p32 protein levels are integral to mitochondrial and endoplasmic reticulum morphology, cell metabolism and survival

Biochemical Journal

Volumn 453, Issue 3, 2013, Pages 381-391

  Hu, MengJie ^a   Crawford, Simon A ^b   Henstridge, Darren C ^c   Ng, Ivan H W ^a,d   Boey, Esther J H ^a,c   Xu, Yuekang ^a   Febbraio, Mark A ^c   Jans, David A ^d   Bogoyevitch, Marie A ^a  

^a UNIVERSITY OF MELBOURNE   (Australia)

^b UNIVERSITY OF MELBOURNE   (Australia)

^c BAKER IDI HEART AND DIABETES INSTITUTE   (Australia)

^d MONASH UNIVERSITY   (Australia)

Author keywords

Endoplasmic reticulum (ER) morphology; Mitochondrial metabolic activity; Mitochondrial morphology; Stress response

Indexed keywords

ADENOSINE TRIPHOSPHATE; MITOCHONDRIAL PROTEIN; MITOFUSIN 1; MITOFUSIN 2; P32 PROTEIN; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; BIOENERGY; CELL DEATH; CELL DENSITY; CELL METABOLISM; CELL STRUCTURE; CELL SURVIVAL; CELLULAR STRESS RESPONSE; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; FRAGMENTATION REACTION; GENE SILENCING; HELA CELL; HUMAN; HUMAN CELL; HYPEROSMOTIC STRESS; MITOCHONDRIAL RESPIRATION; MITOCHONDRION; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEPLETION; PROTEIN EXPRESSION; RIBOSOME; TRANSMISSION ELECTRON MICROSCOPY;

ADENOSINE TRIPHOSPHATE; CARRIER PROTEINS; ENDOPLASMIC RETICULUM; HELA CELLS; HUMANS; IMMUNOBLOTTING; MICROSCOPY, CONFOCAL; MITOCHONDRIA; MITOCHONDRIAL PROTEINS;

EID: 84880081465     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20121829     Document Type: Article

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