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1 ause of the frequent loss of function of the von Hippel-Lindau tumor suppressor protein.
2 okine signaling (SOCS)-box proteins, and the von Hippel-Lindau tumor suppressor protein.
4 D184161 also increased HIF-1alpha binding to von Hippel-Lindau tumor suppressor protein, an E3 ligase
5 than the nucleus, where it co-localized with von Hippel-Lindau tumor suppressor protein and the HIF h
6 f HIF-1 is required for its binding with the von Hippel-Lindau tumor suppressor protein and the subse
11 f the HIF-1alpha pathway through deletion of von Hippel-Lindau tumor-suppressor protein or pharmacolo
13 bers of oxygen-sensing pathway including the von Hippel-Lindau tumor suppressor protein (pVHL) and th
26 stinal epithelium-specific disruption of the von Hippel-Lindau tumor suppressor protein (VHL) resulte
27 ha subunits of HIF allows recognition by the von Hippel-Lindau tumor suppressor protein (VHL), a comp
28 echnology, intestinal-specific disruption of von Hippel-Lindau tumor suppressor protein (Vhl), hypoxi
29 ne-specific disruption of genes encoding the von Hippel-Lindau tumor suppressor protein (Vhl), hypoxi
31 conditions, HIF-1alpha is recognized by the von Hippel-Lindau tumor-suppressor protein (VHL), a comp
33 entas did not differ, but HIF-1alpha and the von Hippel-Lindau tumor suppressor protein were overexpr
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