Allosteric mechanism of water-channel gating by Ca2+–calmodulin
about
X-ray structure of human aquaporin 2 and its implications for nephrogenic diabetes insipidus and traffickingFragment Screening of Human Aquaporin 1Variability of Protein Structure Models from Electron Microscopy.The aquaporin zero puzzle.Calmodulin and PI(3,4,5)P₃ cooperatively bind to the Itk pleckstrin homology domain to promote efficient calcium signaling and IL-17A production.The pilus usher controls protein interactions via domain masking and is functional as an oligomer.Plasma Membrane Abundance of Human Aquaporin 5 Is Dynamically Regulated by Multiple Pathways.MALDI Imaging Mass Spectrometry Spatially Maps Age-Related Deamidation and Truncation of Human Lens Aquaporin-0.Auto-Adhesion Potential of Extraocular Aqp0 during Teleost Development.Spatial distributions of phosphorylated membrane proteins aquaporin 0 and MP20 across young and aged human lenses.Aquaporins in the eye: expression, function, and roles in ocular diseaseCloning and Stress-Induced Expression Analysis of Calmodulin in the Antarctic Alga Chlamydomonas sp. ICE-L.CaMELS: In silico prediction of calmodulin binding proteins and their binding sites.A Proteomic Approach for the Identification of Up-Regulated Proteins Involved in the Metabolic Process of the Leiomyoma.In vivo analysis of aquaporin 0 function in zebrafish: permeability regulation is required for lens transparencyGap junction regulation by calmodulin.The many structural faces of calmodulin: a multitasking molecular jackknife.Novel regulation of equlibrative nucleoside transporter 1 (ENT1) by receptor-stimulated Ca2+-dependent calmodulin binding.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.Applying bimolecular fluorescence complementation to screen and purify aquaporin protein:protein complexesCalmodulin Gates Aquaporin 0 Permeability through a Positively Charged Cytoplasmic Loop.The Hevea brasiliensis XIP aquaporin subfamily: genomic, structural and functional characterizations with relevance to intensive latex harvesting.Plant and animal aquaporins crosstalk: what can be revealed from distinct perspectives.Aquaporin Protein-Protein Interactions.The Role of Aquaporins in Ocular Lens Homeostasis.Role of Pore-Lining Residues in Defining the Rate of Water Conduction by Aquaporin-0.Molecular Biology of Aquaporins.Sub-nanometre mapping of the aquaporin-water interface using multifrequency atomic force microscopy.A Mechanism of Calmodulin Modulation of the Human Cardiac Sodium Channel.Aqp0a Regulates Suture Stability in the Zebrafish Lens.
P2860
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P2860
Allosteric mechanism of water-channel gating by Ca2+–calmodulin
description
2013 nî lūn-bûn
@nan
2013 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Allosteric mechanism of water-channel gating by Ca2+–calmodulin
@ast
Allosteric mechanism of water-channel gating by Ca2+–calmodulin
@en
Allosteric mechanism of water-channel gating by Ca2+–calmodulin
@nl
type
label
Allosteric mechanism of water-channel gating by Ca2+–calmodulin
@ast
Allosteric mechanism of water-channel gating by Ca2+–calmodulin
@en
Allosteric mechanism of water-channel gating by Ca2+–calmodulin
@nl
altLabel
Allosteric mechanism of water channel gating by Ca2+–calmodulin
@en
Allosteric mechanism of water-channel gating by Ca2+-calmodulin.
@en
prefLabel
Allosteric mechanism of water-channel gating by Ca2+–calmodulin
@ast
Allosteric mechanism of water-channel gating by Ca2+–calmodulin
@en
Allosteric mechanism of water-channel gating by Ca2+–calmodulin
@nl
P2860
P50
P3181
P356
P1476
Allosteric mechanism of water-channel gating by Ca2+–calmodulin
@en
P2860
P2888
P304
P3181
P356
10.1038/NSMB.2630
P4011
09b4ac1a7ea8acd352f9eceadb3ae9e97d025d0e
P407
P577
2013-09-01T00:00:00Z
P5875
P6179
1037496685