Disposal of iron by a mutant form of lipocalin 2

Nature Communications

Volumn 7, Issue , 2016, Pages

  Barasch, Jonathan ^a   Hollmen, Maria ^a   Deng, Rong ^a   Hod, Eldad A ^a   Rupert, Peter B ^b   Abergel, Rebecca J ^c   Allred, Benjamin E ^c   Xu, Katherine ^a   Darrah, Shaun F ^a   Tekabe, Yared ^a   Perlstein, Alan ^a   Wax, Rebecca ^a   Bruck, Efrat ^a   Stauber, Jacob ^a   Corbin, Kaitlyn A ^a   Buchen, Charles ^a   Slavkovich, Vesna ^a   Graziano, Joseph ^a   Spitalnik, Steven L ^a   Bao, Guanhu ^d   Strong, Roland K ^b   Qiu, Andong ^a   more..

^a Howard Hughes Medical Institute   (China)

^b UNIVERSITY OF WASHINGTON SCHOOL OF MEDICINE   (United States)

^c LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

^d ANHUI AGRICULTURAL UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

CITRIC ACID; ENTEROCHELIN; IRON; IRON DEXTRAN; MEGALIN; MONOMER; NEUTROPHIL GELATINASE ASSOCIATED LIPOCALIN; TRANSFERRIN; IRON CHELATING AGENT; LCN2 PROTEIN, HUMAN; LCN2 PROTEIN, MOUSE; LIGAND; PROTEIN BINDING; SIDEROPHORE;

BLOOD; CHELATION; GENE EXPRESSION; IRON; LIGAND; MICROORGANISM; MUTATION; PROTEIN; REDOX CONDITIONS; RODENT; SIDEROPHORE; TOXICITY;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; CELL MIGRATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DISSOCIATION CONSTANT; IMMUNODETECTION; IN VITRO STUDY; IN VIVO STUDY; INOCULATION; IRON CHELATION; IRON OVERLOAD; IRON TRANSPORT; IRON URINE LEVEL; KIDNEY TUBULE ABSORPTION; LIGAND BINDING; MOUSE; NONHUMAN; OXIDATION; PH; PROTEIN BINDING; SITE DIRECTED MUTAGENESIS; STATIC ELECTRICITY; STOICHIOMETRY; URINARY EXCRETION; ANIMAL; DISEASE MODEL; GENETICS; HUMAN; INFLAMMATION; KIDNEY; METABOLISM; MUTATION; OXIDATION REDUCTION REACTION; PHYSIOLOGY; TRANSGENIC MOUSE;

MUS;

ANIMALS; DISEASE MODELS, ANIMAL; HUMANS; INFLAMMATION; IRON; IRON CHELATING AGENTS; IRON OVERLOAD; KIDNEY; LIGANDS; LIPOCALIN-2; MICE; MICE, TRANSGENIC; MUTATION; OXIDATION-REDUCTION; PROTEIN BINDING; SIDEROPHORES; TRANSFERRIN;

EID: 84994005309     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms12973     Document Type: Article

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