contributors; Part 1:Introduction; Chapter 1: Biologically Active Food Proteins and Peptides in Health: An Overview; Part 2:Functions of Biologically Active Proteins and Peptides; Chapter 2: Anti-inflammatory/Oxidative Stress Proteins and Peptides; Chapter 3:Antioxidant Peptides; Chapter 4: Antihypertensive Peptides and Their Underlying Mechanisms; Chapter 5: Food Protein-Derived Peptides as Calmodulin Inhibitors; Chapter 6:Soy Protein for the Metabolic Syndrome
Chapter 7:Amyloidogenic Proteins and PeptidesChapter 8: Peptide-Based Immunotherapy for Food Allergy; Chapter 9: Gamma-Aminobutyric Acid; Chapter 10: Food Proteins or Their Hydrolysates as Regulators of Satiety; Part 3: Examples of Food Proteins and Peptides with Biological Activity; Chapter 11: Health-Promoting Proteins and Peptides in Colostrum and Whey; Chapter 12:Functional Food Products with Antihypertensive Effects; Chapter 13: Secreted Lactoferrin and Lactoferrin-Related Peptides: Insight into Structure and Biological Functions Chapter 14: Bioactive Peptides and Proteins from Fish Muscle and CollagenChapter 15: Animal Muscle-Based Bioactive Peptides; Chapter 16: Processing and Functionality of Rice Bran Proteins and Peptides; Chapter 17:Bioactive Proteins and Peptides from Egg Proteins; Chapter 18:Soy Peptides as Functional Food Materials; Chapter 19: Bioactivity of Proteins and Peptides from Peas(Pisum sativum, Vigna unguiculata , and Cicer arietinum L); Chapter 20:Wheat Proteins and Peptides; Part 4: Recent Advances in Bioactive Peptide Analysis for Food Application Chapter 21:Peptidomics for Bioactive Peptide AnalysisChapter 22:In silico Analysis of Bioactive Peptides; Chapter 23: Flavor-Active Properties of Amino Acids, Peptides, and Proteins; Chapter 24: Controlled Release and Delivery Technology of Biologically Active Proteins and Peptides; Index |
Record Nr. | UNINA-9910139218303321 |
Ames, Iowa, : Wiley-Blackwell, c2010 | ||
Materiale a stampa | ||
Lo trovi qui: Univ. Federico II | ||
|
Glutathione and sulfur amino acids in human health and disease / / Roberta Masella and Giuseppe Mazza |
Autore | Masella Roberta |
Edizione | [1st ed.] |
Pubbl/distr/stampa | Hoboken, : Wiley, c2009 |
Descrizione fisica | 1 online resource (626 p.) |
Disciplina |
612.015756
612.3/98 612.398 |
Altri autori (Persone) | MazzaG. <1946-> |
Soggetto topico |
Glutathione - Psychological aspects
Sulfur amino acids - Psychological aspects Glutathione - Therapeutic use Sulfur amino acids - Therapeutic use Glutathione - Metabolism Sulfur amino acids - Metabolism |
ISBN |
1-282-27852-5
9786612278525 0-470-47597-8 0-470-47596-X |
Formato | Materiale a stampa |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
GLUTATHIONE AND SULFUR AMINO ACIDS IN HUMAN HEALTH AND DISEASE; CONTENTS; PREFACE; CONTRIBUTORS; I INTRODUCTION; 1 GLUTATHIONE AND THE SULFUR-CONTAINING AMINO ACIDS: AN OVERVIEW; 1.1 Introduction; 1.2 Why Sulfur-Containing Amino Acids?; 1.3 S-Adenosylmethionine, Nature's Wonder Cofactor; 1.4 Glutathione; 1.5 Taurine-the Second Essential Sulfur-Containing Amino Acid?; 1.6 Conclusions; Acknowledgments; References; II CHEMISTRY AND METABOLISM OF GSH AND SULFUR AMINO ACIDS; 2 SULFUR AMINO ACIDS CONTENTS OF DIETARY PROTEINS: DAILY INTAKE AND REQUIREMENTS; 2.1 Introduction
2.2 Sulfur Amino Acids (SAA) Content of Dietary Protein2.3 Sulfur Amino Acid Intake; 2.4 Nutritional Requirement for Total Sulfur Amino Acids; 2.5 Conclusions; References; 3 CELLULAR COMPARTMENTALIZATION OF GLUTATHIONE; 3.1 Introduction; 3.2 Glutathione Content in Cells; References; 4 INTESTINAL METABOLISM OF SULFUR AMINO ACIDS; 4.1 Introduction; 4.2 Isotopic Approaches to Study Metabolism; 4.3 Evidence of Gut Sulfur Amino Acid Metabolism; 4.4 Other Key Players in Intestinal Sulfur Amino Acid Metabolism; 4.5 Cysteine in Redox Function and Oxidant Stress in the Gut 4.6 Pathophysiology of Sulfur Amino Acid Metabolism in the GIT4.7 Conclusions; References; 5 HEPATIC SULFUR AMINO ACID METABOLISM; 5.1 Introduction; 5.2 Dietary Relation between Methionine and Cysteine; 5.3 Metabolic Relation between Hepatic Sulfur Amino Acids, B Vitamins, and Methyl Group Metabolism; 5.4 Regulation of Sulfur Amino Acid Metabolism and Related Metabolic Pathways in the Liver; 5.5 Impact of Physiologic and Nutritional Factors on Sulfur Amino Acid Metabolism; 5.6 Conclusions; References; III ANTIOXIDANT AND DETOXIFICATION ACTIVITIES 6 GLUTATHIONE AND SULFUR CONTAINING AMINO ACIDS: ANTIOXIDANT AND CONJUGATION ACTIVITIES6.1 Introduction; 6.2 Reactive Oxygen Species and Antioxidants; 6.3 Glutathione Redox Cycle; 6.4 Regulation of GSH and Cysteine Levels; 6.5 Biotransformation; 6.6 ROS-Mediated Cellular Signaling; 6.7 Transcription Regulation of Antioxidant and Conjugation Enzymes; 6.8 Oxidative Stress and Diseases; References; 7 GLUTAREDOXIN AND THIOREDOXIN ENZYME SYSTEMS: CATALYTIC MECHANISMS AND PHYSIOLOGICAL FUNCTIONS; 7.1 Introduction; 7.2 General Characteristics of Glutaredoxins 7.3 General Characteristics of Thioredoxins7.4 Glutaredoxin Mechanism of Action; 7.5 Thioredoxin Mechanism of Action; 7.6 Control of Grx Expression; 7.7 Control of Trx Expression in Mammalian Systems; 7.8 Cellular Functions of Grx; 7.9 Cellular Functions of Trx; 7.10 Reversible Sulfhydryl Oxidation and Disease; 7.11 Conclusions; References; 8 METHIONINE SULFOXIDE REDUCTASES: A PROTECTIVE SYSTEM AGAINST OXIDATIVE DAMAGE; 8.1 Introduction; 8.2 History of the Msr System; 8.3 MsrA and MsrB Protein Structure and Mechanism of Action; 8.4 Msr Reducing Requirement; 8.5 Other Members of the Msr Family 8.6 The Msr System: Both a Repair Enzyme and a Scavenger of ROS |
Record Nr. | UNINA-9910139751303321 |
Masella Roberta | ||
Hoboken, : Wiley, c2009 | ||
Materiale a stampa | ||
Lo trovi qui: Univ. Federico II | ||
|
Protein biosynthesis [[electronic resource] /] / Toma E. Esterhouse, Lado B. Petrinos, editors |
Pubbl/distr/stampa | New York, : Nova Science Publishers, c2009 |
Descrizione fisica | 1 online resource (374 p.) |
Disciplina | 612.3/98 |
Altri autori (Persone) |
EsterhouseToma E
PetrinosLado B |
Soggetto topico | Proteins - Synthesis |
Soggetto genere / forma | Electronic books. |
ISBN | 1-61470-704-9 |
Formato | Materiale a stampa |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto | Protein synthesis and ageing / Kostoula Troulinaki, Nektarios Tavernarakis -- Neuropeptide biosynthesis in the nematode caenorhabditis elegans : from precursor to bioactive peptides / Steven J. Husson, Liliane Schoofs -- Research and review studies stereochemical mechanism of translation based on intersubunit complementaries / Kozo Nagano -- Trans-translation by tmRNA and a protein mimicking tRNA and mRNA / Hyouta Himeno, Daisuke Kurita, Akira Muto -- Modification of mRNA translation initiation to stimulate protein synthesis in sepsis / Thomas C. Vary -- Protein synthesis in hepatocytes of mice as revealed by electron microscopic radioautography / Tetsuji Nagata -- Recent advances in label-free biosensors applications in protein biosynthesis and HTS screening / Shawn o'Malley -- Translating memories : the role of protein biosynthesis in synaptic plasticity / Cara J. Westmark, James S. Malter -- Evolution and the universality of the mechanism of initiation of protein synthesis / Tokumasa Nakamoto -- Secreted protein and peptide biosynthesis : precursor structures and processing mechanisms / Kozlov S.A, Vassilevski A.A, Grishin E.V. -- The effects of temperature on ectotherm protein metabolism / Nia M. Whiteley, Keiron P.P. Fraser -- Protein biosynthesis : a new method for functional expression of sodium-dependent glucose transporter (SGLT) to study inhibition of transport activity and drug discovery / Francisco Castaneda -- Effect of hypoxic conditions on translational control of gene expression / Ota Fuchs -- The role of eukaryotic translation initiation factor 4E and it's binding factors 4E-BP1 and 4E-BP2 in body weight regulation, ageing and tumorigenesis / Ota Fuchs. |
Record Nr. | UNINA-9910461535903321 |
New York, : Nova Science Publishers, c2009 | ||
Materiale a stampa | ||
Lo trovi qui: Univ. Federico II | ||
|
Protein biosynthesis [[electronic resource] /] / Toma E. Esterhouse, Lado B. Petrinos, editors |
Pubbl/distr/stampa | New York, : Nova Science Publishers, c2009 |
Descrizione fisica | 1 online resource (374 p.) |
Disciplina | 612.3/98 |
Altri autori (Persone) |
EsterhouseToma E
PetrinosLado B |
Soggetto topico | Proteins - Synthesis |
ISBN | 1-61470-704-9 |
Formato | Materiale a stampa |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto | Protein synthesis and ageing / Kostoula Troulinaki, Nektarios Tavernarakis -- Neuropeptide biosynthesis in the nematode caenorhabditis elegans : from precursor to bioactive peptides / Steven J. Husson, Liliane Schoofs -- Research and review studies stereochemical mechanism of translation based on intersubunit complementaries / Kozo Nagano -- Trans-translation by tmRNA and a protein mimicking tRNA and mRNA / Hyouta Himeno, Daisuke Kurita, Akira Muto -- Modification of mRNA translation initiation to stimulate protein synthesis in sepsis / Thomas C. Vary -- Protein synthesis in hepatocytes of mice as revealed by electron microscopic radioautography / Tetsuji Nagata -- Recent advances in label-free biosensors applications in protein biosynthesis and HTS screening / Shawn o'Malley -- Translating memories : the role of protein biosynthesis in synaptic plasticity / Cara J. Westmark, James S. Malter -- Evolution and the universality of the mechanism of initiation of protein synthesis / Tokumasa Nakamoto -- Secreted protein and peptide biosynthesis : precursor structures and processing mechanisms / Kozlov S.A, Vassilevski A.A, Grishin E.V. -- The effects of temperature on ectotherm protein metabolism / Nia M. Whiteley, Keiron P.P. Fraser -- Protein biosynthesis : a new method for functional expression of sodium-dependent glucose transporter (SGLT) to study inhibition of transport activity and drug discovery / Francisco Castaneda -- Effect of hypoxic conditions on translational control of gene expression / Ota Fuchs -- The role of eukaryotic translation initiation factor 4E and it's binding factors 4E-BP1 and 4E-BP2 in body weight regulation, ageing and tumorigenesis / Ota Fuchs. |
Record Nr. | UNINA-9910789899503321 |
New York, : Nova Science Publishers, c2009 | ||
Materiale a stampa | ||
Lo trovi qui: Univ. Federico II | ||
|
Protein biosynthesis / / Toma E. Esterhouse, Lado B. Petrinos, editors |
Edizione | [1st ed.] |
Pubbl/distr/stampa | New York, : Nova Science Publishers, c2009 |
Descrizione fisica | 1 online resource (374 p.) |
Disciplina | 612.3/98 |
Altri autori (Persone) |
EsterhouseToma E
PetrinosLado B |
Soggetto topico | Proteins - Synthesis |
ISBN | 1-61470-704-9 |
Formato | Materiale a stampa |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto | Protein synthesis and ageing / Kostoula Troulinaki, Nektarios Tavernarakis -- Neuropeptide biosynthesis in the nematode caenorhabditis elegans : from precursor to bioactive peptides / Steven J. Husson, Liliane Schoofs -- Research and review studies stereochemical mechanism of translation based on intersubunit complementaries / Kozo Nagano -- Trans-translation by tmRNA and a protein mimicking tRNA and mRNA / Hyouta Himeno, Daisuke Kurita, Akira Muto -- Modification of mRNA translation initiation to stimulate protein synthesis in sepsis / Thomas C. Vary -- Protein synthesis in hepatocytes of mice as revealed by electron microscopic radioautography / Tetsuji Nagata -- Recent advances in label-free biosensors applications in protein biosynthesis and HTS screening / Shawn o'Malley -- Translating memories : the role of protein biosynthesis in synaptic plasticity / Cara J. Westmark, James S. Malter -- Evolution and the universality of the mechanism of initiation of protein synthesis / Tokumasa Nakamoto -- Secreted protein and peptide biosynthesis : precursor structures and processing mechanisms / Kozlov S.A, Vassilevski A.A, Grishin E.V. -- The effects of temperature on ectotherm protein metabolism / Nia M. Whiteley, Keiron P.P. Fraser -- Protein biosynthesis : a new method for functional expression of sodium-dependent glucose transporter (SGLT) to study inhibition of transport activity and drug discovery / Francisco Castaneda -- Effect of hypoxic conditions on translational control of gene expression / Ota Fuchs -- The role of eukaryotic translation initiation factor 4E and it's binding factors 4E-BP1 and 4E-BP2 in body weight regulation, ageing and tumorigenesis / Ota Fuchs. |
Record Nr. | UNINA-9910813327003321 |
New York, : Nova Science Publishers, c2009 | ||
Materiale a stampa | ||
Lo trovi qui: Univ. Federico II | ||
|
Protein Degradation [[electronic resource] ] : Cell Biology of the Ubiquitin-Proteasome System |
Autore | Mayer R. John |
Pubbl/distr/stampa | Hoboken, : Wiley, 2008 |
Descrizione fisica | 1 online resource (254 p.) |
Disciplina |
572.76
612.3/98 |
Altri autori (Persone) |
CiechanoverAaron J
RechsteinerMartin |
Collana | Protein Degradation |
Soggetto topico |
Cell Physiology
Proteins - Metabolism Proteins - metabolism Proteins --Metabolism Ubiquitin Ubiquitin - physiology Animal Biochemistry Human Anatomy & Physiology Health & Biological Sciences |
Soggetto genere / forma | Electronic books. |
ISBN |
1-282-37219-X
9786612372193 3-527-62022-2 3-527-62029-X |
Formato | Materiale a stampa |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Protein Degradation; Contents; Preface; List of Contributors; 1 Ubiquitin: A New Player in the Peroxisome Field; 1.1 Introduction; 1.2 Matrix Protein Import into Peroxisomes is Mediated by Cycling Receptors; 1.3 Pex5p is Monoubiquitinated in Wild-type Cells, but Polyubiquitinated in Late-acting pex Mutants; 1.4 Ubiquitination of Pex18p; 1.5 Role for the RING Finger and AAA Peroxins in Pex5p Ubiquitination and Recycling; 1.6 Pex5p Monoubiquitination: A Role in Receptor Recycling; 1.7 Conclusions/Future Prospects; Acknowledgements; References
2 The Ubiquitin Proteasome System and Muscle Development2.1 Introduction; 2.2 Muscle Histology; 2.3 UPS and Developing Muscle; 2.3.1 Ubiquitin-dependent Degradation of MyoD; 2.3.2 Degradation of MyoD by SCF(MAFbx); 2.3.3 Other Muscle Regulatory Factors; 2.4 UPS and Organizing Muscle; 2.4.1 Ozz-E3-dependent β-Catenin Regulation in the Muscle; 2.4.2 Regulation of Myosin Assembly by CHN-1 and UFD-2; 2.5 UPS and Muscle Destruction or Degeneration; 2.5.1 N-end Rule and Muscle Atrophy; 2.5.2 MuRFs, E3 Enzymes in Atrophying Muscles; 2.5.3 Atrogin-1/MAFbx Function in Muscle Atrophy 2.5.4 Activation of Muscle-atrophy Pathways2.6 Concluding Remarks; References; 3 The COP9 Signalosome: Structural and Biochemical Conservation and Its Roles in the Regulation of Plant Development; 3.1 Introduction; 3.2 The Plant COP9 Signalosome; 3.3 CSN Involvement in the Ubiquitin-Proteasome Pathway; 3.4 Plant CSN Biochemical Activities; 3.4.1 Deneddylation; 3.4.2 Subcellular Partitioning; 3.5 CSN Functions in Plant Development; 3.5.1 Floral Development; 3.5.2 Responses to Plant Hormones; 3.5.3 Disease Resistance; 3.5.4 Photomorphogenesis; 3.6 Conclusions; References 4 Ubiquitin and Protein Sorting to the Lysosome4.1 Introduction; 4.2 Identification of Ubiquitin as an Endosomal Sorting Signal; 4.3 Ubiquitin-mediated Sorting at the Endosome: The MVB Sorting Machinery; 4.3.1 Endosome-associated Ubiquitin Interacting Domains: Structure and Function; 4.3.2 The Hrs-STAM Complex and the Endosomal Clathrin Coat; 4.3.3 GGA and Tom1: Alternative Sorting Adapters?; 4.3.4 The ESCRT Machinery; 4.3.5 Vps4-SKD1; 4.4 Ubiquitin Ligases and Endosomal Sorting; 4.4.1 Nedd4 Family; 4.4.2 c-Cbl; 4.5 Endosomal DUBs; 4.5.1 Ubp1 and Ubp2; 4.5.2 Doa4; 4.5.3 UBPY; 4.5.4 AMSH 4.6 Polyubiquitin Linkages and Endocytosis4.6.1 Proteasome Involvement in Endocytic Sorting; 4.6.2 K63-linked Ubiquitin; 4.7 Future Directions; Acknowledgements; References; 5 ISG15-dependent Regulation; 5.1 Introduction and Overview; 5.2 The Discovery of ISG15; 5.3 Structure and Properties of the ISG15 Protein; 5.4 The ISG15 Conjugation Pathway; 5.4.1 Activation of ISG15 by UbE1L; 5.4.2 UbcH8 is an ISG15-specific Conjugating Enzyme; 5.4.3 Candidate ISG15-specific Ligases; 5.5 Regulation of Intracellular ISG15 Pools; 5.6 Functional Roles for ISG15; 5.6.1 ISG15 as an Extracellular Cytokine 5.6.2 Role of ISG15 in the Antiviral Response |
Record Nr. | UNINA-9910144008003321 |
Mayer R. John | ||
Hoboken, : Wiley, 2008 | ||
Materiale a stampa | ||
Lo trovi qui: Univ. Federico II | ||
|
Protein Degradation [[electronic resource] ] : Cell Biology of the Ubiquitin-Proteasome System |
Autore | Mayer R. John |
Pubbl/distr/stampa | Hoboken, : Wiley, 2008 |
Descrizione fisica | 1 online resource (254 p.) |
Disciplina |
572.76
612.3/98 |
Altri autori (Persone) |
CiechanoverAaron J
RechsteinerMartin |
Collana | Protein Degradation |
Soggetto topico |
Cell Physiology
Proteins - Metabolism Proteins - metabolism Proteins --Metabolism Ubiquitin Ubiquitin - physiology Animal Biochemistry Human Anatomy & Physiology Health & Biological Sciences |
ISBN |
1-282-37219-X
9786612372193 3-527-62022-2 3-527-62029-X |
Formato | Materiale a stampa |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Protein Degradation; Contents; Preface; List of Contributors; 1 Ubiquitin: A New Player in the Peroxisome Field; 1.1 Introduction; 1.2 Matrix Protein Import into Peroxisomes is Mediated by Cycling Receptors; 1.3 Pex5p is Monoubiquitinated in Wild-type Cells, but Polyubiquitinated in Late-acting pex Mutants; 1.4 Ubiquitination of Pex18p; 1.5 Role for the RING Finger and AAA Peroxins in Pex5p Ubiquitination and Recycling; 1.6 Pex5p Monoubiquitination: A Role in Receptor Recycling; 1.7 Conclusions/Future Prospects; Acknowledgements; References
2 The Ubiquitin Proteasome System and Muscle Development2.1 Introduction; 2.2 Muscle Histology; 2.3 UPS and Developing Muscle; 2.3.1 Ubiquitin-dependent Degradation of MyoD; 2.3.2 Degradation of MyoD by SCF(MAFbx); 2.3.3 Other Muscle Regulatory Factors; 2.4 UPS and Organizing Muscle; 2.4.1 Ozz-E3-dependent β-Catenin Regulation in the Muscle; 2.4.2 Regulation of Myosin Assembly by CHN-1 and UFD-2; 2.5 UPS and Muscle Destruction or Degeneration; 2.5.1 N-end Rule and Muscle Atrophy; 2.5.2 MuRFs, E3 Enzymes in Atrophying Muscles; 2.5.3 Atrogin-1/MAFbx Function in Muscle Atrophy 2.5.4 Activation of Muscle-atrophy Pathways2.6 Concluding Remarks; References; 3 The COP9 Signalosome: Structural and Biochemical Conservation and Its Roles in the Regulation of Plant Development; 3.1 Introduction; 3.2 The Plant COP9 Signalosome; 3.3 CSN Involvement in the Ubiquitin-Proteasome Pathway; 3.4 Plant CSN Biochemical Activities; 3.4.1 Deneddylation; 3.4.2 Subcellular Partitioning; 3.5 CSN Functions in Plant Development; 3.5.1 Floral Development; 3.5.2 Responses to Plant Hormones; 3.5.3 Disease Resistance; 3.5.4 Photomorphogenesis; 3.6 Conclusions; References 4 Ubiquitin and Protein Sorting to the Lysosome4.1 Introduction; 4.2 Identification of Ubiquitin as an Endosomal Sorting Signal; 4.3 Ubiquitin-mediated Sorting at the Endosome: The MVB Sorting Machinery; 4.3.1 Endosome-associated Ubiquitin Interacting Domains: Structure and Function; 4.3.2 The Hrs-STAM Complex and the Endosomal Clathrin Coat; 4.3.3 GGA and Tom1: Alternative Sorting Adapters?; 4.3.4 The ESCRT Machinery; 4.3.5 Vps4-SKD1; 4.4 Ubiquitin Ligases and Endosomal Sorting; 4.4.1 Nedd4 Family; 4.4.2 c-Cbl; 4.5 Endosomal DUBs; 4.5.1 Ubp1 and Ubp2; 4.5.2 Doa4; 4.5.3 UBPY; 4.5.4 AMSH 4.6 Polyubiquitin Linkages and Endocytosis4.6.1 Proteasome Involvement in Endocytic Sorting; 4.6.2 K63-linked Ubiquitin; 4.7 Future Directions; Acknowledgements; References; 5 ISG15-dependent Regulation; 5.1 Introduction and Overview; 5.2 The Discovery of ISG15; 5.3 Structure and Properties of the ISG15 Protein; 5.4 The ISG15 Conjugation Pathway; 5.4.1 Activation of ISG15 by UbE1L; 5.4.2 UbcH8 is an ISG15-specific Conjugating Enzyme; 5.4.3 Candidate ISG15-specific Ligases; 5.5 Regulation of Intracellular ISG15 Pools; 5.6 Functional Roles for ISG15; 5.6.1 ISG15 as an Extracellular Cytokine 5.6.2 Role of ISG15 in the Antiviral Response |
Record Nr. | UNINA-9910830200703321 |
Mayer R. John | ||
Hoboken, : Wiley, 2008 | ||
Materiale a stampa | ||
Lo trovi qui: Univ. Federico II | ||
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