HDAC6 regulates mutant SOD1 aggregation through two SMIR motifs and tubulin acetylation

Journal of Biological Chemistry

Volumn 288, Issue 21, 2013, Pages 15035-15045

  Gal, Jozsef ^a   Chen, Jing ^a   Barnett, Kelly R ^a   Yang, Liuqing ^a   Brumley, Erin ^a   Zhu, Haining ^a  

^a UNIVERSITY OF KENTUCKY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYOTROPHIC LATERAL SCLEROSIS; COMMON FEATURES; CU/ZN-SUPEROXIDE DISMUTASE; CULTURED CELL; HISTONE DEACETYLASES; INTERACTION REGION; MUTANT PROTEINS; PROTEIN AGGREGATION;

ACETYLATION; OXYGEN;

PROTEINS;

ALPHA TUBULIN; COPPER ZINC SUPEROXIDE DISMUTASE; HISTONE DEACETYLASE 6; MESSENGER RNA; MUTANT PROTEIN; PROTEIN P62;

ACETYLATION; AMYOTROPHIC LATERAL SCLEROSIS; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME REGULATION; GENE; GENE SILENCING; HDAC6 GENE; MICROTUBULE ASSEMBLY; MOUSE; NEUROPATHOLOGY; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DEFECT; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; STRUCTURE ACTIVITY RELATION; UBIQUITINATION;

AMYOTROPHIC LATERAL SCLEROSIS (LOU GEHRIG'S DISEASE); CU/ZN SUPEROXIDE DISMUTASE (SOD1) (SOD1); HISTONE DEACETYLASE; HISTONE DEACETYLASE 6; NEURODEGENERATIVE DISEASES; P62/SEQUESTOSOME 1; PROTEIN AGGREGATION; SUPEROXIDE DISMUTASE (SOD);

ACETYLATION; AMINO ACID MOTIFS; AMINO ACID SUBSTITUTION; AMYOTROPHIC LATERAL SCLEROSIS; ANIMALS; HEK293 CELLS; HISTONE DEACETYLASES; HUMANS; MICE; MICE, TRANSGENIC; MICROTUBULES; MUTATION, MISSENSE; PROTEOLYSIS; SUPEROXIDE DISMUTASE; TUBULIN; UBIQUITINATED PROTEINS;

EID: 84878243123     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.431957     Document Type: Article

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