Excess of homocysteine, a product of the metabolism of the essential amino acid methionine, is associated with poor health, is linked to heart and brain diseases in general human populations, and accelerates mortality in heart disease patients. Neurological and cardiovascular abnormalities occur in patients with severe genetic hyperhomocysteinemia and lead to premature death due to vascular complications. Although it is considered a non-protein amino acid, studies over the past dozen years have discovered mechanisms by which homocysteine becomes a component of proteins. Homocysteine-containing proteins lose their normal biological function and become auto-immunogenic and pro-thrombotic. In this book, the author, a pioneer and a leading contributor to the field, describes up-to date studies of the biological chemistry of homocysteine-containing proteins, as well as pathological consequences and clinical implications of their formation. This is a comprehensive account of the broad range of basic science and medical implications of homocysteine-containing proteins for health and disease. ​

This is an unusually comprehensive 2001 account of the broad range of medical implications of homocysteine.

This state-of-the-art review provides an in-depth and critical summary of homocysteine from its molecular basis to clinical relevance and current clinical trials of folic acid and vitamin B6. Written by leading workers in the field, the book provides an authoritative, comprehensive and thoroughly up-to-date overview for scientists and clinicians and any others engaged in the field. It will also be useful to anyone involved in managing vascular patients or cardiac risk factors, as well as biochemists, pharmacologists, general physicians, cardiologists and clinical and basic researchers with an interest in preventive medicine.

Protein Modificomics: From Modifications to Clinical Perspectives comprehensively deals with all of the most recent aspects of post-translational modification (PTM) of proteins, including discussions on diseases involving PTMs, such as Alzheimer's, Huntington's, X-linked spinal muscular atrophy-2, aneurysmal bone cyst, angelman syndrome and OFC10. The book also discusses the role PTMs play in plant physiology and the production of medicinally important primary and secondary metabolites. The understanding of PTMs in plants helps us enhance the production of these metabolites without greatly altering the genome, providing robust eukaryotic systems for the production and isolation of desired products without considerable downstream and isolation processes.

The complex roles of glutathione and sulfur amino acids in human health Glutathione (γ-L-glutamyl-L-cysteinylglycine, GSH) is a major antioxidant acting as a free radical scavenger that protects the cell from reactive oxygen species (ROS). Sulfur amino acids (SAAs), such as methionine and cysteine, play a critical role in the maintenance of health. GSH depletion as well as alterations of SAA metabolism are linked to a host of disease states including liver cirrhosis, various pulmonary diseases, myocardial ischemia and reperfusion injury, aging, Parkinson's disease, Alzheimer's disease, sepsis, and others. This book provides researchers with a comprehensive review of the biochemistry, absorption, metabolism, biological activities, disease prevention, and health promotion of glutathione and sulfur amino acids. The twenty-two chapters explore such topics as: Chemistry, absorption, transport, and metabolism of GSH and sulfur amino acids Antioxidant and detoxification properties of GSH and sulfur amino acids, highlighting the enzymatic systems involved in antioxidant defenses Biological activities of GSH and sulfur amino acids and their role in modulating cell processes Role of GSH and sulfur amino acid deficiency and alteration in the onset of diseases and in aging Protective effects exerted by GSH and sulfur amino acids when used as drugs, functional foods, and nutraceuticals in humans and animals Special attention is paid to the molecular mechanisms for the modulation of transcription factors and enzyme activities, as well as the nutritional and therapeutic significance of dietary sulfur amino acids as shown in human and animal models. With more than 2,000 scientific references, this book provides food scientists, nutritionists, biochemists, food technologists, chemists, molecular biologists, and public health professionals with a comprehensive and up-to-date examination of glutathione and sulfur amino acids in human health and disease.

This invaluable volume, written by an international group of scientists, presents an overview of the AdoMet-dependent methyltransferases, with special emphasis on structure-function relationships.S-adenosyl-L-methionine (AdoMet) is the second most commonly used enzyme cofactor after ATP. The AdoMet-dependent methyltransferases act on a wide variety of target molecules, including DNA, RNA, protein, polysaccharides, lipids and a range of small molecules.The well-conserved architecture of these enzymes, and the implications of this conservation for their evolutionary history, are major themes of this book. The thirteen chapters describe in detail the structures, enzyme kinetics and biological roles of the AdoMet-dependent methyltransferases from a wide range of cell types: plant, animal, bacterial and archaeal.

This book familiarizes the reader with some recent trends in the theory and practice of thrombolysis. It covers the field of fibrinolysis from the standpoint of basic scientists and clinicians and delivers the state-of-the-art information on the biochemistry and pharmacology of fibrinolysis, as well as related novel methodological and diagnostic tools in the field. An introductory chapter summarizes the basic molecular mechanisms in fibrinolysis (plasminogen, its endogenous activators and their inhibitors, plasmin and its inhibitors). Recent developments in our understanding of fibrin formation are described in the context of its impact on fibrinolysis. The discussion of neutrophil extracellular traps in the modulation of fibrin assembly and the consequences regarding plasminogen activation and plasmin action addresses a novel aspect of fibrinolysis.