The effect of the interaction between aquaporin 0 (AQP0) and the filensin tail region on AQP0 water permeability
about
Biological significance and topological basis of aquaporin-partnering protein-protein interactionsAquaporins in the eye: expression, function, and roles in ocular diseaseHarpin Hpa1 Interacts with Aquaporin PIP1;4 to Promote the Substrate Transport and Photosynthesis in Arabidopsis.The water permeability of lens aquaporin-0 depends on its lipid bilayer environment.Intact and N- or C-terminal end truncated AQP0 function as open water channels and cell-to-cell adhesion proteins: end truncation could be a prelude for adjusting the refractive index of the lens to prevent spherical aberration.Identification of a direct Aquaporin-0 binding site in the lens-specific cytoskeletal protein filensin.Aqp0a Regulates Suture Stability in the Zebrafish Lens.
P2860
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P2860
The effect of the interaction between aquaporin 0 (AQP0) and the filensin tail region on AQP0 water permeability
description
2011 nî lūn-bûn
@nan
2011年の論文
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2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
The effect of the interaction ...... ion on AQP0 water permeability
@ast
The effect of the interaction ...... ion on AQP0 water permeability
@en
type
label
The effect of the interaction ...... ion on AQP0 water permeability
@ast
The effect of the interaction ...... ion on AQP0 water permeability
@en
prefLabel
The effect of the interaction ...... ion on AQP0 water permeability
@ast
The effect of the interaction ...... ion on AQP0 water permeability
@en
P2093
P2860
P1433
P1476
The effect of the interaction ...... ion on AQP0 water permeability
@en
P2093
Akiko Mitsuishi
Emi Nakashima
Katsuya Furuki
Makoto Takehana
Mikako Oka
Yosuke Nakazawa
P2860
P304
P577
2011-12-13T00:00:00Z