ライフサイエンスコーパス: aquaporin 0

1 d gamma-crystallins, filensin, CP49, and MIP/aquaporin 0.

2 esembling the phenotype reported for altered aquaporin-0 activity without detectable cytotoxic effect

3 differentiation, including Prox1, p57(KIP2), aquaporin 0 and beta-crystallins.

4 he intracellular/canalicular localization of aquaporins 0 and 8 and the basolateral localization of a

5 ractions of hepatocytes showed enrichment of aquaporins 0 and 8 in microsomes and canalicular plasma

6 a membrane; the subcellular distributions of aquaporins 0 and 9 were unaffected.

7 er channel, the major intrinsic protein (the aquaporin 0); and a cotransporter, the Na+/glucose cotra

8 proteins in the eye lens, the water channel aquaporin-0 (AQP-0) and the connexins Cx46 and Cx50, are

9 t was shown that RD alters the expression of aquaporin-0 (AQP-0), and this modulation is prevented by

10 ility of the curvature-neutral water channel aquaporin 0 (AQP0) is insensitive to it.

11 Aquaporin 0 (AQP0) is the major intrinsic protein in the

12 We determined the x-ray structure of bovine aquaporin 0 (AQP0) to a resolution of 2.2 A.

13 Aquaporin 0 (AQP0), a lens-specific membrane protein, is

14 Aquaporin 0 (AQP0), also known as major intrinsic protei

15 Aquaporin 0 (AQP0), the major intrinsic protein of the e

16 Aquaporin 0 (AQP0), the most abundant membrane protein i

17 Aquaporin 0 (AQP0), the most abundant membrane protein i

18 turnover in fiber cells of the ocular lens, Aquaporin 0 (AQP0), the most abundant membrane protein i

19 Lens-specific aquaporin-0 (AQP0) functions as a specific water pore an

20 Aquaporin-0 (AQP0) is a tetrameric membrane protein and

21 Aquaporin-0 (AQP0) is the major intrinsic protein of len

22 Aquaporin-0 (AQP0) is the most prevalent intrinsic prote

23 The lens-specific water pore aquaporin-0 (AQP0) is the only aquaporin known to form m

24 c studies of the lens-specific water channel aquaporin-0 (AQP0) revealed atomistic views of such inte

25 Aquaporin-0 (AQP0) tetramers form square arrays in lens

26 mbranes with a high density of reconstituted aquaporin-0 (AQP0) water channels.

27 ave previously described the interactions of aquaporin-0 (AQP0) with dimyristoyl phosphatidylcholine

28 altered alphaA-crystallin membrane protein (aquaporin-0 (AQP0), a specific lens membrane protein) in

29 Major intrinsic protein (MIP), also known as aquaporin-0 (AQP0), is the most abundant membrane protei

30 Aquaporin-0 (AQP0), previously known as major intrinsic

31 demonstrates that mutations in two zebrafish aquaporin 0s, Aqp0a and Aqp0b, alter water state and mac

32 ns in hepatocytes (aquaporin 8 aquaporin 9 > aquaporin 0) by reverse transcription-polymerase chain r

33 ion of expression, activity and stability of aquaporin-0, connexins, cytoskeletal proteins, and the m

34 Aquaporin-0 exists as a 113 kDa tetramer, with each subu

35 ertebrate lens, otherwise known as MIP26 and Aquaporin 0, is abundantly expressed as a lens fiber mem

36 Major intrinsic protein (MIP), also called aquaporin-0, is essential for lens transparency and is s

37 reated lenses was preceded by an increase in aquaporin-0 serine-235 phosphorylation and levels of con

38 a tetrameric alpha-helical membrane channel (Aquaporin-0) solubilized by n-Dodecyl beta-D-Maltoside a

39 yl beta-d-maltopyranoside corona surrounding aquaporin-0, the most abundant membrane protein of the e

40 romolecular crowding with in vivo studies of aquaporin 0 zebrafish mutants that disrupt its regulatio