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Journal ArticleDOI

Aquaporins: water channel proteins of the cell membrane

TLDR
The diverse and characteristic distribution of aquaporins in the body suggests their important and specific roles in each organ.
About
This article is published in Progress in Histochemistry and Cytochemistry.The article was published on 2004-05-25. It has received 371 citations till now. The article focuses on the topics: Aquaporin 2 & Aquaporin.

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Citations
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Oogenesis in teleosts: How fish eggs are formed

TL;DR: Recent advances on teleost fish oocyte differentiation, maturation and ovulation are highlighted, including those involved in the degeneration and reabsorption of ovarian follicles (atresia).
Journal ArticleDOI

The human urinary proteome contains more than 1500 proteins, including a large proportion of membrane proteins.

TL;DR: The analysis provides a high-confidence set of proteins present in human urinary proteome and provides a useful reference for comparing datasets obtained using different methodologies and may prove useful in biomarker discovery in the future.
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Phylogeny and evolution of the major intrinsic protein family

TL;DR: This work states that with the recent increase in genomic projects, there is a considerable increase in the quantity and taxonomic range of MIPs in molecular databases.
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Theoretical aspects of water-holding in meat.

TL;DR: Irrespective of the lack of theoretical explanation on the mechanism of water-holding in meat, the meat industry is able to control the macroscopic behaviour of meat-based ingredients rather well and more attention should be paid to heavy meromyosin, Z-line and other elements of molecular size or colloidal size.
References
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Journal ArticleDOI

Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein.

TL;DR: Oocytes from Xenopus laevis microinjected with in vitro-transcribed CHIP28 RNA exhibited increased osmotic water permeability; this was reversibly inhibited by mercuric chloride, a known inhibitor of water channels, so it is likely that ChIP28 is a functional unit of membrane water channels.
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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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Aquaporin-4 deletion in mice reduces brain edema after acute water intoxication and ischemic stroke.

TL;DR: It is shown that mice deficient in aquaporin-4 (AQP4), a glial membrane water channel, have much better survival than wild-type mice in a model of brain edema caused by acute water intoxication, and suggested that AQP4 inhibition may provide a new therapeutic option for reducingbrain edema in a wide variety of cerebral disorders.
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Claudin-based tight junctions are crucial for the mammalian epidermal barrier a lesson from claudin-1–deficient mice

TL;DR: Findings provide the first evidence that continuous claudin-based TJs occur in the epidermis and that these TJs are crucial for the barrier function of the mammalian skin.
Journal ArticleDOI

Specialized membrane domains for water transport in glial cells : high-resolution immunogold cytochemistry of aquaporin-4 in rat brain

TL;DR: The highly polarized AQP4 expression indicates that these cells are equipped with specific membrane domains that are specialized for water transport, thereby mediating the flow of water between glial cells and the cavities filled with CSF and the intravascular space.
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