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ProteomicsIdentification of protein N-termini in Cyanophora paradoxa cyanelles: Transit peptide composition and sequence determinants for precursor maturation
Glaucophytes, rhodophyta and chloroplastida represent the three evolutionary lineages that diverged after primary endosymbiosis. Comparative analyses between members of these three lineages are a rich source of information on ancestral plastid features. We analyzed the composition and the cleavage s...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2016-12-14 | PXD002187 | Pride
Cyanophera paradoxa Ms Chloroplast transit peptide Tails 
ProteomicsOne-step N-terminomics based on isolation of protein N-terminal peptides from LysargiNase digests by tip-based strong cation exchange chromatography
Large-scale isolation of protein N-terminal peptides from LysargiNase digests was achieved by one-step strong cation exchange chromatography with disposable and parallel-processable pipette-tip columns. Novel cleavage sites for signal or transit peptides and non-canonical translation initiation site...
ORGANISM(S): Homo Sapiens (human) 
2024-08-13 | PXD048917 | JPOST Repository
UnknownPlastid transit peptides-where do they come from and where do they all belong? Multi-genome and pan-genomic assessment of chloroplast transit peptide evolution.
Not available
S-EPMC7456531 | biostudies-literature
UnknownCharacterization of signal and transit peptides based on motif composition and taxon-specific patterns.
Not available
S-EPMC10514287 | biostudies-literature
UnknownColonic Transit Time and Gut Peptides in Adult Patients with Slow and Normal Colonic Transit Constipation.
Not available
S-EPMC5610809 | biostudies-literature
UnknownTransit Peptides Often Require Downstream Unstructured Sequence for Efficient Chloroplast Import in Chlamydomonas reinhardtii.
Not available
S-EPMC9133816 | biostudies-literature
UnknownNon-native, N-terminal Hsp70 molecular motor recognition elements in transit peptides support plastid protein translocation.
Not available
S-EPMC4367265 | biostudies-literature
ProteomicsPeroxisomal targeting of the protein phosphatase Ptc5 via mitochondrial transit
Correct intracellular distribution of proteins is critical for the function of eukaryotic cells. Certain proteins are targeted to more than one cellular compartment, e.g. to mitochondria and peroxisomes. The protein phosphatase Ptc5 from Saccharomyces cerevisiae contains an N-terminal mitochondrial ...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2020-05-22 | PXD018591 | Pride
Protein phosphatase Yeast Peroxisome Ptc5 
UnknownImproving Signal and Transit Peptide Predictions Using AlphaFold2-predicted Protein Structures.
Not available
S-EPMC10843742 | biostudies-literature
UnknownEvolution of rubisco complex small subunit transit peptides from algae to plants.
Not available
S-EPMC5571161 | biostudies-literature
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