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000928502 019__ $$a1140382441$$a1142703380
000928502 020__ $$a9783030143398
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000928502 0247_ $$a10.1007/978-3-030-14339-8$$2doi
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000928502 24500 $$aProtein reviews.$$nVolume 20,$$pPurinergic receptors /$$cM. Zouhair Atassi, editor.
000928502 24630 $$aPurinergic receptors
000928502 260__ $$aCham :$$bSpringer,$$c2020.
000928502 300__ $$a1 online resource (252 pages).
000928502 336__ $$atext$$btxt$$2rdacontent
000928502 337__ $$acomputer$$bc$$2rdamedia
000928502 338__ $$aonline resource$$bcr$$2rdacarrier
000928502 347__ $$atext file$$bPDF$$2rda
000928502 4901_ $$aAdvances in Experimental Medicine and Biology Ser. ;$$vv.1111
000928502 500__ $$aIncludes index.
000928502 5050_ $$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.
000928502 506__ $$aAccess limited to authorized users.
000928502 520__ $$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.
000928502 588__ $$aDescription based on print version record.
000928502 650_0 $$aPurines$$xReceptors.
000928502 7001_ $$aAtassi, M. Zouhair,$$eeditor.
000928502 77608 $$iPrint version:$$aAtassi, M. Zouhair$$tProtein Reviews - Purinergic Receptors : Volume 20$$dCham : Springer International Publishing AG,c2020$$z9783030143381
000928502 830_0 $$aAdvances in experimental medicine and biology.$$pProtein reviews ;$$vv. 1111.
000928502 852__ $$bebk
000928502 85640 $$3SpringerLink$$uhttps://univsouthin.idm.oclc.org/login?url=http://link.springer.com/10.1007/978-3-030-14339-8$$zOnline Access$$91397441.1
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