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

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/00216208:11320/24:10493303

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

C - Kapitola v odborné knize

CEP obor

—

OECD FORD obor

30103 - Neurosciences (including psychophysiology)

Projekt

<a href="/cs/project/GA22-13750S" target="_blank" >GA22-13750S: Signální dráhy ovlivňující funkci lidského TRPC5 receptoru: predikce jejich vztahu k bolesti při revmatoidní artritidě</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2024

Kód důvěrnosti údajů

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

Název knihy nebo sborníku

Macromolecular Protein Complexes V : Structure and Function

ISBN

978-3-031-58842-6

Počet stran výsledku

38

Strana od-do

207-244

Počet stran knihy

563

Název nakladatele

Springer

Místo vydání

Cham

Kód UT WoS kapitoly

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