000 | 05697nam a22005655i 4500 | ||
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001 | 978-3-319-24750-2 | ||
003 | DE-He213 | ||
005 | 20180206183046.0 | ||
007 | cr nn 008mamaa | ||
008 | 151215s2016 gw | s |||| 0|eng d | ||
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_a9783319247502 _9978-3-319-24750-2 |
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050 | 4 | _aQD431-431.7 | |
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_aPSBC _2bicssc |
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_a572.633 _223 |
245 | 1 | 0 |
_aRegulation of Membrane Na+-K+ ATPase _h[recurso electrónico] / _cedited by Sajal Chakraborti, Naranjan S Dhalla. |
264 | 1 |
_aCham : _bSpringer International Publishing : _bImprint: Springer, _c2016. |
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300 |
_aXI, 436 p. 100 illus., 44 illus. in color. _bonline resource. |
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336 |
_atext _btxt _2rdacontent |
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337 |
_acomputer _bc _2rdamedia |
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_aonline resource _bcr _2rdacarrier |
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_atext file _bPDF _2rda |
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490 | 1 |
_aAdvances in Biochemistry in Health and Disease ; _v15 |
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505 | 0 | _aPart A -- 1 Na+/K+-ATPase: A Perspective -- 2 Na+/K+-ATPase and Its Role in Signal Transduction -- 3 Na+ K+-ATPase Cell Signaling Pathways and Cancer -- 4 Calcium Controls the P2-ATPase Mediated Homeostasis: Essential Role of NaAF -- 5 Na+/K+-ATPase ?4: An Isoform Dedicated to Sperm Function -- 6 The Role of the 2nd Na+ Pump in Mammals and Parasites -- 7 Myocardial Na+/K+-ATPase and SERCA: Clinical and Pathological Significance from a Cytological perspective -- 8 Understanding the Dysfunction of Na+/K+-ATPase in Rapid-Onset Dystonia- Parkinsonism and Amyotrophic Lateral Sclerosis -- 9 Activity of Membrane ATPases in Human Erythrocytes Under the Influence of Highly Hydroxylated Fullerenol -- 10 Xenobiotics-mediated Modulation of ATPases and Biomedical Implications -- 11 Emerging Role of Dysadherin in Metastasis -- 12 The Astrocytic Na+/K+-ATPase - Stimulation by Increased Extracellular K+, ?-Adrenergic Activation, Ouabain-mediated Signaling, and Interaction with the Transporter NKCC1 -- 13 Uncoupling of P-type ATPases -- 14 Phospholemman: A Brief Overview -- 15 Regulation of the Cardiac Na+/K+-ATPase by Phospholemman -- 16 Regulation of Brain Na+/K+- ATPase Activity by Noradrenaline with Particular Reference to Normal and Altered Rapid Eye Movement Sleep -- 17 Regulation Na+/K+-ATPase Activity in the Nervous System -- 18 Regulation of Membrane Na+/K+ ATPase in Health and Disease -- 19 Redox Regulation of the Na+/K+ ATPase in the Cardiovascular System -- 20 Regulation of Na+/K+-ATPase in Pulmonary Vasculature -- 21 Exercise-induced Regulation of the Na, K-pump in Skeletal Muscles -- 22 Advances in the Understanding of Renal Proximal Tubular Na+/K+-ATPase Regulation by Parathyroid Hormone and Dopamine -- 23 Regulation of Na+/ K+-ATPase in Epithelial-Mesenchymal Transition and Cancer -- 24 Metal Based Compounds, Modulators of Na+/K+-ATPase with Anticancer Activity. | |
520 | _aNa+-K+ ATPase or Na-pump ATPase, a member of ?P?-type ATPase superfamily, is characterized by association of multiple isoforms mainly of it?s ?- and ?- subunits. At present four different ?- (?-1,?-2,?-3 and ?-4) and three ?- (?-1, ?-2, and ?-3) isoforms have been identified in mammalian cells and their differential expressions are tissue specific. Regulation of Na+-K+ ATPase activity is an important but a complex process, which involves short-term and long-term mechanisms. Short-term regulation of Na+-K+ ATPase is either mediated by changes in intracellular Na+ concentrations that directly affect the Na+-pump activity or by phosphorylation/dephosphorylation-mediated by some stimulants leading to changes in its expression and transport properties. On the other hand, long-term regulation of Na+-K+ ATPase is mediated by hormones, such as mineralocorticoids and thyroid hormones, which cause changes in the transcription of genes of ?- and ?- subunits leading to an increased expression in the level of Na+-pump. Several studies have revealed a relatively new type of regulation that involves the association of small, single span membrane proteins with this enzyme. These proteins belong to the FXYD family, the members of which share a common signature sequence encompassing the transmembrane domain adjacent to the isoform(s) of ?-? subunits of Na+-K+ ATPase. Considering the extraordinary importance of Na+-K+ ATPase in cellular function, several internationally established investigators have contributed their articles in the monograph entitled ?Regulation of Membrane Na+-K+ ATPase? for inspiring young scientists and graduate students to enrich their knowledge on the enzyme, and we are sure that this book will soon be considered as a comprehensive scientific literature in the area of Na+-K+ ATPase regulation in health and disease. | ||
650 | 0 | _aLife sciences. | |
650 | 0 | _aMolecular biology. | |
650 | 0 | _aProteins. | |
650 | 0 | _aCell membranes. | |
650 | 0 | _aAtomic structure. | |
650 | 0 | _aMolecular structure. | |
650 | 0 | _aSpectra. | |
650 | 1 | 4 | _aLife Sciences. |
650 | 2 | 4 | _aProtein Structure. |
650 | 2 | 4 | _aMembrane Biology. |
650 | 2 | 4 | _aProtein Science. |
650 | 2 | 4 | _aAtomic/Molecular Structure and Spectra. |
650 | 2 | 4 | _aMolecular Medicine. |
700 | 1 |
_aChakraborti, Sajal. _eeditor. |
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700 | 1 |
_aDhalla, Naranjan S. _eeditor. |
|
710 | 2 | _aSpringerLink (Online service) | |
773 | 0 | _tSpringer eBooks | |
776 | 0 | 8 |
_iPrinted edition: _z9783319247489 |
830 | 0 |
_aAdvances in Biochemistry in Health and Disease ; _v15 |
|
856 | 4 | 0 |
_zLibro electrónico _uhttp://148.231.10.114:2048/login?url=http://dx.doi.org/10.1007/978-3-319-24750-2 |
912 | _aZDB-2-SBL | ||
942 | _cLIBRO_ELEC | ||
999 |
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