Atassi | Protein Reviews - Purinergic Receptors | Buch | 978-3-030-14338-1 | sack.de

Buch, Englisch, 247 Seiten, Format (B × H): 183 mm x 260 mm, Gewicht: 693 g

Reihe: Protein Reviews

Atassi

Protein Reviews - Purinergic Receptors

Volume 20
1. Auflage 2019
ISBN: 978-3-030-14338-1
Verlag: Springer International Publishing

Volume 20

Buch, Englisch, 247 Seiten, Format (B × H): 183 mm x 260 mm, Gewicht: 693 g

Reihe: Protein Reviews

ISBN: 978-3-030-14338-1
Verlag: Springer International Publishing


The 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.
Atassi Protein Reviews - Purinergic Receptors jetzt bestellen!

Zielgruppe


Research


Autoren/Hrsg.


Weitere Infos & Material


The 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.



Ihre Fragen, Wünsche oder Anmerkungen
Vorname*
Nachname*
Ihre E-Mail-Adresse*
Kundennr.
Ihre Nachricht*
Lediglich mit * gekennzeichnete Felder sind Pflichtfelder.
Wenn Sie die im Kontaktformular eingegebenen Daten durch Klick auf den nachfolgenden Button übersenden, erklären Sie sich damit einverstanden, dass wir Ihr Angaben für die Beantwortung Ihrer Anfrage verwenden. Selbstverständlich werden Ihre Daten vertraulich behandelt und nicht an Dritte weitergegeben. Sie können der Verwendung Ihrer Daten jederzeit widersprechen. Das Datenhandling bei Sack Fachmedien erklären wir Ihnen in unserer Datenschutzerklärung.