Impaired routing of wild type FXYD2 after oligomerisation with FXYD2-G41R might explain the dominant nature of renal hypomagnesemia

Biochimica et Biophysica Acta - Biomembranes

Volumn 1778, Issue 2, 2008, Pages 398-404

  Cairo, Edinio R ^a   Friedrich, Thomas ^b   Swarts, Herman G P ^a   Knoers, Nine V ^a   Bindels, René J M ^a   Monnens, Leo A ^a   Willems, Peter H G M ^a   De Pont, Jan Joep H H M ^a   Koenderink, Jan B ^a  

^a RADBOUD UNIVERSITY MEDICAL CENTER   (Netherlands)

^b MAX PLANCK INSTITUTE OF BIOPHYSICS   (Germany)

Author keywords

FXYD2; Hypomagnesemia; Na,K ATPase

Indexed keywords

DITHIOTHREITOL; FXYD2 PROTEIN; G41R PROTEIN; PROTEIN DERIVATIVE; PROTEIN SUBUNIT; UNCLASSIFIED DRUG;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; CELL MEMBRANE; FEMALE; GLYCOSYLATION; HYPOMAGNESEMIA; IMMUNOPRECIPITATION; MOLECULAR MECHANICS; MUTATION; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN BINDING; RENAL HYPOMAGNESEMIA; WILD TYPE;

AMINO ACID SEQUENCE; ANIMALS; BIOPOLYMERS; HUMANS; KIDNEY; MAGNESIUM; MUTAGENESIS, SITE-DIRECTED; SODIUM-POTASSIUM-EXCHANGING ATPASE; XENOPUS LAEVIS;

EID: 38349046659     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2007.10.009     Document Type: Article

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