PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
11282911-9	2001	CONCLUSIONS: These results suggest that mitochondrial chaperonins HSP60 and HSP10 in combination or individually play an important role in maintaining mitochondrial integrity and capacity for ATP generation, which are the crucial factors in determining survival of cardiac myocytes undergoing ischemia/reperfusion injury.	Adenosine Triphosphate	192-195	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	76-81
32431608-9	2020	Infusion of 5-10-sP (n = 5) and HSP10 (n = 5) into isolated hearts before I/R improved mitochondrial ADP-stimulated respiration, ATP production and prevented mitochondrial ROS formation compared to the I/R group (n = 5); this effect was abrogated by 5HD and chelerythrine.	Adenosine Diphosphate	101-104	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	32-37
32431608-9	2020	Infusion of 5-10-sP (n = 5) and HSP10 (n = 5) into isolated hearts before I/R improved mitochondrial ADP-stimulated respiration, ATP production and prevented mitochondrial ROS formation compared to the I/R group (n = 5); this effect was abrogated by 5HD and chelerythrine.	Adenosine Triphosphate	129-132	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	32-37
32431608-9	2020	Infusion of 5-10-sP (n = 5) and HSP10 (n = 5) into isolated hearts before I/R improved mitochondrial ADP-stimulated respiration, ATP production and prevented mitochondrial ROS formation compared to the I/R group (n = 5); this effect was abrogated by 5HD and chelerythrine.	ros	172-175	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	32-37
32431608-9	2020	Infusion of 5-10-sP (n = 5) and HSP10 (n = 5) into isolated hearts before I/R improved mitochondrial ADP-stimulated respiration, ATP production and prevented mitochondrial ROS formation compared to the I/R group (n = 5); this effect was abrogated by 5HD and chelerythrine.	5-(2-Hydroxyethyl)nonane-1,9-Diol	250-253	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	32-37
32431608-9	2020	Infusion of 5-10-sP (n = 5) and HSP10 (n = 5) into isolated hearts before I/R improved mitochondrial ADP-stimulated respiration, ATP production and prevented mitochondrial ROS formation compared to the I/R group (n = 5); this effect was abrogated by 5HD and chelerythrine.	chelerythrine	258-271	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	32-37
32431608-11	2020	5HD reduced the ADP-stimulated respiration in the HSP10 group (65.84 +- 3.3 nmol O2/min/mg PTN), ATP production (193.7 +- 12.1 mumol ATP/200mug PTN) and increased ROS in the 5-10-sP group (274.4 +- 21.7 nmol H2O2/200 mug PTN).	Adenosine Diphosphate	16-19	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	50-55
32431608-14	2020	HSP10 can act directly on mitochondria and protects against hypoxia/reoxygenation injury by mKATP activation.	mkatp	92-97	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	0-5
31155149-12	2019	Further research revealed that ghrelin treatment significantly activated the UPRmt as demonstrated by the increased expression of heat shock protein 60 (HSP60), heat shock protein 10 (HSP10), caseinolytic protease 1 (CLPP1), and high-temperature requirement protein A2 (HTRA2).	Ghrelin	31-38	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	161-182
31155149-12	2019	Further research revealed that ghrelin treatment significantly activated the UPRmt as demonstrated by the increased expression of heat shock protein 60 (HSP60), heat shock protein 10 (HSP10), caseinolytic protease 1 (CLPP1), and high-temperature requirement protein A2 (HTRA2).	Ghrelin	31-38	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	184-189
23056601-8	2012	Significant alterations were found in the expression of heat shock proteins (HSP27, alpha-B crystallin, HSP70, HSP10 and HSP60), whose levels were markedly up-regulated after morphine treatment or withdrawal.	Morphine	175-183	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	111-116
15544816-5	2004	From size-exclusion chromatography experiments in the presence of various concentrations of Gdn-HCl at 25 degrees C, both cpn10s showed unfolding-refolding characteristics similar to those of GroES, i.e. two-stage unfolding reactions that include formation of a partially folded monomer.	gdn-hcl	92-99	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	122-127
15544816-6	2004	Although the partially folded monomer of TmaES was considerably more stable compared to GroES and RatES, it was found that the overall stabilities of all three cpn10s were achieved significantly by inter-subunit interactions.	tmaes	41-46	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	160-165
9262643-1	1997	Chaperonin 10 protein from Rattus norvegicus (Rat cpn 10) has been reported to bind chaperonin 60 from Escherichia coli (GroEL) in an ATP-dependent manner.	Adenosine Triphosphate	134-137	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	0-13
9262643-5	1997	Rat cpn 10 was prepared using a highly effective synthetic protocol involving HBTU/HOBt activation and capping with N-(2-chlorobenzyloxycarbonyloxy) succinimide to terminate unreacted amino groups.	2-(1H-benzotriazol-1-yl)-1,1,3,3-tetramethyluronium hexafluorophosphate	78-82	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	4-10
9262643-1	1997	Chaperonin 10 protein from Rattus norvegicus (Rat cpn 10) has been reported to bind chaperonin 60 from Escherichia coli (GroEL) in an ATP-dependent manner.	Adenosine Triphosphate	134-137	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	50-56
9262643-5	1997	Rat cpn 10 was prepared using a highly effective synthetic protocol involving HBTU/HOBt activation and capping with N-(2-chlorobenzyloxycarbonyloxy) succinimide to terminate unreacted amino groups.	1-hydroxybenzotriazole	83-87	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	4-10
9262643-5	1997	Rat cpn 10 was prepared using a highly effective synthetic protocol involving HBTU/HOBt activation and capping with N-(2-chlorobenzyloxycarbonyloxy) succinimide to terminate unreacted amino groups.	n-(2-chlorobenzyloxycarbonyloxy) succinimide	116-160	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	4-10
9262643-2	1997	Chemically synthesized Rat cpn10 was immobilized in a defined orientation to agarose-bound monomeric avidin using a reversible biotinylated affinity label (1), attached to the N alpha-terminal residue.	Sepharose	77-84	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	27-32
9223007-3	1995	We report the application of a biotinylated probe, activated as the succinimidyl carbonate, for the purification of a 101 residue chaperonin protein from Rattus norvegicus (rat cpn10), previously synthesized using an optimized synthetic protocol.	succinimidyl carbonate	68-90	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	177-182
8844261-5	1996	Highly homogeneous Rat Cpn10 was obtained using an optimised synthetic strategy and one-step purification procedure (method C), involving (i) HBTU/HOBt activation, (ii) N-(2-chlorobenzyloxycarbonyloxy)succinimide as capping agent and (iii) the incorporation of a reversible Fmoc-based chromatographic probe, derivatised with a lipophilic group for fast one-step RP purification, to give an overall yield of 9.6%.	2-(1H-benzotriazol-1-yl)-1,1,3,3-tetramethyluronium hexafluorophosphate	142-146	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	23-28
8844261-5	1996	Highly homogeneous Rat Cpn10 was obtained using an optimised synthetic strategy and one-step purification procedure (method C), involving (i) HBTU/HOBt activation, (ii) N-(2-chlorobenzyloxycarbonyloxy)succinimide as capping agent and (iii) the incorporation of a reversible Fmoc-based chromatographic probe, derivatised with a lipophilic group for fast one-step RP purification, to give an overall yield of 9.6%.	1-hydroxybenzotriazole	147-151	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	23-28
8844261-5	1996	Highly homogeneous Rat Cpn10 was obtained using an optimised synthetic strategy and one-step purification procedure (method C), involving (i) HBTU/HOBt activation, (ii) N-(2-chlorobenzyloxycarbonyloxy)succinimide as capping agent and (iii) the incorporation of a reversible Fmoc-based chromatographic probe, derivatised with a lipophilic group for fast one-step RP purification, to give an overall yield of 9.6%.	Nitrogen	169-170	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	23-28
8844261-5	1996	Highly homogeneous Rat Cpn10 was obtained using an optimised synthetic strategy and one-step purification procedure (method C), involving (i) HBTU/HOBt activation, (ii) N-(2-chlorobenzyloxycarbonyloxy)succinimide as capping agent and (iii) the incorporation of a reversible Fmoc-based chromatographic probe, derivatised with a lipophilic group for fast one-step RP purification, to give an overall yield of 9.6%.	succinimide	200-212	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	23-28
9223007-5	1995	Free rat cpn10 was released from avidin-agarose column with 5% aqueous triethylamine and after desalting by RP-HPLC gave 9.9% recovery.	Sepharose	40-47	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	9-14
9223007-5	1995	Free rat cpn10 was released from avidin-agarose column with 5% aqueous triethylamine and after desalting by RP-HPLC gave 9.9% recovery.	triethylamine	71-84	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	9-14
7904573-3	1994	It is concluded that cpn10, unlike the majority of nuclear-encoded proteins of the mitochondrial matrix, is synthesised without a cleavable targeting signal and that, following removal of the initiating methionine, it becomes acetylated prior to mitochondrial import.	Methionine	203-213	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	21-26
7906228-1	1994	Chaperonin-60 and chaperonin-10 form stable binary complexes in the presence of ATP.	Adenosine Triphosphate	80-83	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	18-31
7906228-3	1994	ATP-dependent binary complexes formed between chaperonin-60 and chaperonin-10 in potato mitochondrial extracts were isolated by affinity chromatography on a column of immobilised chaperonin-60 antibodies.	Adenosine Triphosphate	0-3	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	64-77
7904573-4	1994	Incubation of 3H- or 35S-labelled cpn10 with mitochondria confirms these conclusions and shows that cpn10 is imported into mitochondria in an energy-dependent process which is inhibited by the presence of 2,4-dinitrophenol.	Tritium	14-16	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	100-105
7904573-4	1994	Incubation of 3H- or 35S-labelled cpn10 with mitochondria confirms these conclusions and shows that cpn10 is imported into mitochondria in an energy-dependent process which is inhibited by the presence of 2,4-dinitrophenol.	Sulfur-35	21-24	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	34-39
7904573-4	1994	Incubation of 3H- or 35S-labelled cpn10 with mitochondria confirms these conclusions and shows that cpn10 is imported into mitochondria in an energy-dependent process which is inhibited by the presence of 2,4-dinitrophenol.	Sulfur-35	21-24	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	100-105
7904573-4	1994	Incubation of 3H- or 35S-labelled cpn10 with mitochondria confirms these conclusions and shows that cpn10 is imported into mitochondria in an energy-dependent process which is inhibited by the presence of 2,4-dinitrophenol.	2,4-Dinitrophenol	205-222	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	34-39
7904573-4	1994	Incubation of 3H- or 35S-labelled cpn10 with mitochondria confirms these conclusions and shows that cpn10 is imported into mitochondria in an energy-dependent process which is inhibited by the presence of 2,4-dinitrophenol.	2,4-Dinitrophenol	205-222	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	100-105
1348860-6	1992	This process depended completely upon rat Hsp10 and was abolished in the presence of a nonhydrolyzable ATP analogue.	Adenosine Triphosphate	103-106	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	42-47
9346868-2	1994	Two syntheses of rat cpn10 were performed, the first using a classical carbodiimide-mediated double coupling protocol (Method A) and the second a more efficient HBTU/HOBT/single coupling procedure (Method B).	Carbodiimides	71-83	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	21-26
9346868-2	1994	Two syntheses of rat cpn10 were performed, the first using a classical carbodiimide-mediated double coupling protocol (Method A) and the second a more efficient HBTU/HOBT/single coupling procedure (Method B).	1-hydroxybenzotriazole	166-170	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	21-26
8101099-0	1993	The complete primary structure of rat chaperonin 10 reveals a putative beta alpha beta nucleotide-binding domain with homology to p21ras.	alpha beta nucleotide	76-97	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	38-51
1977163-3	1990	Thus, like the bacterial homologue, mitochondrial cpn10 facilitates a K(+)- and Mg.ATP-dependent discharge of unfolded (or partially folded) ribulose bisphosphate carboxylase from bacterial chaperonin 60 (cpn60; also known as groEL).	Adenosine Triphosphate	83-86	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	50-55
1977163-4	1990	Instrumental to its identification, mitochondrial cpn10 and bacterial cpn60 form a stable complex in the presence of Mg.ATP.	Magnesium	117-119	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	50-55
1977163-4	1990	Instrumental to its identification, mitochondrial cpn10 and bacterial cpn60 form a stable complex in the presence of Mg.ATP.	Adenosine Triphosphate	120-123	heat shock protein family E (Hsp10) member 1	Rattus norvegicus	50-55