PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
34132035-0	2021	Quantitative Proteomics Reveals Arsenic Attenuates Stem-Loop Binding Protein Stability via a Chaperone Complex Containing Heat Shock Proteins and ERp44.	Arsenic	32-39	endoplasmic reticulum protein 44	Homo sapiens	146-151	
34132035-5	2021	In this study, we established the first comprehensive SLBP interaction network by affinity purification-mass spectrometry (AP-MS) analysis, and further demonstrated arsenic enhanced the association between SLBP and a crucial chaperone complex containing heat shock proteins (HSPs) and ERp44.	Arsenic	165-172	endoplasmic reticulum protein 44	Homo sapiens	285-290	
34132035-7	2021	Taken together, our study provides a potential new mechanism that a chaperone complex containing HSPs and ERp44 attenuates the stability of SLBP under both normal and arsenic exposure conditions, which could be essential for arsenic-induced high cell migration.	Arsenic	167-174	endoplasmic reticulum protein 44	Homo sapiens	106-111	
34132035-7	2021	Taken together, our study provides a potential new mechanism that a chaperone complex containing HSPs and ERp44 attenuates the stability of SLBP under both normal and arsenic exposure conditions, which could be essential for arsenic-induced high cell migration.	Arsenic	225-232	endoplasmic reticulum protein 44	Homo sapiens	106-111