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1 mber), and increased sodium tolerance (yeast TMEM16).
2 lso expressed in these cells, while TMEM16B, TMEM16D and TMEM16E were all at least 50 times less abun
3 ther family members, such as TMEM16C (ANO3), TMEM16D (ANO4), TMEM16F (ANO6), TMEM16G (ANO7) and TMEM1
7 he structural basis of anion conduction in a TMEM16 channel and it defines the foundation for the div
12 ng and validated the idea that ions permeate TMEM16 Cl(-) channels via a structurally homologous path
13 ts, the anoctamin family (ANO, also known as TMEM16) exhibits characteristics most similar to those e
14 Whether distant relatives of the vertebrate TMEM16 families also form CaCCs is an intriguing open qu
15 elated calcium-activated ion channels in the TMEM16 family and conducting systematic mutagenesis of a
17 and SCN2A (rs3769955: P = 3.1 x 10(-10)), a TMEM16 family gene (ANO3; rs114444506: P = 3.7 x 10(-20)
19 EM16E), aberrant X segregation (a Drosophila TMEM16 family member), and increased sodium tolerance (y
20 s mutant, the first knockout of a vertebrate TMEM16 family member, provides a mouse model of tracheom
29 underlies the evolutionary divergence of the TMEM16 family, and that other homologues, such as TMEM16
30 chemistry facilitate lipid permeation in the TMEM16 family, and we hypothesize that membrane interact
35 emain to be elucidated and the links between TMEM16 functions and human physiology and pathologies ne
37 The recent identification of an ancestral TMEM16 homologue with intrinsic channel and scramblase a
38 gated channel, with characteristics of other TMEM16 homologues, and a Ca(2+)-dependent scramblase, wi
39 roteins in yeast: Ist2 (related to mammalian TMEM16 ion channels), the tricalbins (Tcb1/2/3, ortholog
40 structure of the fungal Nectria haematococca TMEM16 (nhTMEM16) scramblase suggested a putative mechan
41 ctamin 1), a member of the transmembrane 16 (TMEM16) protein family, forms CaCCs in pulmonary artery
43 sults suggest cooperative roles for CLCA and TMEM16 proteins in influencing the physiology of multipl
44 tions that alter ion channel activity of the TMEM16 proteins localize around the groove, it was sugge
46 ly to be a general functional feature of the TMEM16 scramblases and therefore of general importance i
48 y members of the anoctamin (Ano, also called Tmem16) superfamily, but the mechanisms of Ano1 gating b
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