PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
2453298-4	1987	The mutation, mna1-1, is especially interesting since it causes a loss of both mitochondrial DNA and RNA when the mutant is grown on a fermentable carbon source at the restrictive temperature.	Carbon	147-153	dynamin-related GTPase MGM1	Saccharomyces cerevisiae S288C	14-20
32041880-2	2020	Here, we determined the crystal structure of Saccharomyces cerevisiae short Mgm1 (s-Mgm1) in complex with GDP.	Guanosine Diphosphate	106-109	dynamin-related GTPase MGM1	Saccharomyces cerevisiae S288C	76-80
32041880-2	2020	Here, we determined the crystal structure of Saccharomyces cerevisiae short Mgm1 (s-Mgm1) in complex with GDP.	Guanosine Diphosphate	106-109	dynamin-related GTPase MGM1	Saccharomyces cerevisiae S288C	84-88
11038180-2	2000	Here, we show that mitochondrial fragmentation and mitochondrial genome loss caused by lesions in MGM1 are suppressed by three novel mutations, gag1, gag2, and gag3 (for glycerol-adapted growth).	Glycerol	170-178	dynamin-related GTPase MGM1	Saccharomyces cerevisiae S288C	98-102
23045528-2	2012	RESULTS: Decreasing phosphatidylethanolamine reduces the rate of lipid mixing and the biogenesis of Mgm1, a mitochondrial fusion protein.	phosphatidylethanolamine	20-44	dynamin-related GTPase MGM1	Saccharomyces cerevisiae S288C	100-104
19236101-0	2009	The dynamin-related protein Mgm1p assembles into oligomers and hydrolyzes GTP to function in mitochondrial membrane fusion.	Guanosine Triphosphate	74-77	dynamin-related GTPase MGM1	Saccharomyces cerevisiae S288C	28-33
19236101-3	2009	Previous studies suggest that Mgm1p mediates mitochondrial inner membrane fusion in a manner similar to that of other dynamin proteins that use GTP hydrolysis and oligomerization to induce structural changes in lipid bilayers; however, a direct demonstration of these activities has yet to be presented.	Guanosine Triphosphate	144-147	dynamin-related GTPase MGM1	Saccharomyces cerevisiae S288C	30-35
19236101-7	2009	A mutation in the GTPase effector domain, involved in assembly and assembly-stimulated GTP hydrolysis, has basal GTPase activity similar to that of wild-type Mgm1p but has a weaker propensity to form oligomers.	Guanosine Triphosphate	18-21	dynamin-related GTPase MGM1	Saccharomyces cerevisiae S288C	158-163
19236101-8	2009	Finally, our data indicate that Mgm1p interacts specifically with negatively charged phospholipids found in mitochondrial membranes, and point mutations in the predicted lipid-binding domain abrogate these interactions.	Phospholipids	85-98	dynamin-related GTPase MGM1	Saccharomyces cerevisiae S288C	32-37
19236101-10	2009	Together, these data indicate that Mgm1p mediates fusion through oligomerization, GTP hydrolysis, and lipid binding in a manner similar to those of other dynamin mechanoenzymes.	Guanosine Triphosphate	82-85	dynamin-related GTPase MGM1	Saccharomyces cerevisiae S288C	35-40
14644195-8	2003	Loss of function of OPA-1, analogous to deficiency of its yeast homologue, Mgm1p, is expected to lead to mitochondrial fission, loss of mitochondrial DNA, respiratory deficits and an increase in reactive oxygen species.	Oxygen	204-210	dynamin-related GTPase MGM1	Saccharomyces cerevisiae S288C	75-80
15096522-0	2004	Alternative topogenesis of Mgm1 and mitochondrial morphology depend on ATP and a functional import motor.	Adenosine Triphosphate	71-74	dynamin-related GTPase MGM1	Saccharomyces cerevisiae S288C	27-31
15096522-6	2004	Formation of the short isoform of Mgm1 and mitochondrial morphology further depend on a functional protein import motor and on the ATP level in the matrix.	Adenosine Triphosphate	131-134	dynamin-related GTPase MGM1	Saccharomyces cerevisiae S288C	34-38
7916673-4	1993	Loss of MGM1 resulted in slow growth on rich medium, failure to grow on non-fermentable carbon sources, and loss of mitochondrial DNA.	Carbon	88-94	dynamin-related GTPase MGM1	Saccharomyces cerevisiae S288C	8-12
10037792-5	1999	A version of mgm1 mutated in a conserved residue in the putative GTP-binding site was unable to complement any of the mutant defects.	Guanosine Triphosphate	65-68	dynamin-related GTPase MGM1	Saccharomyces cerevisiae S288C	13-17
8575026-0	1995	New alleles of mgm1: a gene encoding a protein with a GTP-binding domain related to dynamin.	Guanosine Triphosphate	54-57	dynamin-related GTPase MGM1	Saccharomyces cerevisiae S288C	15-19
7507812-11	1993	They contain the typical GTP-binding motif and show significant homology to other members of a new family of GTPases that includes rat dynamin, Drosophila Shibire and the yeast proteins Vps1/Spo15 and Mgm1.	Guanosine Triphosphate	25-28	dynamin-related GTPase MGM1	Saccharomyces cerevisiae S288C	201-205
1532158-5	1992	The MGM1 protein has a 200-amino-acid region that is highly related to a family of GTP-binding proteins of apparently diverse function that includes the microtubule-binding protein, dynamin D100.	Guanosine Triphosphate	83-86	dynamin-related GTPase MGM1	Saccharomyces cerevisiae S288C	4-8