ライフサイエンスコーパス: aquaglyceroporin

1 y water (aquaporins) or water plus glycerol (aquaglyceroporins).

2 either directly or indirectly modulating the aquaglyceroporin.

3 er and glycerol, suggesting that PbAQP is an aquaglyceroporin.

4 ant, PtNIP1;1 has been shown to be an active aquaglyceroporin.

5 on that is mediated mainly by aquaporins and aquaglyceroporins.

6 channels, which becomes a glycine residue in aquaglyceroporins.

7 rins, and the water-plus-glycerol-conducting aquaglyceroporins.

8 teins have the conserved signature motifs of aquaglyceroporins.

9 protein showed highest homology (39-50%) to aquaglyceroporins.

10 More recently, aquaglyceroporin 2 (AQP2) loss of function was linked to

11 Aquaglyceroporin 7 (AQP7) facilitates glycerol flux acro

12 Aquaglyceroporin-9 (AQP9) facilitates diffusion of water

13 Expressed in liver, aquaglyceroporin-9 (AQP9) is permeated by glycerol, arse

14 This is the first report where a parasite aquaglyceroporin activity is post-translationally modula

15 ysiological role of glycerol transport by an aquaglyceroporin, and indicate that glycerol is a major

16 eotides was found in the gene coding for the aquaglyceroporin AQP1 in both resistant isolates.

17 We conclude that the unconventional aquaglyceroporin, AQP2, renders cells sensitive to both

18 cently, a locus encoding two closely related aquaglyceroporins, AQP2 and AQP3, was linked to MPXR in

19 Multifunctional aquaglyceroporins AQP3, AQP7, and AQP9 are permeated by

20 The related aquaglyceroporin AQP7 is required for dendritic cell che

21 In this study, the ability of mammalian aquaglyceroporins AQP7 and AQP9 to substitute for the ye

22 erial aquaglyceroporin GlpF and to mammalian aquaglyceroporins AQP7 and AQP9.

23 Here we report the presence of an aquaglyceroporin, AQP9, in mouse erythrocytes.

24 ase), the S. meliloti ars operon includes an aquaglyceroporin (aqpS) in place of arsB.

25 Aquaglyceroporin aquaporin (AQP)3 is the major glycerol

26 The aquaglyceroporins are a subfamily of aquaporins that con

27 Aquaglyceroporins are transmembrane proteins belonging t

28 ed interactions between these inhibitors and aquaglyceroporins at similar binding sites.

29 This is the first report of an aquaglyceroporin being localized to the flagellum of any

30 ls of Escherichia coli is facilitated by the aquaglyceroporin channel GlpF and that transport of Sb(I

31 The method is applied and tested on an aquaglyceroporin channel through a series of simulations

32 III), are believed to be transported through aquaglyceroporin channels as they behave as inorganic mo

33 enic resistance operon is interesting, since aquaglyceroporin channels have previously been shown to

34 n efficient water-specific AQP (ClAQP1), two aquaglyceroporins (ClGlp1 and ClGlp2) and a homolog of D

35 the aquaporins (AQPs) Drip and Prip and the aquaglyceroporins Eglp2 and Eglp4 As predicted from thei

36 the expression of the glycerol channels, or aquaglyceroporins, encoded by the aquaporin 3 (Aqp3), Aq

37 Aquaglyceroporins form the subset of the aquaporin water

38 The yeast aquaglyceroporin Fps1 is important for osmoadaptation by

39 lux, Hog1 action impedes the function of the aquaglyceroporin Fps1, in part, by displacing channel co

40 t the identification and characterization of aquaglyceroporins from Leishmania major (LmAQP1) and Lei

41 monials has a two base-pair insertion in the aquaglyceroporin gene LdAQP1 that prevents the transport

42 Disruption of FPS1, the aquaglyceroporin gene, reduced glucose-independent uptak

43 membrane protein homologous to the bacterial aquaglyceroporin GlpF and to mammalian aquaglyceroporins

44 Here, we show that the E. coli aquaglyceroporin GlpF has only little activity in lipid

45 The aquaglyceroporin GlpF is a transmembrane channel of Esch

46 Aquaglyceroporin GlpF selectively conducts water and lin

47 rmined the structure of the Escherichia coli aquaglyceroporin GlpF with bound water, in native (2.7 a

48 ly identified AQP9 inhibitor RF03176 blocked aquaglyceroporin H(2)O(2) permeability.

49 f water (aquaporins) or water plus glycerol (aquaglyceroporins) has been found in diverse life forms.

50 In other organisms, aquaglyceroporins have been shown to facilitate uptake o

51 port of the uptake of a metalloid drug by an aquaglyceroporin in Leishmania, suggesting a strategy to

52 We also demonstrate a major role for aquaglyceroporins in pentamidine and melarsoprol cross-r

53 and contribute to a set of isoform-specific aquaglyceroporin inhibitors that will facilitate the eva

54 The Leishmania major aquaglyceroporin, LmAQP1, is responsible for the transpo

55 The Leishmania major aquaglyceroporin, LmAQP1, is responsible for the transpo

56 Leishmania major aquaglyceroporin (LmjAQP1) adventitiously facilitates th

57 on-transporting principal cells, wherein the aquaglyceroporins localize to opposite plasma membranes,

58 to further characterize the function of this aquaglyceroporin membrane protein at atomic detail using

59 in TIP-like aquaporins, tryptophan found in aquaglyceroporins (NIP I), and alanine found in water-im

60 AQP9 is the major aquaglyceroporin of the epididymis, liver, and periphera

61 fied the orthologue of Plasmodium falciparum aquaglyceroporin (PfAQP) in the rodent malaria parasite,

62 Aquaporin-9, an aquaglyceroporin present in diverse tissues, is unique a

63 We hypothesize that the Plasmodium aquaglyceroporin provides the pathway for glycerol uptak

64 report the first cloning of an S. japonicum aquaglyceroporin (SjAQP) from an isolate from Jiangsu pr

65 operon was deleted and the gene for the GlpF aquaglyceroporin was disrupted (strain OSBR1).

66 Nodulin 26 is an aquaglyceroporin with a modest osmotic water permeabilit

67 This is the first report of an aquaglyceroporin with a physiological function in arseni