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1 PEPD binds to the proline-rich domain in p53, which inhi
2 PEPD differs from all known EGFR ligands in that it does
3 PEPD mutations also increase resurgent currents, which i
4 PEPD mutations impair Nav1.7 fast inactivation and incre
5 PEPD mutations in the putative inactivation gate have be
7 enotype with characteristics of both IEM and PEPD and show that this mutation renders DRG and trigemi
9 ges in channel function seen in both IEM and PEPD mutations: A1632E hyperpolarizes (-7 mV) the voltag
10 patient with overlapping symptoms of IEM and PEPD was reported, displaying a shift of both activation
11 al phenotype with characteristics of IEM and PEPD, with an alanine 1632 substitution by glutamate (A1
13 disruption of the fast-inactivated state by PEPD mutations can be more moderate than previously indi
17 known as Xaa-Pro dipeptidase or peptidase D (PEPD), is a ubiquitously expressed cytosolic enzyme that
19 ted that a paroxysmal extreme pain disorder (PEPD) mutation in the human peripheral neuronal sodium c
20 syndrome, paroxysmal extreme pain disorder (PEPD), characterized by rectal, periocular, and perimand
21 (IEM) and paroxysmal extreme pain disorder (PEPD), enhance Nav1.7 function via distinct mechanisms.
26 nherited "paroxysmal extreme pain disorder" (PEPD) differs in its clinical picture and affects proxim
29 doxorubicin and H2O2 each must free p53 from PEPD in order to achieve robust p53 activation, which is
31 nt non-PEPD mutation (V1300F) and the I1461T PEPD mutation, located in the putative inactivation gate
33 d their effects on gating to an adjacent non-PEPD mutation (V1300F) and the I1461T PEPD mutation, loc
36 We speculated that selective attenuation of PEPD-enhanced resurgent currents might contribute to thi
40 e viral IFN-I antagonist, NS5, to prolidase (PEPD), a cellular dipeptidase implicated in primary immu
41 nctionally characterized two of the D3/S4-S5 PEPD mutations (V1298F and V1299F) and compared their ef
42 leavage of procaspase-9 at the cleavage site PEPD(315) to yield the large (p35) and small (p12) caspa
43 present in the extracellular space, but that PEPD is released from injured cells and tissues and that
44 n this article, however, we demonstrate that PEPD directly binds to and activates epidermal growth fa
46 93 cells expressing wild-type Nav1.7 and the PEPD mutants T1464I and M1627K, we examined the effects
53 t with biophysical characteristics common to PEPD (impaired fast inactivation) and IEM (hyperpolarize
57 .7 function due to mutations associated with PEPD, but not IEM, are important in I(NaR) generation, s
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