rdf-syntax-grammar
mods:
  schema location: http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-2.xsd
  title info:
    title: Protein Reviews - Purinergic Receptors
    sub title: Volume 20
  name:
    name part: Atassi, M. Zouhair.
    role:
      role term: editor.
    role:
      role term: edt
    role:
      role term: http://id.loc.gov/vocabulary/relators/edt
  name:
    name part: SpringerLink (Online service)
  type of resource: text
  origin info:
    place:
      place term: gw
    date issued: 2019
    edition: 1st ed. 2019.
    issuance: monographic
  language:
    language term: eng
  physical description:
    form: electronic
    form: electronic resource
    reformatting quality: access
    form: remote
    extent: VIII, 247 p. 47 illus., 46 illus. in color. online resource.
  abstract: 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, immunolo…
  table of contents: 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.
  note: edited by M. Zouhair Atassi.
  subject:
    topic: Proteins
  subject:
    topic: Protein Structure
  classification: QD431-431.7
  classification: 572.633
  related item:
    title info:
      title: Springer eBooks
  related item:
    title info:
      title: Protein Reviews, 1111
  identifier: 9783030143398
  identifier: https://doi.org/10.1007/978-3-030-14339-8
  record info:
    record creation date: 200203
    record change date: 20200203085039.0
    record identifier: 978-3-030-14339-8