MPN+, a putative catalytic motif found in a subset of MPN domain proteinsfrom eukaryotes and prokaryotes, is critical for Rpn11 function

BMC Biochemistry

Volumn 3, Issue , 2002, Pages 1-12

  Maytal Kivity, Vered ^a   Reis, Noa ^a   Hofmann, Kay ^b   Glickman, Michael H ^a  

^a TECHNION ISRAEL INSTITUTE OF TECHNOLOGY   (Israel)

^b Memorec Biotec GmbH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID DERIVATIVE; CYSTEINE; HYDROLASE; METALLOPROTEINASE; MUTANT PROTEIN; PROTEASOME; PROTEINASE; PRSS27 PROTEIN, HUMAN; RPN11 PROTEIN, S CEREVISIAE; RPN11 PROTEIN, S POMBE; SACCHAROMYCES CEREVISIAE PROTEIN; SCHIZOSACCHAROMYCES POMBE PROTEIN; SERINE PROTEINASE; TRANSACTIVATOR PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CELL GROWTH; EUKARYOTE; OXIDATIVE STRESS; PHENOTYPE; PROKARYOTE; PROTEIN DEGRADATION; PROTEIN DOMAIN; SEQUENCE ALIGNMENT; SITE DIRECTED MUTAGENESIS; TEMPERATURE DEPENDENCE; AMINO ACID SEQUENCE; CHEMISTRY; ENZYME ACTIVE SITE; EUKARYOTIC CELL; FACTUAL DATABASE; GENETICS; MOLECULAR GENETICS; PHYSIOLOGY; PROKARYOTIC CELL;

ARCHAEA; EUKARYOTA; PROKARYOTA;

AMINO ACID SEQUENCE; CATALYTIC DOMAIN; DATABASES, FACTUAL; ENDOPEPTIDASES; EUKARYOTIC CELLS; MOLECULAR SEQUENCE DATA; PROKARYOTIC CELLS; SACCHAROMYCES CEREVISIAE PROTEINS; SCHIZOSACCHAROMYCES POMBE PROTEINS; SERINE ENDOPEPTIDASES; TRANS-ACTIVATORS;

EID: 34248350363     PISSN: 14712091     EISSN: None     Source Type: Journal    
DOI: 10.1186/1471-2091-3-28     Document Type: Article

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