Chemical genetic screening identifies sulfonamides that raise organellar pH and interfere with membrane traffic

Traffic

Volumn 5, Issue 7, 2004, Pages 478-492

  Nieland, Thomas J F ^a,b   Feng, Yan ^b   Brown, Jing Xu ^c   Chuang, Tuan Daniel ^d   Buckett, Peter D ^c   Wang, Jin ^e   Xie, Xiao Song ^e   McGraw, Timothy E ^d   Kirchhausen, Tomas ^a,b   Wessling Resnick, Marianne ^c  

^a HARVARD MEDICAL SCHOOL   (United States)

^b Harvard Inst Chem and Cell Biol   (United States)

^c HARVARD SCHOOL OF PUBLIC HEALTH   (United States)

^d WEILL CORNELL MEDICAL COLLEGE   (United States)

^e Univ of Texas SW Medical Center   (United States)

Author keywords

Chemical genetics; Membrane traffic; Organelle pH; Sulfonamides

Indexed keywords

ADENOSINE TRIPHOSPHATE; CELL SURFACE RECEPTOR; CHEMICAL COMPOUND; IONOPHORE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; SULFONAMIDE; TRANSFERRIN; TRANSFERRIN RECEPTOR;

ACIDIFICATION; ANIMAL CELL; ARTICLE; CELL DISRUPTION; CELL FUNCTION; CELL MEMBRANE TRANSPORT; CELL ORGANELLE; CELL PH; CELL SURFACE; CHEMICAL GENETICS; CHEMICAL STRUCTURE; CONTROLLED STUDY; ENDOCYTOSIS; ENDOPLASMIC RETICULUM; ENDOSOME; ENZYME INHIBITION; EXOCYTOSIS; EXPERIMENTAL DESIGN; GENETIC IDENTIFICATION; GOLGI COMPLEX; HUMAN; HUMAN CELL; IN VITRO STUDY; IRON TRANSPORT; LYSOSOME; NONHUMAN; PRIORITY JOURNAL; PROTEIN HYDROLYSIS; PROTEIN TRANSPORT; RECEPTOR DOWN REGULATION;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; ANIMALS; BETA-GALACTOSIDASE; CELL MEMBRANE; COLORING AGENTS; DOSE-RESPONSE RELATIONSHIP, DRUG; DOWN-REGULATION; ENDOPLASMIC RETICULUM; ENDOSOMES; EPITHELIAL CELLS; EXOCYTOSIS; GENETIC TECHNIQUES; GOLGI APPARATUS; HUMANS; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; IONOPHORES; IRON; K562 CELLS; KINETICS; LYSOSOMES; MEMBRANE GLYCOPROTEINS; MODELS, CHEMICAL; PROTONS; RECEPTORS, LDL; SULFONAMIDES; TRANSFERRIN; VACUOLAR PROTON-TRANSLOCATING ATPASES; VIRAL ENVELOPE PROTEINS;

EID: 3142737966     PISSN: 13989219     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1398-9219.2004.00193.x     Document Type: Article

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