The C-terminal basic residues contribute to the chemical- and voltage-dependent activation of TRPA1.
about
Structure of the TRPA1 ion channel suggests regulatory mechanismsSpecies-specific temperature sensitivity of TRPA1Warmth suppresses and desensitizes damage-sensing ion channel TRPA1Activation of Transient Receptor Potential Ankyrin-1 by Insoluble Particulate Material and Association with AsthmaSensitization of TRPA1 by Protein Kinase AC-terminal acidic cluster is involved in Ca2+-induced regulation of human transient receptor potential ankyrin 1 channel.The Outer Pore and Selectivity Filter of TRPA1The transient receptor potential channel TRPA1: from gene to pathophysiology.Genetic variants affecting human TRPA1 or TRPM8 structure can be classified in vitro as 'well expressed', 'poorly expressed' or 'salvageable'.The molecular basis for species-specific activation of human TRPA1 protein by protons involves poorly conserved residues within transmembrane domains 5 and 6.Possible involvement of transient receptor potential ankyrin 1 in Ca2+ signaling via T-type Ca2+ channel in mouse sensory neurons.Regulation of the transient receptor potential channel TRPA1 by its N-terminal ankyrin repeat domain.
P2860
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P2860
The C-terminal basic residues contribute to the chemical- and voltage-dependent activation of TRPA1.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
The C-terminal basic residues ...... dependent activation of TRPA1.
@en
type
label
The C-terminal basic residues ...... dependent activation of TRPA1.
@en
prefLabel
The C-terminal basic residues ...... dependent activation of TRPA1.
@en
P2093
P2860
P50
P356
P1433
P1476
The C-terminal basic residues ...... -dependent activation of TRPA1
@en
P2093
Abdul Samad
Jan Benedikt
Jan Teisinger
Lucie Sura
P2860
P304
P356
10.1042/BJ20101256
P407
P577
2011-01-01T00:00:00Z