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Post-Translational Modifications (PTMs) may occur at any stage following the translation process in the lifecycle of specific proteins. PTMs regulate several cellular processes including protein stability, subcellular localization, and protein-protein interactions. In recent years, more and more target proteins of PTMs have been proved to be related to epigenetic regulation and cell fate. Some enzymes that catalyze PTMs have also been found to be involved in human diseases. This book intends to provide the reader with an overview of the current state of the art in this research field, which focuses on the recent advances, new findings and perspectives in cellular functions, and their clinical significance in human diseases. We hope this book will help researchers in this area.
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Over a decade ago, a small cellular protein of 12 kDa, with 18% homology to the well-known ubiquitin protein, was co-discovered and termed Small Ubiquitin-like Modifier, or SUMO. Sumoylation is a post-translational modification that utilizes SUMO as the modifier group covalently attached to target substrates. This state-of-the art review on the sumoylation system deals with protein modification as it pertains to regulation of diverse cellular functions. Each chapter has been written by a leading researcher and covers the role of sumoylation in fundamental biochemical activities (transcription, RNA processing, chromatin remodelling, DNA repair, nucleocytoplasmic transport, ion channel regulation, and metabolic pathways). The text also examines the part sumoylation plays in critical cellular processes such as mitosis, meiosis, differentiation, senescence, and apoptosis. Lastly, the emerging role of sumoylation in specific diseases, including cancer and diabetes as well as neurodegenerative ones, is explored with an emphasis on defining molecular mechanisms that may provide new targets for treatment or prevention. While SUMO was discovered more than 10 years ago, this is still a relatively young field, and much remains to be discovered about the biochemical and biological properties of this modification system. In just the last few years, it has become clear that sumoylation modifies hundreds of cellular proteins, and there has been increased appreciation for the breadth of cellular functions that are impacted by this post-translational modification.
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Post - Translational Modification: A Practical Approach and its companion volume Protein Expression: A Practical Approach form the final part of the PAS mini-series on protein synthesis and processing. This volume begins with a chapter on protein sequencing followed by a chapter on protein folding and import into organelles. The next three chapters cover the three major forms of covalent modification: phosphorylation, glycosylation, and lipid modification. Proteolytic processing the is the next topic and the final two chapters are concerned with protein turnover in mammalian cells and yeast. This book is a comprehensive volume of the best current methodology and is designed to be used at the bench or away from the bench to gain insight into future experimental approached.
Genetics --- Biology --- Health & Biological Sciences --- Post-translational modification
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The field of proteomics holds great promise for identifying non-targeted, global molecular profiles ""signatures"" of normal and diseased cells. This work shows that strategies based on the separate analysis of subcellular compartments provide the means to determine protein location in a cell.
Proteomics. --- Proteins --- Protein binding. --- Gene expression. --- DNA microarrays. --- Post-translational modification. --- Structure.
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This book describes transcription factors in the context of hematopoietic development and reveal mechanistic insights how they orchestrate specific gene expression patterns. Several examples from lymphoid and myeloid lineages are given as well as particular examples of leukemia fusion proteins that contain a part of a transcription factor. In the given chapters covering each one particular example, the function of transcription factors is characterized in normal as well as leukemic contexts. New technologies such as ChIP-Seq or RNA-Seq, that make use of genome-wide sequencing, have shown that such master regulators of blood cell development often work in combinatorial fashion and, when dysregulated, results in leukemogenesis. This book is not only intended for experts but it should also be a useful resource for younger scientists or scientists from other disciplines, who may use this book as a stimulating starting point for further discoveries and/ or translational endeavors.
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This book provides a timely review of the role of histone modifications in epigenetic control of gene expression. Topics covered include: basic mechanisms of molecular recognition of histone post-translational modification (PTMs); combinatorial readout of histone PTMs by tandem epigenome reader domains; genome-wide profiling of histone PTM interactions; small molecule modulation of histone PTM interactions and their potential as a new approach to therapeutic intervention in human diseases. All chapters were written by leading scientists who made the original key discoveries of the structure and mechanism of evolutionarily conserved reader domains, which serve to direct gene transcription in chromatin through interactions with DNA-packing histones in a PTM-sensitive manner.
Biomedicine. --- Gene Expression. --- Posttranslational Modification. --- Protein-Ligand Interactions. --- Gene Function. --- Medicine. --- Gene expression. --- Medical genetics. --- RNA-ligand interactions. --- Post-translational modification of proteins. --- Médecine --- Expression génique --- Génétique médicale --- Post-translational modification. --- Human Anatomy & Physiology --- Health & Biological Sciences --- Physiology --- Histones. --- Proteins. --- Posttranslational modification. --- Basic proteins --- Chromatin --- Nucleoproteins --- Post-translational modification . --- Clinical genetics --- Diseases --- Heredity of disease --- Human genetics --- Medical sciences --- Pathology --- Genetic disorders --- 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 --- Genes --- Genetic regulation --- Genetic aspects --- Synthesis --- Expression --- Proteins . --- Proteids --- Biomolecules --- Polypeptides --- Proteomics
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This book focuses on the three most important aspects of ageing research: nutrition, physical exercise and epigenetics. The contributors discuss ways that age-related epigenetic imprints such as DNA methylation and histone acetylation are modified by these two interventions. The emphasis on epigenetics helps to illuminate the underlying mechanisms of anti-ageing interventions, as ageing and disease are predominately epigenetic phenomena. Among the highlights are chapter-length discussion of such topics as: how anti-inflammatory action of calorie restriction underlies the retardation of ageing and age-related diseases (Chapter 3); epigenetic modification of gene expression by exercise (Chapter 5); the role of functional foods and their bioactive components in bone health (Chapter 8); and an account of the first decade of a study of calorie restriction in nonhuman primates, conducted by the National Institute on Ageing. .
Biomedicine. --- Biomedicine general. --- Geriatrics/Gerontology. --- Cell Biology. --- Clinical Nutrition. --- Aging. --- Posttranslational Modification. --- Medicine. --- Geriatrics. --- Personal health and hygiene. --- Post-translational modification of proteins. --- Cytology. --- Aging --- Médecine --- Gériatrie --- Cytologie --- Vieillissement --- Research. --- Recherche --- Aging_xResearch. --- Post-translational modification. --- Epigenetics. --- Nutrition. --- Health aspects. --- Alimentation --- Food --- Nutrition --- Age --- Ageing --- Senescence --- Health aspects --- Physiological effect --- Clinical nutrition. --- Posttranslational modification. --- Cell biology. --- Health --- Physiology --- Diet --- Dietetics --- Digestion --- Food habits --- Malnutrition --- Genetics --- Developmental biology --- Gerontology --- Longevity --- Age factors in disease --- Post-translational modification . --- 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 --- Cell biology --- Cellular biology --- Biology --- Cells --- Cytologists --- Medicine --- Older people --- Clinical sciences --- Medical profession --- Human biology --- Life sciences --- Medical sciences --- Pathology --- Physicians --- Synthesis --- Diseases --- Health and hygiene --- Biomedicine, general. --- Clinical nutrition --- Diet and disease --- Dietotherapy --- Medical nutrition therapy --- MNT (Medical nutrition therapy) --- Nutrition therapy --- Therapeutics, Physiological --- Health Workforce --- Therapeutic use --- Biomedical Research. --- Ageing. --- Post-translational Modifications. --- Biological research --- Biomedical research
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This collection of review articles describes the structure, function and mechanism of individual protein methyltransferase enzymes including protein lysine methyltransferases, protein arginine methyltransferases, and also the less abundant protein histidine methyltransferases and protein N-terminal end methyltransferases. The topics covered in the individual reviews include structural aspects (domain architecture, homologs and paralogs, and structure), biochemical properties (mechanism, sequence specificity, product specificity, regulation, and histone and non-histone substrates), cellular features (subcellular localization, expression patterns, cellular roles and function, biological effects of substrate protein methylation, connection to cell signaling pathways, and connection to chromatin regulation) and their role in diseases. This review book is a useful resource for scientists working on protein methylation and protein methyltransferases and those interested in joining this emerging research field.
protein lysine methylation --- H3K9 methylation --- PKMT --- enzyme specificity --- enzyme regulation --- heterochromatin --- protein post-translational modification --- NSD3 --- WHSC1L1 --- structure and function --- protein arginine methylation --- PRMT7 --- epigenetics --- cancer --- immunity --- pluripotency --- SETDB1 --- methyltransferase --- schizophrenia --- Huntington’s disease --- Rett syndrome --- Prader–Willi syndrome --- congenital heart diseases --- inflammatory bowel disease --- MLL2 --- structure --- H3K4me3 --- chromatin regulation --- disease --- dystonia --- NSD1 --- H3K36 --- SOTOS --- NUP98-NSD1 --- AML --- PRMT6 --- post-translational modification --- H3R2me2a --- SETD3 --- posttranslational modifications --- protein histidine methylation --- actin --- polymerization --- cytoskeleton --- enteroviruses --- oncogenesis --- PRMT5 --- cardiovascular disease --- neurodegenerative diseases --- diabetes --- inflammation --- G9a --- GLP --- EHMT2 --- EHMT1 --- post translational modification --- lysine methylation --- N-terminal methylation --- translation --- eEF1A --- METTL13 --- neuron --- synapse --- dendritic spine --- actin cytoskeleton --- GTPase --- PRMT1 --- arginine methylation --- H4R3 methylation --- transcriptional regulation --- cell signaling --- DNA damage repair --- PRMT2 --- SH3 --- SETMAR --- Metnase --- H3K36me2 --- Hsmar1 --- non-homologous end joining repair --- NHEJ --- transposase --- transposable elements --- histone --- SET7/9 --- SETD7 --- lysine-specific methyltransferase (PKMT) --- cell proliferation --- stress response --- post-translational protein modification --- n/a --- Huntington's disease --- Prader-Willi syndrome
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This volume focusses on oxidative modifications of lipid molecules and the successive generation of singlet oxygen. The book also covers the secondary adductions of these reactive species with proteins and aminophospholipids. During lipid peroxidation, the initial event is the formation of lipid hydroperoxide, which is followed by an oxidation event that starts a chain-reaction. The formed lipid hydroperoxide gradually decomposes into harmful aldehydes, which are the advanced end-products of lipid peroxidation. The book consists of three sections: Part I, entitled Lipid peroxidation and small molecule adducts focusses on the biochemical events that are involved in lipid peroxidation and to the formation of small molecules like singlet molecular oxygen. This part of the book also introduces the hexanoyl-lysine adduct. Part II, entitled Pathophysiological consequences covers a range of damaging physiological consequences of lipid peroxidation, ranging from atherosclerosis to neurodegenerative disorders. Finally, Part III, entitled Applications for diagnosis and development of functional food looks into potential diagnostic uses of lipid peroxidation, the possible beneficial effects that can be achieved and new assays in food safely that have been developed.
Lipids --- Lipids. --- Peroxidation. --- Lipides --- Lipins --- Lipoids --- Medicine. --- Cancer research. --- Food --- Posttranslational modification. --- Biomedicine. --- Cancer Research. --- Posttranslational Modification. --- Food Science. --- Biotechnology. --- Biomolecules --- Steroids --- Oncology. --- Post-translational modification . --- Food science. --- Science --- 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 --- Tumors --- Synthesis --- Food—Biotechnology. --- Cancer research
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