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000799918 019__ $$a1004225459$$a1004528765
000799918 020__ $$a9789811025136$$q(electronic book)
000799918 020__ $$a9811025134$$q(electronic book)
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000799918 050_4 $$aQP609.P78
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000799918 24500 $$aProteases in physiology and pathology /$$cSajal Chakraborti, Naranjan S. Dhalla, editors.
000799918 260__ $$aSingapore :$$bSpringer,$$c2017.
000799918 300__ $$a1 online resource.
000799918 336__ $$atext$$btxt$$2rdacontent
000799918 337__ $$acomputer$$bc$$2rdamedia
000799918 338__ $$aonline resource$$bcr$$2rdacarrier
000799918 5050_ $$aDedication; Preface; Contents; About the Editors; Part I: Regulation of Proteases in Health and Disease; 1: Physiological and Pathological Functions of Mitochondrial Proteases; 1.1 Introduction; 1.2 Physiological Roles of Mitoproteases; 1.2.1 Proteolysis in the Outer Membrane; 1.2.2 Proteolysis in the Intermembrane Space; 1.2.3 Proteolysis in the Inner Membrane; 1.2.4 Proteolysis in the Mitochondrial Matrix; 1.3 Pathological Contributions of Mitoproteases; 1.3.1 Mitochondrial Proteases in Cancer; 1.3.2 Mitochondrial Proteases in Neurodegenerative Diseases
000799918 5058_ $$a1.3.3 Mitochondrial Proteases in Multisystemic Diseases1.4 Conclusions; References; 2: The Role of Matrix Metalloproteinase-2 and Metalloproteinase-9 in Embryonic Neural Crest Cells and Their Derivatives; 2.1 Introduction; 2.2 Matrix Metalloproteinases; 2.3 MMP-2 and MMP-9 in the Onset of NCC Migration; 2.4 MMP-2 and MMP-9 in NCC Derivatives in Embryos and Adults; 2.4.1 Cranial Cartilage and Bone; 2.4.2 Heart; 2.4.3 Melanocytes; 2.4.4 Adipocytes; 2.4.5 Enteric Neurons; 2.4.6 Glial Cells; 2.5 Activators and Repressors of MMP-2 and MMP-9 in NCCs; 2.6 Conclusion; References
000799918 5058_ $$a3: The Matrix Metalloproteinase and Tissue Inhibitors of Metalloproteinase Balance in Physiological and Pathological Remodeling of Skeletal Muscles3.1 Introduction; 3.2 MMPs and TIMPs in Skeletal Muscles: Expression and Role; 3.2.1 MMPs /TIMPs in Skeletal Muscle Cells; 3.2.1.1 Role of MMPs in Myogenic Cells; MMPs Contribute to Cell Migration; MMPs Contribute to Cell Fusion; 3.3 MMPs in Remodeling Skeletal Muscles; 3.3.1 Skeletal Muscle Plasticity; 3.3.2 Skeletal Muscle Degeneration and Regeneration; 3.4 Deregulation of MMPs in Skeletal Muscle Diseases; 3.4.1 Inflammatory Myopathies
000799918 5058_ $$a3.4.2 Muscular Dystrophies3.4.3 Neurogenic Myopathies; 3.5 MMPs/TIMPs Are Involved in Inflammation and Fibrosis of Diseased Skeletal Muscles; 3.5.1 MMP Involvement in Skeletal Muscle Inflammation; 3.5.2 MMP/TIMP Involvement in Skeletal Muscle Fibrosis; 3.6 Conclusion and Perspectives; References; 4: Role of BMP1/Tolloid like Proteases in Bone Morphogenesis and Tissue Remodeling; 4.1 Introduction; 4.2 Structure of the Protease Domain of BTPs; 4.2.1 Primary Structure; 4.2.2 X-ray Structure; 4.3 Substrate Specificity; 4.4 Biological Roles of BTPs; 4.4.1 Matrix Assembly
000799918 5058_ $$a4.4.2 Activation of Signalling Molecules4.5 BTP's and Disease; 4.5.1 Fibrosis; 4.5.2 Bone Disorders; 4.5.3 Cancer; 4.6 Modulators of BTPs; 4.6.1 Activators; 4.6.2 Inhibitors; 4.7 Conclusion and Future Perspectives; References; 5: Role of Proteases in the Regulation of N-Myristoyltransferase; 5.1 Introduction; 5.2 Differential Regulation of N-Myristoyltransferase Isoforms; 5.3 Regulation of NMT Functions by Proteases; 5.4 Summary; References; 6: Role of Tissue Factor-FVIIa Blood Coagulation Initiation Complex in Cancer; 6.1 Introduction
000799918 506__ $$aAccess limited to authorized users.
000799918 520__ $$aUsing a multidisciplinary approach, this book describes the biochemical mechanisms associated with dysregulation of proteases and the resulting pathophysiological consequences. It highlights the role and regulation of different types of proteases as well as their synthetic and endogenous inhibitors. The role of proteases was initially thought to be limited to general metabolic digestion. However, we now know that the role of protein breakdown is much more complex, and proteases have multiple functions: they are coupled to turnover and can affect protein composition, function and synthesis. In addition to eliminating abnormal proteins, breakdown has many modulatory functions, including activating and inactivating enzymes, modulating membrane function, altering receptor channel properties, affecting transcription and cell cycles and forming active peptides. The ubiquity of proteases in nature makes them an important target for drug development. This in-depth, comprehensive is a valuable resource for researchers involved in identifying new targets for drug development. With its multidisciplinary scope, it bridges the gap between fundamental and translational research in the biomedical and pharmaceutical industries, making it thought-provoking reading for scientists in the field.
000799918 588__ $$aDescription based on print version record.
000799918 650_0 $$aProteolytic enzymes.
000799918 7001_ $$aChakraborti, Sajal.
000799918 7001_ $$aDhalla, Naranjan S.
000799918 77608 $$iPrint version:$$z9811025126$$z9789811025129$$w(OCoLC)954008378
000799918 852__ $$bebk
000799918 85640 $$3SpringerLink$$uhttps://univsouthin.idm.oclc.org/login?url=http://link.springer.com/10.1007/978-981-10-2513-6$$zOnline Access$$91397441.1
000799918 909CO $$ooai:library.usi.edu:799918$$pGLOBAL_SET
000799918 980__ $$aEBOOK
000799918 980__ $$aBIB
000799918 982__ $$aEbook
000799918 983__ $$aOnline
000799918 994__ $$a92$$bISE