K Takata, T Matsuzaki, Y Tajika - Progress in Histochemistry and Cytochemistry, 2004 - Elsevier Aquaporins (AQP) are integral membrane proteins that serve as channels in the transfer of
water, and in some cases, small solutes across the membrane. They are conserved in
bacteria, plants, and animals. Structural analyses of the molecules have revealed the ... Cited by 122 - Related articles - BL Direct - All 4 versions
W Zhang, S Patil, B Chauhan, S Guo, DR Powell, J … - Journal of Biological …, 2006 - ASBMB Page 1. 1 FOXO1 REGULATES MULTIPLE METABOLIC PATHWAYS IN THE LIVER: EFFECTS
ON GLUCONEOGENIC, GLYCOLYTIC AND LIPOGENIC GENE EXPRESSION Wenwei Zhang
1,2 , Sandip Patil 1,2 , Balwant Chauhan 1,2 , Shaodong Guo 1,2 , David R. Powell 3 , ... Cited by 102 - Related articles - BL Direct - All 5 versions
JM Carbrey, DA Gorelick-Feldman, D … - Proceedings of the …, 2003 - National Acad Sciences Aquaglyceroporins form the subset of the aquaporin water channel family that is permeable to
glycerol and certain small, uncharged solutes. AQP9 has unusually broad solute permeability
and is expressed in hepatocyte plasma membranes. Proteoliposomes reconstituted with ... Cited by 95 - Related articles - BL Direct - All 11 versions
M Hara-Chikuma, E Sohara, T Rai, M Ikawa, M … - Journal of Biological …, 2005 - ASBMB Aquaporin-7 (AQP7) is a water/glycerol transporting protein expressed in adipocyte plasma
membranes. We report here remarkable age-dependent hypertrophy in adipocytes in
AQP7-deficient mice. Wild type and AQP7 null mice had similar growth at 0–16 weeks as ... Cited by 80 - Related articles - All 6 versions
T Hibuse, N Maeda, T Funahashi, K … - Proceedings of the …, 2005 - National Acad Sciences In adipocytes, hydrolysis of triglycerides results in the release of free fatty acids and glycerol.
Aquaporin 7 (AQP7), a member of aquaglyceroporins, is known to permeabilize glycerol and
water. We recently generated Aqp7-knockout (KO) mice and demonstrated that such mice ... Cited by 75 - Related articles - BL Direct - All 10 versions
- ►nih.gov P Agre - Bioscience Reports, 2004 - Springer Thank you very much. I am humbled, I am delighted; I am honored. This is every scientist's
dream: to give the Nobel Lecture in Stockholm. But I would not be honest if I did not tell you that
I am having a little anxiety being on this platform. I have lectured a number of times in ... Cited by 69 - Related articles - BL Direct - All 27 versions
T Matsuzaki, Y Tajika, A Ablimit, T Aoki, H Hagiwara … - Medical Electron …, 2004 - Springer Abstract Fluid transfer such as secretion and absorption is one of the major functions of the digestive
system. Aquaporins are water channel proteins providing water transfer across the cellular
membrane. At least six aquaporin isoforms are expressed in the digestive system. ... Cited by 54 - Related articles - All 4 versions
J Badaut, JM Petit, JF Brunet, PJ Magistretti, C … - Neuroscience, 2004 - Elsevier Aquaporin 9 (AQP9) is a recently cloned water channel that is permeable to
monocarboxylate, glycerol and urea. In rat, AQP9 has been found in testis and liver as well as
in brain where its expression has been initially shown in glial cells in forebrain. However, ... Cited by 52 - Related articles - All 5 versions
- ►nih.gov N Maeda, T Funahashi, T Hibuse, A … - Proceedings of the …, 2004 - National Acad Sciences Adipocytes hydrolyze triglycerides and secrete free fatty acids and glycerol into the
circulation. The molecular mechanism involved in glycerol transport from adipocytes has not
been elucidated. Here, we investigated glycerol and glucose metabolism in mice lacking ... Cited by 53 - Related articles - All 9 versions
D Ferri, A Mazzone, GE Liquori, G Cassano, M … - Hepatology, 2003 - interscience.wiley.com Aquaporins are channel proteins widely expressed in nature and known to facilitate the rapid
movement of water across numerous cell membranes. A mammalian aquaporin, AQP8, was
recently discovered and found to have a very distinct evolutionary pathway. To ... Cited by 44 - Related articles - All 5 versions
