The preferential heterodimerization of human small heat shock proteins HSPB1 and HSPB6 is dictated by the N-terminal domain

Archives of Biochemistry and Biophysics

Volumn 610, Issue , 2016, Pages 41-50

  Heirbaut, Michelle ^a   Lermyte, Frederik ^b   Martin, Esther M ^b,c   Beelen, Steven ^a   Verschueren, Tim ^b   Sobott, Frank ^b,c   Strelkov, Sergei V ^a   Weeks, Stephen D ^a  

^a DEPARTMENT OF PHARMACEUTICAL AND PHARMACOLOGICAL SCIENCES   (Belgium)

^b UNIVERSITY OF ANTWERP   (Belgium)

^c UNIVERSITY OF LEEDS   (United Kingdom)

Author keywords

Chaperone; Heterooligomers; HSP20; HSP27; Native mass spectrometry; Small angle x ray scattering

Indexed keywords

HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 6; HETERODIMER; OLIGOMER; UNCLASSIFIED DRUG; CHAPERONE; HEAT SHOCK PROTEIN 20; HSPB1 PROTEIN, HUMAN; HSPB6 PROTEIN, HUMAN; RECOMBINANT PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; DIMERIZATION; MASS SPECTROMETRY; MOLECULAR MECHANICS; PRIORITY JOURNAL; PROTEIN CROSS LINKING; X RAY CRYSTALLOGRAPHY; CHEMISTRY; HUMAN; MOLECULAR WEIGHT; MUTAGENESIS; PROTEIN DOMAIN; PROTEIN MULTIMERIZATION; RADIATION SCATTERING; TEMPERATURE;

HSP20 HEAT-SHOCK PROTEINS; HSP27 HEAT-SHOCK PROTEINS; HUMANS; MASS SPECTROMETRY; MOLECULAR CHAPERONES; MOLECULAR WEIGHT; MUTAGENESIS; PROTEIN DOMAINS; PROTEIN MULTIMERIZATION; RECOMBINANT PROTEINS; SCATTERING, RADIATION; TEMPERATURE;

EID: 84992111128     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2016.10.002     Document Type: Article

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