PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
14517240-3	2003	Here we show that ERp44 mediates Ero1alpha ER localization through the formation of reversible mixed disulfides.	Disulfides	101-111	endoplasmic reticulum protein 44	Homo sapiens	18-23	
32161259-5	2020	sERr is relieved upon protein synthesis attenuation and is accompanied by the generation of large mixed disulfide bonded complexes, including ERp44.	Disulfides	104-113	endoplasmic reticulum protein 44	Homo sapiens	142-147	
11847130-5	2002	ERp44 forms mixed disulfides with both hEROs and cargo folding intermediates.	Disulfides	18-28	endoplasmic reticulum protein 44	Homo sapiens	0-5	
35247515-0	2022	Inhibitors of ERp44, PDIA1, and AGR2 induce disulfide-mediated oligomerization of Death Receptors 4 and 5 and cancer cell death.	Disulfides	44-53	endoplasmic reticulum protein 44	Homo sapiens	14-19	
34957576-0	2022	Biogenesis of secretory immunoglobulin M requires intermediate non-native disulfide bonds and engagement of the protein disulfide isomerase ERp44.	Disulfides	120-129	endoplasmic reticulum protein 44	Homo sapiens	140-145	
34957576-6	2022	The rearrangement of the C-terminal tails into a native quaternary structure is guaranteed by the engagement of protein disulfide isomerase ERp44, which attacks the non-native C575 bonds.	Disulfides	120-129	endoplasmic reticulum protein 44	Homo sapiens	140-145	
33173013-5	2020	ERp44 also patrols the secretion of correctly assembled disulfide-linked oligomeric proteins.	Disulfides	56-65	endoplasmic reticulum protein 44	Homo sapiens	0-5	
28373561-10	2017	Mutational analyses showed that ERp44 forms mixed disulfides with specific cysteines residing on negatively charged loop regions of Ero1alpha.	Disulfides	50-60	endoplasmic reticulum protein 44	Homo sapiens	32-37	
29858230-4	2018	We further show that ER oxidoreductin 1alpha (Ero1alpha), the pivotal sulfhydryl oxidase that catalyzes disulfide formation in the ER, is phosphorylated by Fam20C in the Golgi apparatus and retrograde-transported to the ER mediated by ERp44.	Disulfides	104-113	endoplasmic reticulum protein 44	Homo sapiens	235-240	
23685074-3	2013	Here we unveil how ERp44 cycles between cisGolgi and ER in a pH-regulated manner, patrolling assembly of disulfide-linked oligomers such as IgM and adiponectin.	Disulfides	105-114	endoplasmic reticulum protein 44	Homo sapiens	19-24	
27642162-4	2016	Our data reveal that ERp44 binds the oxidized form of peroxiredoxin 4 via thiol-disulfide interchange reactions.	Disulfides	80-89	endoplasmic reticulum protein 44	Homo sapiens	21-26	
25512553-4	2014	We previously reported that an endoplasmic reticulum chaperone, ERp44, binds to Cys200 and Cys209 residues of SERT to build a disulfide bond.	Disulfides	126-135	endoplasmic reticulum protein 44	Homo sapiens	64-69	
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.	Disulfides	159-168	endoplasmic reticulum protein 44	Homo sapiens	83-88	
22451649-1	2012	In heterologous and endogenous expression systems, we studied the role of ERp44 and its complex partner endoplasmic reticulum (ER) oxidase 1-alpha (Ero1-Lalpha) in mechanisms regulating disulfide bond formation for serotonin transporter (SERT), an oligomeric glycoprotein.	Disulfides	186-195	endoplasmic reticulum protein 44	Homo sapiens	74-79	
24489546-4	2013	By virtue of the same cysteine, unassembled secretory IgM subunits are recognized and retained (via mixed disulfide bonds) by members of the protein disulfide isomerase family, in particular ERp44.	Disulfides	106-115	endoplasmic reticulum protein 44	Homo sapiens	191-196	
22451649-2	2012	ERp44 is an ER lumenal chaperone protein that favors the maturation of disulfide-linked oligomeric proteins.	Disulfides	71-80	endoplasmic reticulum protein 44	Homo sapiens	0-5	
22451649-13	2012	Based on these collective findings, we hypothesize that ERp44 together with Ero1-Lalpha plays an important role in disulfide formation of SERT, which may be a prerequisite step for the assembly of SERT molecules in oligomeric form.	Disulfides	115-124	endoplasmic reticulum protein 44	Homo sapiens	56-61	
18178549-3	2008	Here we show that ERp44 interacts with FGE forming heterodimeric and, to a lesser extent, also heterotetrameric and octameric complexes, which are stabilized through disulfide bonding between cysteine 29 of ERp44 and cysteines 50 and 52 in the N-terminal region of FGE.	Disulfides	166-175	endoplasmic reticulum protein 44	Homo sapiens	18-23	
18178549-3	2008	Here we show that ERp44 interacts with FGE forming heterodimeric and, to a lesser extent, also heterotetrameric and octameric complexes, which are stabilized through disulfide bonding between cysteine 29 of ERp44 and cysteines 50 and 52 in the N-terminal region of FGE.	Disulfides	166-175	endoplasmic reticulum protein 44	Homo sapiens	207-212