Phosphomimics destabilize Hsp27 oligomeric assemblies and enhance chaperone activity

Chemistry and Biology

Volumn 22, Issue 2, 2015, Pages 186-195

  Jovcevski, Blagojce ^a   Kelly, Megan A ^a   Rote, Anthea P ^a   Berg, Tracey ^a   Gastall, Heidi Y ^b   Benesch, Justin L P ^b   Aquilina, J Andrew ^a   Ecroyd, Heath ^a  

^a UNIVERSITY OF WOLLONGONG   (Australia)

^b UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; DIMER; HEAT SHOCK PROTEIN 27; OLIGOMER; SERINE; RECOMBINANT PROTEIN;

ANIMAL CELL; ARTICLE; CIRCULAR DICHROISM; COLLISIONALLY ACTIVATED DISSOCIATION; DISULFIDE BOND; FEMALE; GEL PERMEATION CHROMATOGRAPHY; HEAT STRESS; HUMAN; HUMAN CELL; MASS SPECTROMETRY; MOLECULAR SIZE; MOLECULAR WEIGHT; MOUSE; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; BIOSYNTHESIS; CELL LINE; CHEMISTRY; DIMERIZATION; GENETICS; HEK293 CELL LINE; METABOLISM; PHOSPHORYLATION; PROTEIN FOLDING; SITE DIRECTED MUTAGENESIS;

MAMMALIA;

CELL LINE; CIRCULAR DICHROISM; DIMERIZATION; HEK293 CELLS; HSP27 HEAT-SHOCK PROTEINS; HUMANS; MASS SPECTROMETRY; MOLECULAR CHAPERONES; MUTAGENESIS, SITE-DIRECTED; PHOSPHORYLATION; PROTEIN FOLDING; RECOMBINANT PROTEINS;

EID: 84923126434     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2015.01.001     Document Type: Article

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