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008			200203s2019 gw a o |||| 0|eng d
020			_a9783030143398
024	7		_a10.1007/978-3-030-14339-8 _2doi
040			_aES-MaUEC _bspa _cES-MaUEC _dES-MaUEC
050		4	_aQP551 _b2019 EB
245	0	0	_aProtein Reviews - Purinergic Receptors _bVolume 20 _cedited by M. Zouhair Atassi.
250			_aFirst edition
264		1	_aCham, Switzerland _bSpringer International Publishing _c2019
300			_a1 recurso en línea (VIII, 247 páginas) _b47 ilustraciones, 46 ilustraciones a color
336			_2rdacontent _aTexto _btxt
337			_2rdamedia _aelectrónico _bc
338			_2rdacarrier _arecurso electrónico _bcr
347			_atext file _bPDF
490	0		_aProtein Reviews _x2520-1891 _v1111
490	0		_aBiomedical and Life Sciences (Springer-11642)
505	0		_aThe phox homology (PX) domain -- The Modeling of PH domains/phosphoinositides Interactions and beyond -- BAR domain proteins regulate Rho GTPase signaling -- AP180 N-terminal Homology (ANTH) and Epsin N-terminal Homology (ENTH) Domains: Physiological Functions and Involvement in Disease -- Polyphosphoinositide-Binding Domains: Insights from Peripheral Membrane and Lipid-Transfer Proteins -- Physiological functions of phosphoinositide-modifying enzymes and their interacting proteins in Arabidopsis -- Molecular mechanisms of vaspin action - from adipose tissue to skin and bone, from blood vessels to the brain -- Exceptionally selective substrate targeting by the metalloprotease anthrax lethal factor -- Salmonella, E. coli, and Citrobacter type III secretion system effector proteins that alter host innate immunity -- New techniques to study intracellular receptors in living cells: Insights into RIG-I-like receptor signaling.
520	3		_aThe Protein Reviews series serves as a publication vehicle for reviews that focus on crucial contemporary and vital aspects of protein structure, function, evolution and genetics. Volume 20, Purinergic Receptors, has ten chapters. The first five chapters deal with various aspects of membrane binding. The first chapter focuses on the phox-homology (PX) domain, which is a phosphoinositide-binding domain conserved in all eukaryotes and present in forty-nine human proteins. The next chapter deals with the modeling of PH domains/phosphoinositides interactions. This is followed by a chapter on BAR domain proteins regulate Rho GTPase signaling. The BAR (Bin-Amphiphysin-Rvs) domain is a membrane lipid binding domain present in a wide variety of proteins, often proteins with a role in Rho-regulated signaling pathways. The fourth article presents AP180 N-terminal homology (ANTH) and Epsin N-terminal homology (ENTH) domains and discusses their physiological functions and involvement in disease. The fifth article reviews the polyphosphoinositide-binding domains and presents insights from peripheral membrane and lipid-transfer proteins. This is followed by a chapter on the physiological functions of phosphoinositide-modifying enzymes and their interacting proteins in Arabidopsis, then by a chapter on the molecular mechanisms of Vaspin action in various tissues such as adipose tissue, skin, bone, blood vessels, and the brain. The eighth chapter deals with exceptionally selective substrate targeting by the metalloprotease anthrax lethal factor followed by an article on Salmonella, E. coli, and Citrobacter type III secretion system effector proteins that alter host innate immunity. The last chapter presents New techniques to study intracellular receptors in living cells, with insights into RIG-I-like receptor signaling. Volume 20 is intended for research scientists, clinicians, physicians and graduate students in the fields of biochemistry, cell biology, molecular biology, immunology and genetics.
988			_aPrimersemestre_2020_BiomedLife
650		7	_aProteínas _2embne _9139861
700	1		_aAtassi, M. Zouhair _eeditor literario _4edt _4http://id.loc.gov/vocabulary/relators/edt
773	0		_tSpringer eBooks
776	0	8	_iPrinted edition: _z9783030143381
776	0	8	_iPrinted edition: _z9783030143404
776	0	8	_iPrinted edition: _z9783030143411
856	4	0	_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://doi.org/10.1007/978-3-030-14339-8 _zAcceso a este recurso digital (usuarios Universidad Europea de Madrid)
942			_2lcc _cLE _n0
998			_b03/2020 _dz _ek _zSI