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| 008 | 170920s2017 si o 000 0 eng d | ||
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_a9789811025136 _q(electronic bk.) |
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_aQP609.P78 _b2017 EB |
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| 245 | 0 | 0 |
_aProteases in physiology and pathology _cSajal Chakraborti, Naranjan S. Dhalla, editors. |
| 264 | 1 |
_aSingapore _bSpringer International Publishing _c2017 |
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| 300 | _a1 recurso en línea | ||
| 336 |
_aTexto _btxt _2rdacontent |
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| 337 |
_aelectrónico _bc _2rdamedia |
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| 338 |
_arecurso electrónico _bcr _2rdacarrier |
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| 347 |
_atext file _bPDF |
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| 500 |
_a _bSpringer Biomedical and Life Sciences eBooks 2017 English+International |
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| 505 | 0 | _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 | |
| 505 | 8 | _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 | |
| 505 | 8 | _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 | |
| 505 | 8 | _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 | |
| 505 | 8 | _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 | |
| 520 | 3 | _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. | |
| 650 | 7 |
_aEnzimas _2embne _0(OCoLC)fst01079783 _0 _9138640 |
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| 700 | 1 |
_aChakraborti, Sajal. _984935 |
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| 700 | 1 |
_aDhalla, Naranjan S. _984616 |
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| 856 | 4 | 0 |
_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=http://link.springer.com/10.1007/978-981-10-2513-6 _zAcceso a este recurso digital (usuarios Universidad Europea de Madrid) |
| 988 | _aEBOOK, asignarmaterias, EBSPRINGER_2017 | ||
| 998 |
_b02/2018 _dz _e- _zSI |
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| 999 |
_c96524 _d96524 _x1 |
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