IndraLab

Statements

PTPRC activates KCNMA1. 9 / 9
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"[XREF_BIBR] However, nonconserved substitutions of BK beta1 subunit amino acids in the vicinity of the cholane C24 carboxyl did not necessarily change LCA induced BK channel activation, [XREF_BIBR - XREF_BIBR] suggesting that the chemical requirements in the steroid lateral chain for cholanes to activate BK channels are rather lax."
22945504
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"These data are consistent with those shown in XREF_FIG and underscore that the distance between the negatively charged atom and the steroidal ring " core " is a critical determinant for effective BK channel activation by LCA and analogues."
22945504
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"These data are consistent with those shown in xref and underscore that the distance between the negatively charged atom and the steroidal ring “core” is a critical determinant for effective BK channel activation by LCA and analogues."
22945504
sparser
"In contrast to the detailed aforementioned information on the structural requirements in the LCA nucleus for BK channel activation, the chemical determinants in the steroid lateral chain that participate in BK channel activation by LCA and analogs remain to be identified."
22945504
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"LCA enhances KCa1.1 currents only when the channel contains the beta1 subunit [XREF_BIBR, XREF_BIBR, XREF_BIBR]."
27165430
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"This extremely high positive correlation, together with previous data establishing that LCA induced dilation of MCA is due to LCA activation of smooth muscle BK channels [XREF_BIBR], strongly suggest that the larger LCA induced BK channel activation in myocytes of BA or CA vs. that of ACA, MCA, PCA or MA, is an important contributor to the larger LCA induced dilation of the former group of arteries vs. the latter."
28012000
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"This LCA action is significantly larger than LCA induced BK channel activation in ACA, MCA, PCA and MA myocytes (p < 0.05)."
28012000
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"[XREF_BIBR] BK channel activation by 150 microM LCA (XREF_FIG) served as positive control."
22945504
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"LCA activates the BK channel by direct interaction with the transmembrane domain of the β1 subunit [ xref ]."
31208099