Point mutations in the aromatic/arginine region in aquaporin 1 allow passage of urea, glycerol, ammonia, and protons

Proceedings of the National Academy of Sciences of the United States of America

Volumn 103, Issue 2, 2006, Pages 269-274

  Beitz, Eric ^a   Wu, Binghua ^a   Holm, Lars M ^b   Schultz, Joachim E ^a   Zeuthen, Thomas ^b  

^a UNIVERSITY OF TÜBINGEN   (Germany)

^b UNIVERSITY OF COPENHAGEN   (Denmark)

Author keywords

Mutational analysis; Proton filter; Solute selectivity

Indexed keywords

ALANINE; AMMONIA; AQUAPORIN; AQUAPORIN 1; ARGININE; ASPARAGINE; GLYCEROL; HISTIDINE; MUTANT PROTEIN; PHENYLALANINE; PROLINE; PROTON; UREA; VALINE;

AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; DELETION MUTANT; MEMBRANE PERMEABILITY; NONHUMAN; NUCLEOTIDE SEQUENCE; OOCYTE; PARTICLE SIZE; POINT MUTATION; PRIORITY JOURNAL; PROTEIN STRUCTURE; PROTON TRANSPORT; RAT; WATER PERMEABILITY; YEAST;

AMMONIA; ANIMALS; AQUAPORIN 1; ARGININE; ELECTROPHYSIOLOGY; GLYCEROL; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MUTATION; OOCYTES; PATCH-CLAMP TECHNIQUES; PROTEIN STRUCTURE, TERTIARY; PROTONS; RATS; SACCHAROMYCES CEREVISIAE; SOLUBILITY; UREA; WATER; XENOPUS LAEVIS;

MAMMALIA;

EID: 31044449089     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0507225103     Document Type: Article

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