PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
30290218-5	2019	An emerging molecular mechanism behind such regulatory function is the activity of GSTP as a redox chaperonine responsible for the selective glutathionylation of protein Cys residues in the different subcellular compartments.	chaperonine	99-110	glutathione S-transferase pi 1	Homo sapiens	83-87
27189986-2	2016	Previous studies showed that protein interaction with the GroEL/GroES chaperonine and Hsp90 chaperone can buffer the impact of slightly deleterious mutations in the protein sequence.	chaperonine	70-81	GroEL	Escherichia coli	58-63
27189986-2	2016	Previous studies showed that protein interaction with the GroEL/GroES chaperonine and Hsp90 chaperone can buffer the impact of slightly deleterious mutations in the protein sequence.	chaperonine	70-81	chaperonin GroES	Escherichia coli	64-69
17846899-4	2007	As an illustration, it is demonstrated that the 800-kDa chaperonine GroEL synthesized with the D-S30 cell-free system had a uniform deuteration level of about 95% and assembled into its biologically active oligomeric form.	chaperonine	56-67	GroEL	Escherichia coli	68-73
34208178-3	2021	In fact, the molecule HSP70 acts as a chaperonine being able to impact at several level the homeostasis of neurons.	chaperonine	38-49	heat shock protein family A (Hsp70) member 4	Homo sapiens	22-27
9175768-1	1997	Paracentrotus lividus mitochondrial matrix contains a constitutive hsp of 56-KDa which cross reacts with a serum anti-hsp-60 chaperonine from yeast mitochondria.	chaperonine	125-136	chaperone ATPase HSP60	Saccharomyces cerevisiae S288C	118-124
7553912-2	1995	Both additional tubulins probably bind GTP but lack GTPase activity, while their synthesis requires the TCP1 chaperonine but is not autoregulated.	chaperonine	109-120	t-complex 1	Homo sapiens	104-108