The vacuolar-type H+-ATPase at a glance - more than a proton pump

Journal of Cell Science

Volumn 127, Issue 23, 2014, Pages 4987-4993

  Maxson, Michelle E ^a   Grinstein, Sergio ^a,b  

^a HOSPITAL FOR SICK CHILDREN   (Canada)

^b ST MICHAEL'S HOSPITAL   (Canada)

Author keywords

Acidification; pH regulation; Proton motive; Proton pump; Vacuolar ATPase

Indexed keywords

MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

ACIDIFICATION; ARTICLE; CELL MEMBRANE; ELECTRIC POTENTIAL; ENZYME ACTIVITY; ENZYME DEGRADATION; ENZYME REGULATION; ENZYME SUBSTRATE; MEMBRANE FUSION; PH; PROTEIN EXPRESSION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; SYNAPSE VESICLE; ANIMAL; ENDOCYTOSIS; ENZYMOLOGY; HUMAN; MEMBRANE POTENTIAL; METABOLISM; PROTEIN DEGRADATION; PROTEIN TRANSPORT; SIGNAL TRANSDUCTION; TRANSPORT VESICLE;

ANIMALS; CELL MEMBRANE; ENDOCYTOSIS; HUMANS; HYDROGEN-ION CONCENTRATION; MEMBRANE POTENTIALS; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN TRANSPORT; PROTEOLYSIS; SIGNAL TRANSDUCTION; TRANSPORT VESICLES; VACUOLAR PROTON-TRANSLOCATING ATPASES;

EID: 84914145216     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.158550     Document Type: Article

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