PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
24489546-6	2013	In this essay we discuss recent findings on how ERp44 governs such assembly control in a pH-dependent manner, shuttling between the cisGolgi and endoplasmic reticulum, and finally on how pERp1/MZB1, possibly as a co-chaperone of GRP94, may help to overrule the thiol-mediated retention in the activated B cell to give way to antibody secretion.	Sulfhydryl Compounds	261-266	endoplasmic reticulum protein 44	Homo sapiens	48-53	
27642162-0	2016	Crystal Structure of the ERp44-Peroxiredoxin 4 Complex Reveals the Molecular Mechanisms of Thiol-Mediated Protein Retention.	Sulfhydryl Compounds	91-96	endoplasmic reticulum protein 44	Homo sapiens	25-30	
27642162-4	2016	Our data reveal that ERp44 binds the oxidized form of peroxiredoxin 4 via thiol-disulfide interchange reactions.	Sulfhydryl Compounds	74-79	endoplasmic reticulum protein 44	Homo sapiens	21-26	
27642162-7	2016	This work provides insights into the mechanisms of thiol-mediated protein retention and indicates the key roles of ERp44 in this biochemical cycle to optimize oxidative folding and redox homeostasis.	Sulfhydryl Compounds	51-56	endoplasmic reticulum protein 44	Homo sapiens	115-120	
23806332-2	2013	(2013) show that a pH-induced conformational change in the quality control protein ERp44 allows retrieval of secretory proteins that contain free thiols via a disulfide linkage from postendoplasmic reticulum compartments to prevent their premature secretion.	Sulfhydryl Compounds	146-152	endoplasmic reticulum protein 44	Homo sapiens	83-88	
33173013-6	2020	Here, we discuss the mechanisms driving ERp44 substrate recognition, with important consequences on the definition of "thiol-mediated quality control".	Sulfhydryl Compounds	119-124	endoplasmic reticulum protein 44	Homo sapiens	40-45	
18552768-1	2008	ERp44 mediates thiol-dependent retention in the early secretory pathway, forming mixed disulphides with substrate proteins through its conserved CRFS motif.	Sulfhydryl Compounds	15-20	endoplasmic reticulum protein 44	Homo sapiens	0-5	
20044026-5	2010	Thiol-mediated retention of adiponectin occurs during transit through the ER, via direct interactions with chaperones including ERp44 and DsbA-L, and facilitates multimerisation and secretion.	Sulfhydryl Compounds	0-5	endoplasmic reticulum protein 44	Homo sapiens	128-133	
19019026-4	2008	Within adipocytes, it is retained in the lumen of the endoplasmic reticulum by binding to the thiol protein ERp44 and released by another thiol protein, Ero1-Lalpha.	Sulfhydryl Compounds	94-99	endoplasmic reticulum protein 44	Homo sapiens	108-113	
18178549-0	2008	ERp44 mediates a thiol-independent retention of formylglycine-generating enzyme in the endoplasmic reticulum.	Sulfhydryl Compounds	17-22	endoplasmic reticulum protein 44	Homo sapiens	0-5	
18177270-9	2008	ERp44 inhibits the secretion of adiponectin oligomers through a thiol-mediated retention.	Sulfhydryl Compounds	64-69	endoplasmic reticulum protein 44	Homo sapiens	0-5	
17805346-3	2007	We show here that ERp44, a soluble protein involved in thiol-mediated retention, interacts with ERGIC-53.	Sulfhydryl Compounds	55-60	endoplasmic reticulum protein 44	Homo sapiens	18-23	
17805346-10	2007	In this process, ERp44 couples thiol-dependent assembly and quality control.	Sulfhydryl Compounds	31-36	endoplasmic reticulum protein 44	Homo sapiens	17-22	
14517240-0	2003	Thiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44.	Sulfhydryl Compounds	0-5	endoplasmic reticulum protein 44	Homo sapiens	75-80	
14517240-5	2003	We conclude that ERp44 is a key element in thiol-mediated retention.	Sulfhydryl Compounds	43-48	endoplasmic reticulum protein 44	Homo sapiens	17-22