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- W2330431723 endingPage "1100" @default.
- W2330431723 startingPage "1091" @default.
- W2330431723 abstract "The DNA sequence has been determined of a gene from Leishmania major that shares sequence identity with members of the eukaryotic heat shock protein (hsp) 70 gene family. The deduced open reading frame for translation shares a number of features common to hsp70 stress proteins, including conserved amino acids implicated in ATP binding and a putative calmodulin-binding site. In addition, the protein has an N-terminal sequence characteristic of a mitochondrial targeting signal. Specific antibodies to this protein, generated by the use of recombinant fusion peptides, recognise a 65 kDa molecule of pI 6.7. This molecule is constitutively expressed and localises to the mitochondrion in all stages of the parasite life cycle. These features suggest a role for this protein as a molecular chaperone in Leishmania." @default.
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- W2330431723 date "1993-04-01" @default.
- W2330431723 modified "2023-09-27" @default.
- W2330431723 title "Expression of a mitochondrial stress protein in the protozoan parasite Leishmania major" @default.
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- W2330431723 doi "https://doi.org/10.1242/jcs.104.4.1091" @default.
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