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1 rsion of exogenously added big endothelin-1 (big ET-1) to ET-1 in subcellular fractions obtained by s
2 ne systemic hemodynamics and plasma ET-1 and big ET-1 concentrations were measured using electrical b
7 indicate that there is an increase in ET and big ET-1 associated with fully developed atherosclerotic
10 is a bona fide activating protease for both big ET-1 and big ET-3 in vivo, and that the cell-cell co
12 , and, to a much lesser extent, also cleaved big ET-1 and big ET-2 at Trp(21)-Val(22), yielding ET-1
15 aled intense immunofluorescence staining for big ET-1 and the 2 isoforms of ECE-1 (ECE-1alpha and ECE
17 efficient hydrolysis of the W21-V22 bond in big ET-1 and which have the sequence QTVP in big ET-3.
18 which has a loop for residues 27-30 (HVVP in big ET-1), which have previously been demonstrated to be
19 eta resulted in an increase in intracellular big ET-1 and a decrease in SMC from the main artery.
20 tracellular site involved in the cleavage of big ET-1 to the biologically active peptide ET-1 by dete
21 nted cGMP, would inhibit ECE-1 conversion of big ET-1 to active ET-1, thus reducing tissue ET-1 conce
23 caused by intravenous infusion of Ang II or big ET-1 to a greater extent and with longer duration th
27 vesicles with a possible role in processing big ET-1 while in transit to the cell surface via the co
28 The findings of this study indicate that big ET-1 is processed to the mature vasoactive peptide b
31 logy modeling were used to determine whether big ET-1 and big ET-3 adopt similar secondary and tertia
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