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1  length 5'-AQP2-5 kb spacer-AQP5-7 kb spacer-AQP6-3'.
2                                              AQP6 colocalizes with H+-ATPase in intracellular vesicle
3    When expressed in Xenopus laevis oocytes, AQP6 exhibits low basal water permeability; however, whe
4                     Unlike other aquaporins, AQP6 functions not as a water channel but as an anion-se
5 is indicated the presence of AQP2, AQP5, and AQP6 genes, but not AQP0.
6   Uniquely, all known mammalian orthologs of AQP6 have an asparagine residue (Asn-60) at the position
7 ly related aquaporins (AQP0, AQP2, AQP5, and AQP6) have been mapped to chromosome band 12q13, suggest
8 g a polyclonal antibody to the C terminus of AQP6, immunoblots revealed a major 30-kDa band in membra
9 AQP2, AQP3, and AQP4 in the collecting duct; AQP6 in the papilla; and AQP7 in the proximal tubule.
10                         In proximal tubules, AQP6 is also abundant in membrane vesicles within the su
11                            Here we show that AQP6 is functionally distinct from other known aquaporin
12                            Here we show that AQP6 is localized exclusively in intracellular membranes
13 n microscopic studies confirmed that >98% of AQP6 is located in intracellular membrane vesicles.
14 iple types of renal epithelia indicates that AQP6 is not simply involved in transcellular fluid absor
15                                In glomeruli, AQP6 is present in membrane vesicles within podocyte cel
16 ieved to be located in plasma membranes, rat AQP6 is restricted to intracellular vesicles in renal ep
17  at the contact point between TM2 and TM5 in AQP6 may function as a teeter board needed for rapid str
18 l inhibitor, Hg2+, the water permeability of AQP6 oocytes rapidly rises up to tenfold and is accompan
19 tance is rapidly and reversibly activated in AQP6 oocytes.
20           Moreover, our studies predict that AQP6 participates in distinct physiological functions su
21                          In collecting duct, AQP6 resides in intracellular membrane vesicles in apica
22 ion of rat kidney homogenates confirmed that AQP6 resides predominantly in vesicular fractions, and i
23           Single-channel analyses have shown AQP6 to flicker rapidly between closed and open status.
24 t a single residue substitution (N60G in rat AQP6) totally eliminates the anion permeability of AQP6
25 totally eliminates the anion permeability of AQP6 when expressed in Xenopus oocytes, but the N60G ooc

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