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Journal ArticleDOI

Water permeability and characterization of aquaporin-11.

Kaya Yakata, +2 more
- 01 May 2011 - 
- Vol. 174, Iss: 2, pp 315-320
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TLDR
The findings indicate that AQP11 could be involved in slow but constant water movement across the membrane, and it is found that Tyr83 facing the channel pore might be a key amino acid residue that decreases the water permeation of AQP 11.
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This article is published in Journal of Structural Biology.The article was published on 2011-05-01. It has received 104 citations till now. The article focuses on the topics: Membrane & Cell membrane.

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Citations
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Journal ArticleDOI

The evolutionary aspects of aquaporin family

TL;DR: This review focuses on the evolutionary aspects of AQP from bacteria to humans in view of the structural and functional diversities of AQPs.
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Evolution and functional diversity of aquaporins.

TL;DR: This review provides new insight into the origin by horizontal gene transfer of plant glycerol-transporting aquaporins (NIPs), and the functional co-option and gene replacement of insect Glycerol transporters.
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Water channel proteins in the gastrointestinal tract

TL;DR: AQP expression and localization at the tissue, cellular and subcellular level in gastrointestinal epithelia, and their modification in various gut diseases are reviewed.
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Beyond water homeostasis: Diverse functional roles of mammalian aquaporins

TL;DR: Elucidating the full range of functional roles of AQPs beyond the passive conduction of water will improve the understanding of mammalian physiology in health and disease and could provide routes to a range of novel therapies.
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The role of mammalian superaquaporins inside the cell

TL;DR: The role of AQP11 in the kidney and liver seems to alleviate the tissue damage and facilitate the recovery and the clarification of the function and roles of the superaquaporin may lead to the identification of new roles of AQPs.
References
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Journal ArticleDOI

Clustal w: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

TL;DR: The sensitivity of the commonly used progressive multiple sequence alignment method has been greatly improved and modifications are incorporated into a new program, CLUSTAL W, which is freely available.
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Comparative Protein Modelling by Satisfaction of Spatial Restraints

TL;DR: A comparative protein modelling method designed to find the most probable structure for a sequence given its alignment with related structures, which is automated and illustrated by the modelling of trypsin from two other serine proteinases.
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The HHpred interactive server for protein homology detection and structure prediction

TL;DR: HHpred is a fast server for remote protein homology detection and structure prediction and is the first to implement pairwise comparison of profile hidden Markov models (HMMs) and allows to search a wide choice of databases.
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Structural determinants of water permeation through aquaporin-1.

TL;DR: An atomic model of human red cell AQP1 is described, providing a possible molecular explanation to a longstanding puzzle in physiology—how membranes can be freely permeable to water but impermeable to protons.
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Cellular and molecular biology of the aquaporin water channels.

TL;DR: The high water permeability characteristic of mammalian red cell membranes is now known to be caused by the protein AQP1, a tetramer with each subunit containing an aqueous pore likened to an hourglass formed by obversely arranged tandem repeats.
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