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007			cr nn 008mamaa
008			110110s2010 xxu| s |||| 0|eng d
020			_a9781441963154 _9978-1-4419-6315-4
040			_cMX-MeUAM
050		4	_aR-RZ
082	0	4	_a610 _223
100	1		_aJahn, Thomas P. _eeditor.
245	1	0	_aMIPs and Their Role in the Exchange of Metalloids _h[recurso electrónico] / _cedited by Thomas P. Jahn, Gerd P. Bienert.
264		1	_aNew York, NY : _bSpringer New York, _c2010.
300			_aXVI, 146p. 36 illus., 16 illus. in color. _bonline resource.
336			_atext _btxt _2rdacontent
337			_acomputer _bc _2rdamedia
338			_aonline resource _bcr _2rdacarrier
347			_atext file _bPDF _2rda
490	1		_aAdvances in Experimental Medicine and Biology, _x0065-2598 ; _v679
505	0		_aAquaporins: A Family of Highly Regulated Multifunctional Channels -- Phylogeny of Major Intrinsic Proteins -- Metalloids, Soil Chemistry and the Environment -- Arsenic Transport in Prokaryotes and Eukaryotic Microbes -- Metalloid Transport by Aquaglyceroporins: Consequences in the Treatment of Human Diseases -- Roles of Vertebrate Aquaglyceroporins in Arsenic Transport and Detoxification -- Molecular Mechanisms of Boron Transport in Plants: Involvement of Arabidopsis NIP5;1 and NIP6;1 -- Silicon Transporters in Higher Plants -- Major Intrinsic Proteins and Arsenic Transport in Plants: New Players and Their Potential Role -- Major Intrinsic Proteins in Biomimetic Membranes.
520			_aSixteen years have passed since human aquaporin-1 (AQP1) was discovered as the first water channel, facilitating trans-membrane water fluxes. Subsequent years of research showed that the water channel AQP1 was only the tip of an iceberg; the iceberg itself being the ubiquitous super family of membrane intrinsic proteins (MIPs) that facilitate trans-membrane transport of water and an increasing number of small, water-soluble and uncharged compounds. Here we introduce you to the superfamily of MIPs and provide a summary about our gradually refined understanding of the phylogenetic relationship of its members. This volume is dedicated to the metalloids, a recently discovered group of substrates for a number of specific MIPs in a diverse spectrum of organisms. Particular focus is given to the essential boron, the beneficial silicon and the highly toxic arsenic. The respective MIP isoforms that facilitate the transport of these metalloids include members from several clades of the phylogenetic tree, suggesting that metalloid transport is an ancient function within this family of channel proteins. Among all the various substrates that have been shown to be transported by MIPs, metalloids take an outstanding position. While water transport seems to be a common function of many MIPs, single isoforms in plants have been identified as being crucially important for the uptake of boric acid as well as silicic acid. Here, the function seems not to be redundant, as mutations in those genes render plants deficient in boron and silicon, respectively.
650		0	_aMedicine.
650	1	4	_aBiomedicine.
650	2	4	_aBiomedicine general.
700	1		_aBienert, Gerd P. _eeditor.
710	2		_aSpringerLink (Online service)
773	0		_tSpringer eBooks
776	0	8	_iPrinted edition: _z9781441963147
830		0	_aAdvances in Experimental Medicine and Biology, _x0065-2598 ; _v679
856	4	0	_zLibro electrónico _uhttp://148.231.10.114:2048/login?url=http://link.springer.com/book/10.1007/978-1-4419-6315-4
596			_a19
942			_cLIBRO_ELEC
999			_c199505 _d199505