Janus-faced Sestrin2 controls ROS and mTOR signalling through two separate functional domains

Nature Communications

Volumn 6, Issue , 2015, Pages

  Kim, Hanseong ^a   An, Sojin ^a   Ro, Seung Hyun ^a,g   Teixeira, Filipa ^a,b,c,d   Jin Park, Gyeong ^a,e   Kim, Cheal ^e   Cho, Chun Seok ^a   Kim, Jeong Sig ^a,f   Jakob, Ursula ^a   Lee, Jun Hee ^a   Cho, Uhn Soo ^a  

^a UNIVERSITY OF MICHIGAN   (United States)

^b UNIVERSITY OF PORTO   (Portugal)

^c UNIVERSITY OF PORTO   (Portugal)

^d UNIVERSITY OF PORTO   (Portugal)

^e Seoul National University of Science and Technology   (South Korea)

^f Soonchunhyang University   (South Korea)

^g UNIVERSITY OF NEBRASKA LINCOLN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HELIX LOOP HELIX PROTEIN; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; OXIDOREDUCTASE; PROTEIN; REACTIVE OXYGEN METABOLITE; SESTRIN2 PROTEIN; UNCLASSIFIED DRUG; MECHANISTIC TARGET OF RAPAMYCIN COMPLEX 1; MULTIPROTEIN COMPLEX; NUCLEAR PROTEIN; SESN2 PROTEIN, HUMAN; TARGET OF RAPAMYCIN KINASE;

CRYSTAL STRUCTURE; MOLECULAR ANALYSIS; PHYSIOLOGICAL RESPONSE; RADICAL;

AGING; ANIMAL CELL; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; CRYSTAL STRUCTURE; EMBRYO; ENZYME INHIBITION; HEK293 CELL LINE; HUMAN; HUMAN CELL; MOUSE; NONHUMAN; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; REDUCTION; SIGNAL TRANSDUCTION; CHEMISTRY; CRYSTALLIZATION; ESCHERICHIA COLI; IMMUNOBLOTTING; IMMUNOPRECIPITATION; IN VITRO STUDY; METABOLISM; PROTEIN TERTIARY STRUCTURE; SIZE EXCLUSION CHROMATOGRAPHY; TUMOR CELL LINE;

CELL LINE, TUMOR; CHROMATOGRAPHY, GEL; CRYSTALLIZATION; ESCHERICHIA COLI; HEK293 CELLS; HELIX-TURN-HELIX MOTIFS; HUMANS; IMMUNOBLOTTING; IMMUNOPRECIPITATION; IN VITRO TECHNIQUES; MULTIPROTEIN COMPLEXES; NUCLEAR PROTEINS; OXIDOREDUCTASES; PROTEIN STRUCTURE, TERTIARY; REACTIVE OXYGEN SPECIES; SIGNAL TRANSDUCTION; TOR SERINE-THREONINE KINASES;

EID: 84948654888     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms10025     Document Type: Article

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