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Volumn 27, Issue 6, 2001, Pages 539-549
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Hydrophobic residues within the predicted N-terminal amphiphilic α-helix of a plant mitochondrial targeting presequence play a major role in in vivo import
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Author keywords
Amphiphilic helix; GFP; Import; Mitochondrial presequence; Plant; Yeast
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Indexed keywords
AMINO ACID;
CARBOXY TERMINAL SEQUENCE;
CONFOCAL MICROSCOPY;
ENZYME SUBUNIT;
F1 ADENOSINE TRIPHOSPHATASE SYNTHASE;
GREEN FLUORESCENT PROTEIN;
HYDROPHOBICITY;
MITOCHONDRION;
POINT MUTATION;
PROTOPLAST;
WESTERN BLOTTING;
CELLS;
ENZYMES;
MICROSCOPIC EXAMINATION;
MUTAGENESIS;
TOBACCO;
GREEN FLUORESCENT PROTEIN (GFP);
PLANTS (BOTANY);
AMINO ACID SEQUENCE;
CONSERVED SEQUENCE;
GREEN FLUORESCENT PROTEINS;
LEUCINE;
LUMINESCENT PROTEINS;
MITOCHONDRIA;
MOLECULAR SEQUENCE DATA;
MUTAGENESIS, SITE-DIRECTED;
PLANT PROTEINS;
PROTEIN PRECURSORS;
PROTEIN PROCESSING, POST-TRANSLATIONAL;
PROTEIN SORTING SIGNALS;
PROTEIN STRUCTURE, SECONDARY;
PROTEIN TRANSPORT;
PROTON-TRANSLOCATING ATPASES;
RECOMBINANT FUSION PROTEINS;
SACCHAROMYCES CEREVISIAE;
SEQUENCE DELETION;
TOBACCO;
TRANSFORMATION, GENETIC;
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EID: 0034796437
PISSN: 09607412
EISSN: None
Source Type: Journal
DOI: 10.1046/j.1365-313X.2001.01098.x Document Type: Article |
Times cited : (59)
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References (36)
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