PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25680528-3	2015	We also find that mutations in the Atg8-family interacting motif (AIM) of Atg3 significantly impairs the PAS/IM localization of Atg3, resulting in inefficient IM expansion.	Aminosalicylic Acid	105-108	ubiquitin-like protein ATG8	Saccharomyces cerevisiae S288C	35-39	
25680528-4	2015	It is suggested that the AIM-mediated PAS/IM localization of Atg3 facilitates membrane expansion in these structures probably by ensuring active production of Atg8-PE on the membranes.	Aminosalicylic Acid	38-41	ubiquitin-like protein ATG8	Saccharomyces cerevisiae S288C	159-163	
18758231-6	2008	In turn, under nutrient-rich conditions, the increased level of Atg11 causes the recruitment of higher than normal levels of Atg8 and Atg9 to the PAS, resulting in the formation of more Cvt vesicles, whereas the vesicle size is not affected.	Aminosalicylic Acid	146-149	ubiquitin-like protein ATG8	Saccharomyces cerevisiae S288C	125-129	
25500271-6	2015	It is involved in a step downstream of PAS (phagophore assembly site) scaffold assembly, and upstream of the recruitment of Atg1, Atg14, Atg5 and Atg8.	Aminosalicylic Acid	39-42	ubiquitin-like protein ATG8	Saccharomyces cerevisiae S288C	146-150	
23078654-4	2013	Mutant cells could not transport Atg8 and Atg9 to the pre-autophagosomal structure/phagophore assembly site (PAS) properly, resulting in multiple Atg8 dots and Atg9 dots dispersed in the cytoplasm.	Aminosalicylic Acid	109-112	ubiquitin-like protein ATG8	Saccharomyces cerevisiae S288C	146-150	
24374083-1	2014	The Atg2-Atg18 complex acts in parallel to Atg8 and regulates Atg9 recycling from phagophore assembly site (PAS) during autophagy in yeast.	Aminosalicylic Acid	108-111	ubiquitin-like protein ATG8	Saccharomyces cerevisiae S288C	43-47	
22240591-2	2012	A ubiquitin-like system mediates the conjugation of the C terminus of Atg8 to the lipid phosphatidylethanolamine (PE), and this conjugate (Atg8-PE) plays a crucial role in autophagosome formation at the phagophore assembly site/pre-autophagosomal structure (PAS).	Aminosalicylic Acid	258-261	ubiquitin-like protein ATG8	Saccharomyces cerevisiae S288C	70-74	
22240591-2	2012	A ubiquitin-like system mediates the conjugation of the C terminus of Atg8 to the lipid phosphatidylethanolamine (PE), and this conjugate (Atg8-PE) plays a crucial role in autophagosome formation at the phagophore assembly site/pre-autophagosomal structure (PAS).	Aminosalicylic Acid	258-261	ubiquitin-like protein ATG8	Saccharomyces cerevisiae S288C	139-143	
22240591-6	2012	We find that Atg8-PE accumulates on various organelle membranes including the vacuole, the endosome and the ER in these cells, which depletes unlipidated Atg8 and thereby attenuates its localization to the PAS.	Aminosalicylic Acid	206-209	ubiquitin-like protein ATG8	Saccharomyces cerevisiae S288C	13-17	
30837368-5	2019	In tip20 conditional mutant yeast, the transport of Atg8 was impaired during starvation, resulting in multiple Atg8 puncta dispersed outside the vacuole that could not be transported to the pre-autophagosomal structure/phagophore assembly site (PAS).	Aminosalicylic Acid	245-248	ubiquitin-like protein ATG8	Saccharomyces cerevisiae S288C	52-56	
18625846-5	2008	We find that an increase in the amount of Atg11 at the PAS enhances the recruitment of Atg8 and Atg9 to this site and facilitates the formation of more cytoplasm-to-vacuole targeting vesicles.	Aminosalicylic Acid	55-58	ubiquitin-like protein ATG8	Saccharomyces cerevisiae S288C	87-91	
18625846-7	2008	During autophagy, the amount of Atg8 at the PAS showed a periodic change, indicating the formation of autophagosomes.	Aminosalicylic Acid	44-47	ubiquitin-like protein ATG8	Saccharomyces cerevisiae S288C	32-36	
30810528-5	2019	As with the PI3P-dependent mechanism, Atg12-Atg5-Atg16 recruited via the Atg12-dependent mechanism stimulates Atg8 lipidation, but also has the specific function of facilitating PAS scaffold assembly.	Aminosalicylic Acid	178-181	ubiquitin-like protein ATG8	Saccharomyces cerevisiae S288C	110-114	
30810528-2	2019	Previous studies in yeast revealed that the autophagy-related E3 complex Atg12-Atg5-Atg16 is recruited to the PAS via Atg16 interaction with Atg21, which binds phosphatidylinositol 3-phosphate (PI3P) produced at the PAS, to stimulate conjugation of the ubiquitin-like protein Atg8 to phosphatidylethanolamine.	Aminosalicylic Acid	110-113	ubiquitin-like protein ATG8	Saccharomyces cerevisiae S288C	276-280	
30810528-2	2019	Previous studies in yeast revealed that the autophagy-related E3 complex Atg12-Atg5-Atg16 is recruited to the PAS via Atg16 interaction with Atg21, which binds phosphatidylinositol 3-phosphate (PI3P) produced at the PAS, to stimulate conjugation of the ubiquitin-like protein Atg8 to phosphatidylethanolamine.	Aminosalicylic Acid	216-219	ubiquitin-like protein ATG8	Saccharomyces cerevisiae S288C	276-280