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1 corroborated that amino acids present within AQP6(194-213) of AQP6 loop C contribute to intracellular
4 When expressed in Xenopus laevis oocytes, AQP6 exhibits low basal water permeability; however, whe
7 Uniquely, all known mammalian orthologs of AQP6 have an asparagine residue (Asn-60) at the position
8 ly related aquaporins (AQP0, AQP2, AQP5, and AQP6) have been mapped to chromosome band 12q13, suggest
9 g a polyclonal antibody to the C terminus of AQP6, immunoblots revealed a major 30-kDa band in membra
11 AQP2, AQP3, and AQP4 in the collecting duct; AQP6 in the papilla; and AQP7 in the proximal tubule.
12 The inability to over-express Aquaporin 6 (AQP6) in the plasma membrane of heterologous cells has h
17 iple types of renal epithelia indicates that AQP6 is not simply involved in transcellular fluid absor
19 ieved to be located in plasma membranes, rat AQP6 is restricted to intracellular vesicles in renal ep
20 amino acids present within AQP6(194-213) of AQP6 loop C contribute to intracellular endoplasmic reti
21 at the contact point between TM2 and TM5 in AQP6 may function as a teeter board needed for rapid str
22 l inhibitor, Hg2+, the water permeability of AQP6 oocytes rapidly rises up to tenfold and is accompan
26 ion of rat kidney homogenates confirmed that AQP6 resides predominantly in vesicular fractions, and i
27 we have identified a region within loop C of AQP6 that is responsible for severely hampering plasma m
29 t a single residue substitution (N60G in rat AQP6) totally eliminates the anion permeability of AQP6
30 totally eliminates the anion permeability of AQP6 when expressed in Xenopus oocytes, but the N60G ooc