Ddi1-like protein from Leishmania major is an active aspartyl proteinase

Cell Stress and Chaperones

Volumn 18, Issue 2, 2013, Pages 171-181

  Perteguer, María J ^a   Gómez Puertas, Paulino ^b   Cañavate, Carmen ^c   Dagger, Francehuli ^d   Gárate, Teresa ^a   Valdivieso, Elizabeth ^d  

^a INSTITUTO DE SALUD CARLOS III   (Spain)

^b CENTRO DE BIOLOGÍA MOLECULAR SEVERO OCHOA   (Spain)

^c WORLD HEALTH ORGANIZATION   (Switzerland)

^d FACULTAD DE CIENCIAS   (Venezuela)

Author keywords

Aspartyl proteinase; Cloning; Ddi1; Leishmania; Retroviral protease; Ubiquitin receptor proteins

Indexed keywords

ALANINE; ASPARTIC ACID; ASPARTIC PROTEINASE; COMPLEMENTARY DNA; DNA DAMAGE INDUCIBLE 1 PROTEIN; GLYCINE; PROTOZOAL PROTEIN; RECOMBINANT PROTEIN; SERINE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BACULOVIRUS; BIOCHEMISTRY; CONTROLLED STUDY; COOH TERMINAL UBIQUITIN ASSOCIATED DOMAIN; ENZYME SPECIFICITY; INSECT CELL; LEISHMANIA MAJOR; MOLECULAR MODEL; NH2 TERMINAL UBIQUITIN LIKE DOMAIN; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN ISOLATION; PROTEIN STRUCTURE; RETROVIRAL ASPARTYL PROTEINASE DOMAIN; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ASPARTIC ACID PROTEASES; COMPUTATIONAL BIOLOGY; DIMERIZATION; KINETICS; LEISHMANIA MAJOR; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTOZOAN PROTEINS; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE ALIGNMENT; SF9 CELLS; SUBSTRATE SPECIFICITY; UBIQUITIN;

EUKARYOTA; LEISHMANIA MAJOR; LEISHMANIA SP.; SACCHAROMYCES CEREVISIAE;

EID: 84878861233     PISSN: 13558145     EISSN: 14661268     Source Type: Journal    
DOI: 10.1007/s12192-012-0368-9     Document Type: Article

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