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Summary Anatomy Item Literature (6354) Expression Attributions Wiki
XB-ANAT-254

Papers associated with oocyte (and mip)

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Positively charged amino acid residues in the extracellular loops A and C of lens aquaporin 0 interact with the negative charges in the plasma membrane to facilitate cell-to-cell adhesion., Kumari S., Exp Eye Res. August 1, 2019; 185 107682.              


The Extracellular C-loop Domain Plays an Important Role in the Cell Adhesion Function of Aquaporin 0., Nakazawa Y., Curr Eye Res. April 1, 2017; 42 (4): 617-624.


Calmodulin Gates Aquaporin 0 Permeability through a Positively Charged Cytoplasmic Loop., Fields JB., J Biol Chem. January 6, 2017; 292 (1): 185-195.


Bi-functionality of Opisthorchis viverrini aquaporins., Geadkaew A., Biochimie. January 1, 2015; 108 149-59.


Functional characterization of an AQP0 missense mutation, R33C, that causes dominant congenital lens cataract, reveals impaired cell-to-cell adhesion., Kumari SS., Exp Eye Res. November 1, 2013; 116 371-85.                  


In vivo analysis of aquaporin 0 function in zebrafish: permeability regulation is required for lens transparency., Clemens DM., Invest Ophthalmol Vis Sci. July 30, 2013; 54 (7): 5136-43.


Quantitative analysis of ascorbic acid permeability of aquaporin 0 in the lens., Nakazawa Y., Biochem Biophys Res Commun. November 11, 2011; 415 (1): 125-30.


Design and characterization of genetically engineered zebrafish aquaporin-3 mutants highly permeable to the cryoprotectant ethylene glycol., Chauvigné F., BMC Biotechnol. April 8, 2011; 11 34.            


The effect of the interaction between aquaporin 0 (AQP0) and the filensin tail region on AQP0 water permeability., Nakazawa Y., Mol Vis. March 23, 2011; 17 3191-9.            


Effects of naturally occurring G103D point mutation of AQP5 on its water permeability, trafficking and cellular localization in the submandibular gland of rats., Karabasil MR., Biol Cell. February 1, 2011; 103 (2): 69-86.


Two distinct aquaporin 0s required for development and transparency of the zebrafish lens., Froger A., Invest Ophthalmol Vis Sci. December 1, 2010; 51 (12): 6582-92.


Zinc modulation of water permeability reveals that aquaporin 0 functions as a cooperative tetramer., Németh-Cahalan KL., J Gen Physiol. November 1, 2007; 130 (5): 457-64.        


Dominant-negative suppression of big brain ion channel activity by mutation of a conserved glutamate in the first transmembrane domain., Yool AJ., Gene Expr. January 1, 2007; 13 (6): 329-37.


Pore selectivity analysis of an aquaglyceroporin by stopped-flow spectrophotometry on bacterial cell suspensions., Hubert JF., Biol Cell. September 1, 2005; 97 (9): 675-86.


Conversion of aquaporin 6 from an anion channel to a water-selective channel by a single amino acid substitution., Liu K., Proc Natl Acad Sci U S A. February 8, 2005; 102 (6): 2192-7.


Water permeability of C-terminally truncated aquaporin 0 (AQP0 1-243) observed in the aging human lens., Ball LE., Invest Ophthalmol Vis Sci. November 1, 2003; 44 (11): 4820-8.


Mosquito (Aedes aegypti ) aquaporin, present in tracheolar cells, transports water, not glycerol, and forms orthogonal arrays in Xenopus oocyte membranes., Duchesne L., Eur J Biochem. February 1, 2003; 270 (3): 422-9.


Cloning and functional expression of an MIP (AQP0) homolog from killifish (Fundulus heteroclitus) lens., Virkki LV., Am J Physiol Regul Integr Comp Physiol. December 1, 2001; 281 (6): R1994-2003.


Functional characterization of a water channel of the nematode Caenorhabditis elegans., Kuwahara M., Biochim Biophys Acta. December 15, 2000; 1517 (1): 107-12.


Functional impairment of lens aquaporin in two families with dominantly inherited cataracts., Francis P., Hum Mol Genet. September 22, 2000; 9 (15): 2329-34.


Oligomerization state of MIP proteins expressed in Xenopus oocytes as revealed by freeze-fracture electron-microscopy analysis., Bron P., J Struct Biol. December 30, 1999; 128 (3): 287-96.


gp120 envelope glycoproteins of human immunodeficiency viruses competitively antagonize signaling by coreceptors CXCR4 and CCR5., Madani N., Proc Natl Acad Sci U S A. July 7, 1998; 95 (14): 8005-10.


Cloning of a novel water and urea-permeable aquaporin from mouse expressed strongly in colon, placenta, liver, and heart., Ma T., Biochem Biophys Res Commun. November 17, 1997; 240 (2): 324-8.


Water and glycerol permeabilities of aquaporins 1-5 and MIP determined quantitatively by expression of epitope-tagged constructs in Xenopus oocytes., Yang B., J Biol Chem. June 27, 1997; 272 (26): 16140-6.


Incorporation of proteins into (Xenopus) oocytes by proteoliposome microinjection: functional characterization of a novel aquaporin., Le Cahérec F., J Cell Sci. June 1, 1996; 109 ( Pt 6) 1285-95.


Glycerol permeability of mutant aquaporin 1 and other AQP-MIP proteins: inhibition studies., Abrami L., Pflugers Arch. January 1, 1996; 431 (3): 408-14.


A method for determining the unitary functional capacity of cloned channels and transporters expressed in Xenopus laevis oocytes., Zampighi GA., J Membr Biol. November 1, 1995; 148 (1): 65-78.


Ion, water and neutral solute transport in Xenopus oocytes expressing frog lens MIP., Kushmerick C., Exp Eye Res. September 1, 1995; 61 (3): 351-62.


A 28 kDa sarcolemmal antigen in kidney principal cell basolateral membranes: relationship to orthogonal arrays and MIP26., Verbavatz JM., J Cell Sci. April 1, 1994; 107 ( Pt 4) 1083-94.

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