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Human Transient Receptor Potential Ankyrin 1 Channel: Structure, Function, and Physiology

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985823%3A_____%2F24%3A00602777" target="_blank" >RIV/67985823:_____/24:00602777 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216208:11320/24:10493303

  • Result on the web

    <a href="https://doi.org/10.1007/978-3-031-58843-3_10" target="_blank" >https://doi.org/10.1007/978-3-031-58843-3_10</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1007/978-3-031-58843-3_10" target="_blank" >10.1007/978-3-031-58843-3_10</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Human Transient Receptor Potential Ankyrin 1 Channel: Structure, Function, and Physiology

  • Original language description

    The transient receptor potential ion channel TRPA1 is a Ca2+-permeable nonselective cation channel widely expressed in sensory neurons, but also in many nonneuronal tissues typically possessing barrier functions, such as the skin, joint synoviocytes, cornea, and the respiratory and intestinal tracts. Here, the primary role of TRPA1 is to detect potential danger stimuli that may threaten the tissue homeostasis and the health of the organism. The ability to directly recognize signals of different modalities, including chemical irritants, extreme temperatures, or osmotic changes resides in the characteristic properties of the ion channel protein complex. Recent advances in cryo-electron microscopy have provided an important framework for understanding the molecular basis of TRPA1 function and have sug¬gested novel directions in the search for its pharmacological regulation. This chap¬ter summarizes the current knowledge of human TRPA1 from a structural and functional perspective and discusses the complex allosteric mechanisms of activa¬tion and modulation that play important roles under physiological or pathophysio¬logical conditions. In this context, major challenges for future research on TRPA1 are outlined.

  • Czech name

  • Czech description

Classification

  • Type

    C - Chapter in a specialist book

  • CEP classification

  • OECD FORD branch

    30103 - Neurosciences (including psychophysiology)

Result continuities

  • Project

    <a href="/en/project/GA22-13750S" target="_blank" >GA22-13750S: Signaling pathways affecting human TRPC5 receptor function: Prediction of their association with rheumatoid arthritis pain</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2024

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Book/collection name

    Macromolecular Protein Complexes V : Structure and Function

  • ISBN

    978-3-031-58842-6

  • Number of pages of the result

    38

  • Pages from-to

    207-244

  • Number of pages of the book

    563

  • Publisher name

    Springer

  • Place of publication

    Cham

  • UT code for WoS chapter