Inherent chaperone-like activity of aspartic proteases reveals a distant evolutionary relation to double-ψ barrel domains of AAA-ATPases

Protein Science

Volumn 16, Issue 4, 2007, Pages 644-653

  Hulko, Michael ^a   Lupas, Andrei N ^a   Martin, Jörg ^a  

^a MAX PLANCK INSTITUTE FOR DEVELOPMENTAL BIOLOGY   (Germany)

Author keywords

AAA ATPase; Aspartic proteases; Chaperones; Double barrel; Protein evolution

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ASPARTIC PROTEINASE; CHAPERONE; CITRATE SYNTHASE; MONOMER; PEPSIN A; THERMOLYSIN; THIOSULFATE SULFURTRANSFERASE; TRYPSIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; GEL PERMEATION CHROMATOGRAPHY; HUMAN IMMUNODEFICIENCY VIRUS 1; MOLECULAR CLONING; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN ISOLATION; PROTEIN STRUCTURE;

EVOLUTION; HIV PROTEASE; MOLECULAR CHAPERONES; PEPSIN A; PROTEIN DENATURATION; THERMOLYSIN; TRYPSIN;

HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 33947727001     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.062478607     Document Type: Article

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