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020			_a9789811556524
024	7		_a10.1007/978-981-15-5652-4 _2doi
040			_aES-MaUEC _bspa _cES-MaUEC _dES-MaUEC
050		4	_aQH450 _b2020 EB
100	1		_aKim, Cheorl-Ho _eautor _4http://id.loc.gov/vocabulary/relators/aut _0http://id.loc.gov/authorities/names/n2013181486 _1http://viaf.org/viaf/306102337 _9675282
245	1	0	_aGM3 Signaling _cby Cheorl-Ho Kim
250			_aFirst edition
264		1	_aSingapore _bSpringer _c2020
300			_a1 recurso en línea (VII, 138 páginas) _b32 ilustraciones, 26 ilustraciones a color
336			_2rdacontent _aTexto _btxt
337			_2rdamedia _aelectrónico _bc
338			_2rdacarrier _arecurso electrónico _bcr
347			_aArchivo de texto _bPDF
490	0		_aBiomedical and Life Sciences (SpringerNature-11642)
490	0		_aBiomedical and Life Sciences (R0) (SpringerNature-43708)
505	0		_a1. History of sialic acids, gangliosides and GM3 -- 2. Synthesis of GM3 -- 3. Molecular localization of GM3 in cells -- 4. Basic function of GM3 as an interacting molecule -- 5. GD3 mimetics with a neurite forming capacity -- 6. GM3 as a pathogenic infection receptor -- 7. GM3 and related gangliosides prevent inflammation and atherosclerosis -- 8. GM3 has an anti-tumor capacity -- 9. GM3 suppresses tumor angiogenesis -- 10. Interaction between EGFR and GM3 -- 11. Membrane ganglioside-specific neuraminidase 3 (NEU3) regulates GM3 signaling -- 12. Regulation of GM3-mediated EGFR signaling by NEU3 sialidase -- 13. VEGFR-GM3 interaction in angiogenesis -- 14. GM3, competing with GM1, interaction with urokinase plasminogen activator receptor (uPAR) in endothelial caveolar-lipid rafts inhibits angiogenesis -- 15. GM3 interacts with TGFβ Rs in the epithelial-mesenchymal transition (EMT) during posterior capsular opacification (PCO) formation -- 16. Galectin-1 promotes tumor growth and escapes immune surveillance -- 17. GM3-HGFR, FGFR and PDGFR cancer cell behavior, and IGF-1R in diabetic wound healing -- 18. GM3, caveolin-1 and insulin receptor in insulin resistance -- 19. GM3 suppresses arthritis -- 20. GM3 protects cochlear hair cells and hearing from corti degeneration -- 21. GM3 increases osteoclast differentiation via direct GM3 cooperation with RANKL and IGF-1 -- 22. GM3 in leukemic cells into terminal differentiation -- 23. α2,3-Sialyllactose (3SL) or α2,6-sialyllactose (6SL) of GM3 glycan in innate immunity. .
520			_aThis book reviews recent progress in understanding of the signaling and biochemistry of GM3 ganglioside in eukaryotic cells. GM3 is the simplest of the gangliosides and the precursor of other gangliosides. It is expressed in the outer leaflet of plasma cell membranes and has roles in the recognition, interaction, binding, adhesion, and motility of cells. In addition, GM3 has been documented to have functional roles in cell migration, proliferation, senescence, and apoptosis. The full range of topics of interest are addressed in the book. The early chapters discuss the synthesis of GM3, its molecular localization in cells, and its basic function as an interacting molecule. The ways in which GM3 exerts its effects via various growth factor receptors are fully explored. Current knowledge of the part played by GM3 in health and disease is discussed in depth. For example, its roles in preventing inflammation, inhibiting tumor angiogenesis and tumor growth, and suppressing arthritis are highlighted, and attention drawn to the significance of GM3 as a driver of impaired wound healing in diabetics. The book will be of interest to all who want a comprehensive update on research in this field.
988			_aSpringer_Biomedlife_03082020
650		7	_2embne _9162770 _aExpresión génica
650		7	_2embne _aCáncer _xInvestigación _9182523
776	0	8	_iPrinted edition: _z9789811556517
776	0	8	_iPrinted edition: _z9789811556531
776	0	8	_iPrinted edition: _z9789811556548
856	4	0	_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://doi.org/10.1007/978-981-15-5652-4 _zAcceso a este recurso digital (usuarios Universidad Europea de Madrid)
942			_2lcc _cLE
998			_b08/2020 _dz _ek _zSI