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Here, we report structural, biochemical, and cell biological analysis of the major selective cargo protein in budding yeast, aminopeptidase I (Ape1), and its complex with the receptor Atg19.
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Parkin then ubiquitinates a number of mitochondrial membrane proteins, both p62 and ULK1 are recruited toward mitochondria for selective cargo recognition (Li et al., 2015).
Upon starvation, Atg17-positive structures appear at aggregates of the selective cargo Ref(2 P/p62 near lysosomes.
Atg11 has been proposed to act as an adaptor protein that links receptors for selective cargo to the core autophagy machinery.
A second question, which may be related to the first, is how selective cargo engagement with the ciliary delivery mechanism is determined.
Phagophores assemble at aggregates of the selective cargo pro-aminopeptidase I in yeast, and p62-positive aggregates may play similar roles in metazoans [3].
NCOA4 is a selective cargo receptor for the autophagic turnover of ferritin, a process critical for regulation of intracellular iron bioavailability.
Precisely how these morphologically-distinct coats are formed, and whether all are functionally equivalent for selective cargo internalization is still disputed.
Autophagy is essentially a nonselective pathway but carries a number of selective cargoes.
The authors have used selective cargos to monitor MVB pathway, it is also important to use selective cargos (e.g. GFP-Atg8) to monitor autophagy and discuss their temporal relationship and relative contributions.
Our results for the early degradation of GFP-Atg8 and the continuous increase in autophagic degradation of highly abundant selective as well as non-selective cargoes throughout starvation are fully consistent with this model.
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