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3.6.4.7
A mechanistic perspective on PEX1 and PEX6, two AAA+ proteins of the peroxisomal protein import machinery
Saccharomyces cerevisiae
3.6.4.7
ATP-driven processes of peroxisomal matrix protein import
Saccharomyces cerevisiae
3.6.4.7
Cysteine-specific ubiquitination protects the peroxisomal import receptor Pex5p against proteasomal degradation
Saccharomyces cerevisiae
3.6.4.7
Disparate peroxisome-related defects in Arabidopsis pex6 and pex26 mutants link peroxisomal retrotranslocation and oil body utilization
Arabidopsis thaliana
3.6.4.7
Nucleotide-dependent assembly of the peroxisomal receptor export complex
Saccharomyces cerevisiae
3.6.4.7
Peroxisomal monoubiquitinated PEX5 interacts with the AAA ATPases PEX1 and PEX6 and is unfolded during its dislocation into the cytosol
Homo sapiens
3.6.4.7
Receptor recognition by the peroxisomal AAA complex depends on the presence of the ubiquitin moiety and is mediated by Pex1p
Saccharomyces cerevisiae
3.6.4.7
Structure and function of p97 and Pex1/6 type II AAA+ complexes
Saccharomyces cerevisiae
3.6.4.7
Structure and function of p97 and Pex1/6 type II AAA+ complexes
Caenorhabditis elegans
3.6.4.7
Structures of the double-ring AAA ATPase Pex1/Pex6 involved in peroxisome biogenesis
Saccharomyces cerevisiae
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