The pertussis toxin S1 subunit is a thermally unstable protein susceptible to degradation by the 20S proteasome

Biochemistry

Volumn 45, Issue 46, 2006, Pages 13734-13740

  Pande, Abhay H ^a,b   Moe, David ^a   Jamnadas, Maneesha ^a   Tatulian, Suren A ^a   Teter, Ken ^a  

^a UNIVERSITY OF CENTRAL FLORIDA   (United States)

^b BIRLA INSTITUTE OF TECHNOLOGY AND SCIENCE   (India)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIODEGRADATION; CONFORMATIONS; MOLECULAR DYNAMICS;

ENDOPLASMIC RETICULUM (ER); ER-ASSOCIATED DEGRADATION (ERAD); INTOXICATION; TOXIN TRANSLOCATION;

PROTEINS;

ADENOSINE DIPHOSPHATE; GUANINE NUCLEOTIDE BINDING PROTEIN; LYSINE; NICOTINAMIDE ADENINE DINUCLEOTIDE; PERTUSSIS TOXIN A; PERTUSSIS TOXIN B; PERTUSSIS TOXIN S1; PROTEASOME; PROTEIN SUBUNIT; TOXIN; UBIQUITIN; UNCLASSIFIED DRUG;

ARTICLE; CELL SURFACE; CONTROLLED STUDY; CYTOSOL; ENDOPLASMIC RETICULUM; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME DENATURATION; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SUBUNIT; HEAT SENSITIVITY; IN VITRO STUDY; INTRACELLULAR TRANSPORT; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN ISOLATION; PROTEIN PROTEIN INTERACTION; PROTEIN TRANSPORT; REGULATORY MECHANISM; THERMOSTABILITY; TOXIN ANALYSIS; UBIQUITINATION;

CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; HYDROLYSIS; PERTUSSIS TOXIN; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN DENATURATION; SPECTROPHOTOMETRY, ULTRAVIOLET; SURFACE-ACTIVE AGENTS; THERMODYNAMICS;

EID: 33751229337     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061175+     Document Type: Article

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