PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
34495738-5	2021	Here, through a compound screen, we found that two bis-biguanide compounds, Chlorhexidine and Alexidine, modified the activity of the inner mitochondrial membrane (IMM)-resident protease OMA1 by altering the integrity of the IMM.	bis-biguanide	51-64	OMA1 zinc metallopeptidase	Homo sapiens	187-191
34495738-5	2021	Here, through a compound screen, we found that two bis-biguanide compounds, Chlorhexidine and Alexidine, modified the activity of the inner mitochondrial membrane (IMM)-resident protease OMA1 by altering the integrity of the IMM.	Chlorhexidine	76-89	OMA1 zinc metallopeptidase	Homo sapiens	187-191
34495738-5	2021	Here, through a compound screen, we found that two bis-biguanide compounds, Chlorhexidine and Alexidine, modified the activity of the inner mitochondrial membrane (IMM)-resident protease OMA1 by altering the integrity of the IMM.	alexidine	94-103	OMA1 zinc metallopeptidase	Homo sapiens	187-191
35290799-12	2022	ADA inhibition increases the proteolytic processing of an Oma1 substrate, the dynamin GTPase Opa1.	N-(2-acetamido)iminodiacetic acid	0-3	OMA1 zinc metallopeptidase	Homo sapiens	58-62
33130089-3	2021	OMA1 is dormant under physiological conditions but rapidly activated upon mitochondrial stress, such as loss of membrane potential or excessive reactive oxygen species.	Oxygen	153-159	OMA1 zinc metallopeptidase	Homo sapiens	0-4
33383158-5	2021	However, when H9c2s are differentiated to a more cardiac-like phenotype via treatment with retinoic acid (RA) in low serum media, loss of Delta psim induces robust, and reversible, cleavage of L-OPA1 and subsequent OMA1 degradation.	h9c2s	14-19	OMA1 zinc metallopeptidase	Homo sapiens	215-219
33383158-5	2021	However, when H9c2s are differentiated to a more cardiac-like phenotype via treatment with retinoic acid (RA) in low serum media, loss of Delta psim induces robust, and reversible, cleavage of L-OPA1 and subsequent OMA1 degradation.	Tretinoin	91-104	OMA1 zinc metallopeptidase	Homo sapiens	215-219
33383158-5	2021	However, when H9c2s are differentiated to a more cardiac-like phenotype via treatment with retinoic acid (RA) in low serum media, loss of Delta psim induces robust, and reversible, cleavage of L-OPA1 and subsequent OMA1 degradation.	Tretinoin	106-108	OMA1 zinc metallopeptidase	Homo sapiens	215-219
33562813-13	2021	The present study also demonstrates that the proteolytic cleavage of Opa1 is affected, and that the level of OMA1 is significantly reduced in shPA200 cells upon oligomycin-induced mitochondrial insult.	Oligomycins	161-171	OMA1 zinc metallopeptidase	Homo sapiens	109-113
29961397-7	2018	Consistent with this, cells lacking OMA1, a key protease responsible for cleavage of OPA1, are protected against OPA1 cleavage and mitochondrial fragmentation in response to H2O2 challenge.	Hydrogen Peroxide	174-178	OMA1 zinc metallopeptidase	Homo sapiens	36-40
31729644-2	2020	Reactive oxygen species modulator 1 (ROMO1) and the overlapping with the M-AAA protease 1 homolog (OMA1) proteins are the most important mitochondrial membrane proteins, which are involved in modulating reactive oxygen species (ROS) production and the regulation of mitochondrial structure dynamics.	Oxygen	9-15	OMA1 zinc metallopeptidase	Homo sapiens	99-103
31729644-2	2020	Reactive oxygen species modulator 1 (ROMO1) and the overlapping with the M-AAA protease 1 homolog (OMA1) proteins are the most important mitochondrial membrane proteins, which are involved in modulating reactive oxygen species (ROS) production and the regulation of mitochondrial structure dynamics.	Oxygen	212-218	OMA1 zinc metallopeptidase	Homo sapiens	99-103
31044600-6	2019	These residues form a disulfide bond, which likely plays a structural role and influences conformational stability and activity of the Oma1 high-mass complex.	Disulfides	22-31	OMA1 zinc metallopeptidase	Homo sapiens	135-139
31044600-9	2019	Conclusion: Disulfide bonds formed by IMS-exposed residues Cys272 and Cys332 play an important evolutionarily conserved role in the regulation of Oma1 function.	Disulfides	12-21	OMA1 zinc metallopeptidase	Homo sapiens	146-150
31044600-9	2019	Conclusion: Disulfide bonds formed by IMS-exposed residues Cys272 and Cys332 play an important evolutionarily conserved role in the regulation of Oma1 function.	ims	38-41	OMA1 zinc metallopeptidase	Homo sapiens	146-150
31044600-10	2019	We propose that the redox status of these cysteines may act as a redox-tunable switch to optimize Oma1 proteolytic function for specific cellular conditions or homeostatic challenges.	Cysteine	42-51	OMA1 zinc metallopeptidase	Homo sapiens	98-102
31130024-7	2019	Meanwhile, we found hyperoside inhibited IR-induced mitochondrial fission by suppressing OMA1 mediated proteolysis of optic atrophy 1 (OPA1).	hyperoside	20-30	OMA1 zinc metallopeptidase	Homo sapiens	89-93
31130024-8	2019	Consistently, in human proximal tubular epithelial cells, hyperoside might inhibit CoCl2-induced mitochondrial fission, oxidative stress, and apoptosis by regulating OMA1-OPA1 axis.	hyperoside	58-68	OMA1 zinc metallopeptidase	Homo sapiens	166-170
31130024-8	2019	Consistently, in human proximal tubular epithelial cells, hyperoside might inhibit CoCl2-induced mitochondrial fission, oxidative stress, and apoptosis by regulating OMA1-OPA1 axis.	cobaltous chloride	83-88	OMA1 zinc metallopeptidase	Homo sapiens	166-170
27786282-3	2016	BAK conformational changes associated with MOMP activate the OMA1 protease to cleave OPA1 resulting in remodeling of the cristae and release of the highly concentrated protons within the cristae invaginations.	bakuchiol	0-3	OMA1 zinc metallopeptidase	Homo sapiens	61-65
29748581-10	2018	Pretreatment of cells with an inhibitor of the proteasome (MG132), prevented leptin-induced OMA1 degradation, implicating the ubiquitination/proteasome system as a part of the protective leptin pathway.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	59-64	OMA1 zinc metallopeptidase	Homo sapiens	92-96
29748581-11	2018	In addition, GSK3 inhibitor (SB216763) was also involved in the degradation of OMA1.	SB 216763	29-37	OMA1 zinc metallopeptidase	Homo sapiens	79-83
30069011-6	2018	OPA1 cleavage and cell death were inhibited by ROS scavengers and by siRNA-mediated knockdown of the mitochondrial protease OMA1, indicating the engagement of a ROS-OMA1-OPA1 axis in T-ALL cells.	Reactive Oxygen Species	47-50	OMA1 zinc metallopeptidase	Homo sapiens	165-169
30069011-6	2018	OPA1 cleavage and cell death were inhibited by ROS scavengers and by siRNA-mediated knockdown of the mitochondrial protease OMA1, indicating the engagement of a ROS-OMA1-OPA1 axis in T-ALL cells.	Reactive Oxygen Species	161-164	OMA1 zinc metallopeptidase	Homo sapiens	124-128
30069011-6	2018	OPA1 cleavage and cell death were inhibited by ROS scavengers and by siRNA-mediated knockdown of the mitochondrial protease OMA1, indicating the engagement of a ROS-OMA1-OPA1 axis in T-ALL cells.	Reactive Oxygen Species	161-164	OMA1 zinc metallopeptidase	Homo sapiens	165-169
26923599-4	2016	Alternatively, insults that depolarize mitochondria and deplete cellular ATP stabilize active OMA1 and promote YME1L degradation.	Adenosine Triphosphate	73-76	OMA1 zinc metallopeptidase	Homo sapiens	94-98
25275009-0	2014	Activation of mitochondrial protease OMA1 by Bax and Bak promotes cytochrome c release during apoptosis.	bakuchiol	53-56	OMA1 zinc metallopeptidase	Homo sapiens	37-41
25275009-6	2014	The mitochondrial metalloprotease OMA1 was activated in this system in a Bax- and Bak-dependent fashion.	bakuchiol	82-85	OMA1 zinc metallopeptidase	Homo sapiens	34-38
25275009-9	2014	Thus it is clear that oligomerized Bax and Bak trigger apoptosis by causing both the permeabilization of the mitochondrial outer membrane and activation OMA1.	bakuchiol	43-46	OMA1 zinc metallopeptidase	Homo sapiens	153-157
25112877-0	2014	p53 is required for cisplatin-induced processing of the mitochondrial fusion protein L-Opa1 that is mediated by the mitochondrial metallopeptidase Oma1 in gynecologic cancers.	Cisplatin	20-29	OMA1 zinc metallopeptidase	Homo sapiens	147-151
25112877-5	2014	The requirements of Oma1 and p53 for CDDP-induced L-Opa1 processing, mitochondrial fragmentation, and apoptosis were examined by siRNA or cDNA.	Cisplatin	37-41	OMA1 zinc metallopeptidase	Homo sapiens	20-24
25112877-7	2014	CDDP induced Oma1 40-kDa form increases in OV2008 cells, not in C13* cells.	Cisplatin	0-4	OMA1 zinc metallopeptidase	Homo sapiens	13-17
25112877-9	2014	Silencing p53 expression attenuated the effects of CDDP in Oma1 (40 kDa) increase, L-Opa1 processing, mitochondrial fragmentation, and apoptosis in chemosensitive OVCA cells, whereas reconstitution of p53 in p53 mutant or null chemoresistant OVCA cells induced Oma1 (40 kDa) increase, L-Opa1 processing, mitochondrial fragmentation, and apoptosis irrespective of the presence of CDDP.	Cisplatin	51-55	OMA1 zinc metallopeptidase	Homo sapiens	59-63
25112877-9	2014	Silencing p53 expression attenuated the effects of CDDP in Oma1 (40 kDa) increase, L-Opa1 processing, mitochondrial fragmentation, and apoptosis in chemosensitive OVCA cells, whereas reconstitution of p53 in p53 mutant or null chemoresistant OVCA cells induced Oma1 (40 kDa) increase, L-Opa1 processing, mitochondrial fragmentation, and apoptosis irrespective of the presence of CDDP.	Cisplatin	51-55	OMA1 zinc metallopeptidase	Homo sapiens	261-265
27325672-5	2016	Pharmacological or genetic prevention of ROS accumulation in Oma1-deficient cells restores this defective TOR signaling.	Reactive Oxygen Species	41-44	OMA1 zinc metallopeptidase	Homo sapiens	61-65
25510854-8	2015	However, KACL mutants with non-conservative amino acid substitutions of arginine 158 or isoleucine 161 abrogated binding of both KACL-specific mAb OMA1 and sNKp65, well in line with the blockade of NKp65-KACL interaction by OMA1.	Arginine	72-80	OMA1 zinc metallopeptidase	Homo sapiens	147-151
25510854-8	2015	However, KACL mutants with non-conservative amino acid substitutions of arginine 158 or isoleucine 161 abrogated binding of both KACL-specific mAb OMA1 and sNKp65, well in line with the blockade of NKp65-KACL interaction by OMA1.	Isoleucine	88-98	OMA1 zinc metallopeptidase	Homo sapiens	147-151
25433032-3	2015	This degradation requires reductions in cellular ATP and involves the activity of the ATP-independent protease OMA1.	Adenosine Triphosphate	49-52	OMA1 zinc metallopeptidase	Homo sapiens	111-115