DROME:Q0KHV6

Species (Taxon ID)	Drosophila melanogaster (Fruit fly). (7227)
Gene Name(s)	No Information Provided. (synonyms: Pink1-RE (ECO:0000313 with EMBL:AFA28429.1))
Protein Name(s)	FI19430p1 (ECO:0000313 with EMBL:AFA28429.1) PTEN-induced putative kinase 1, isoform A (ECO:0000313 with EMBL:AAN09178.1) PTEN-induced putative kinase 1, isoform B (ECO:0000313 with EMBL:AAF46188.1) PTEN-induced putative kinase 1, isoform C (ECO:0000313 with EMBL:AAZ52497.1) PTEN-induced putative kinase 1, isoform D (ECO:0000313 with EMBL:AAZ52498.1) PTEN-induced putative kinase 1, isoform E (ECO:0000313 with EMBL:AAZ52499.1) PTEN-induced putative kinase 1, isoform F (ECO:0000313 with EMBL:AAZ52500.1) PTEN-induced putative kinase 1, isoform G (ECO:0000313 with EMBL:AAZ52501.1) PTEN-induced putative kinase 1, isoform H (ECO:0000313 with EMBL:AAZ52502.1) PTEN-induced putative kinase 1, isoform I (ECO:0000313 with EMBL:AHN59423.1)
External Links
UniProt	Q0KHV6
EMBL	AE014298 AE014298 AE014298 AE014298 AE014298 AE014298 AE014298 AE014298 BT133188 AE014298
RefSeq	NP_001027049.1 NP_001027050.1 NP_001027051.1 NP_001027052.1 NP_001027053.1 NP_001027054.1 NP_572340.2 NP_727110.1
UniGene	Dm.56
SMR	Q0KHV6
IntAct	Q0KHV6
STRING	7227.FBpp0099833
EnsemblMetazoa	FBtr0070956 FBtr0070957 FBtr0100413 FBtr0100414 FBtr0100415 FBtr0100416 FBtr0100419 FBtr0100420
GeneID	31607
KEGG	dme:Dmel_CG4523
UCSC	CG4523-RA
CTD	65018
FlyBase	FBgn0029891
GeneTree	ENSGT00390000001206
OMA	LKMMFNY
OrthoDB	EOG7TBC1R
GenomeRNAi	31607
NextBio	774437
PRO	PR:Q0KHV6
Proteomes	UP000000803
GO	GO:0005737 GO:0005739 GO:0016006 GO:0005524 GO:0004672 GO:0004674 GO:0048749 GO:0035234 GO:0000266 GO:0000422 GO:0007005 GO:0010637 GO:0043524 GO:0043069 GO:0007274 GO:0048078 GO:0090141 GO:0042787 GO:0010821 GO:0006979 GO:0030382
InterPro	IPR011009 IPR000719 IPR008271
Pfam	PF00069
SUPFAM	SSF56112
PROSITE	PS50011 PS00108

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0047497	mitochondrion transport along microtubule	PMID:22396657^[1]	ECO:0000315			P	Figure 3	complete CACAO 3953
	GO:0048312	intracellular distribution of mitochondria	PMID:22396657^[1]	ECO:0000315			P	Figure 4	complete CACAO 3954
involved_in	GO:0007614	short-term memory	PMID:28435104^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0072375	medium-term memory	PMID:28435104^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:1904457	positive regulation of neuronal action potential	PMID:28435104^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:1904061	positive regulation of locomotor rhythm	PMID:28435104^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0048312	intracellular distribution of mitochondria	PMID:22396657^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0047497	mitochondrion transport along microtubule	PMID:22396657^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0048078	positive regulation of compound eye pigmentation	PMID:19692353^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0090141	positive regulation of mitochondrial fission	PMID:21873635^[4]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0029891 PANTHER:PTN001121970 RGD:1305769	P	Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:21873635^[4]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0029891 MGI:MGI:1916193 PANTHER:PTN000540563 UniProtKB:Q9BXM7	P	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:21873635^[4]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0029891 PANTHER:PTN001121970 UniProtKB:Q9BXM7 WB:WBGene00017137 ZFIN:ZDB-GENE-041212-53	C	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:21873635^[4]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0029891 MGI:MGI:1916193 PANTHER:PTN001121970 RGD:1305769 UniProtKB:D6WMX4 UniProtKB:Q9BXM7	F	Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	PMID:21873635^[4]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0029891 PANTHER:PTN000540563 UniProtKB:Q9BXM7	F	Seeded From UniProt	complete
involved_in	GO:0000422	autophagy of mitochondrion	PMID:21873635^[4]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0029891 PANTHER:PTN001121970 UniProtKB:Q9BXM7 WB:WBGene00017137	P	Seeded From UniProt	complete
involved_in	GO:0007005	mitochondrion organization	PMID:29456190^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:29456190^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0043008	ATP-dependent protein binding	PMID:29456190^[5]	ECO:0000353	physical interaction evidence used in manual assertion	FB:FBgn0019960	F	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:29456190^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:29456190^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:1902956	regulation of mitochondrial electron transport, NADH to ubiquinone	PMID:25412178^[6]	ECO:0000316	genetic interaction evidence used in manual assertion	FB:FBgn0019957	P	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:24901221^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:24901221^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007005	mitochondrion organization	PMID:24901221^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:1902956	regulation of mitochondrial electron transport, NADH to ubiquinone	PMID:24652937^[8]	ECO:0000316	genetic interaction evidence used in manual assertion	FB:FBgn0019957	P	Seeded From UniProt	complete
involved_in	GO:0035234	ectopic germ cell programmed cell death	PMID:23523076^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	PMID:22645651^[10]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0051654	establishment of mitochondrion localization	PMID:22396657^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0000422	autophagy of mitochondrion	PMID:20194754^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006511	ubiquitin-dependent protein catabolic process	PMID:20194754^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0010637	negative regulation of mitochondrial fusion	PMID:20194754^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0090141	positive regulation of mitochondrial fission	PMID:20194754^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007274	neuromuscular synaptic transmission	PMID:20049710^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0010821	regulation of mitochondrion organization	PMID:19546216^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:19048081^[14]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:19048081^[14]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0007005	mitochondrion organization	PMID:18799731^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0030382	sperm mitochondrion organization	PMID:18799731^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0000266	mitochondrial fission	PMID:18443288^[16]	ECO:0000316	genetic interaction evidence used in manual assertion	FB:FBgn0261276	P	Seeded From UniProt	complete
involved_in	GO:0007005	mitochondrion organization	PMID:18443288^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0000266	mitochondrial fission	PMID:18443288^[16]	ECO:0000316	genetic interaction evidence used in manual assertion	FB:FBgn0026479	P	Seeded From UniProt	complete
involved_in	GO:0007005	mitochondrion organization	PMID:18230723^[17]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0000266	mitochondrial fission	PMID:18230723^[17]	ECO:0000316	genetic interaction evidence used in manual assertion	FB:FBgn0261276	P	Seeded From UniProt	complete
involved_in	GO:0000266	mitochondrial fission	PMID:18230723^[17]	ECO:0000316	genetic interaction evidence used in manual assertion	FB:FBgn0026479	P	Seeded From UniProt	complete
involved_in	GO:0000266	mitochondrial fission	PMID:18230723^[17]	ECO:0000316	genetic interaction evidence used in manual assertion	FB:FBgn0029870	P	Seeded From UniProt	complete
involved_in	GO:0030382	sperm mitochondrion organization	PMID:16672980^[18]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007005	mitochondrion organization	PMID:16672980^[18]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007005	mitochondrion organization	PMID:16672980^[18]	ECO:0000316	genetic interaction evidence used in manual assertion	FB:FBgn0040491	P	Seeded From UniProt	complete
involved_in	GO:0030382	sperm mitochondrion organization	PMID:16672981^[19]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007005	mitochondrion organization	PMID:16672981^[19]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0016006	Nebenkern	PMID:16672981^[19]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0048749	compound eye development	PMID:16938835^[20]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006979	response to oxidative stress	PMID:16938835^[20]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0043069	negative regulation of programmed cell death	PMID:16938835^[20]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007005	mitochondrion organization	PMID:16818890^[21]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0043524	negative regulation of neuron apoptotic process	PMID:16818890^[21]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0000422	autophagy of mitochondrion	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR040110	P	Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR008271	F	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR040110	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719	F	Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR008271	P	Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000038	ECO:0000323	imported automatically asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F	Seeded From UniProt	complete
involved_in	GO:0016310	phosphorylation	GO_REF:0000038	ECO:0000323	imported automatically asserted information used in automatic assertion	UniProtKB-KW:KW-0418	P	Seeded From UniProt	complete
enables	GO:0016301	kinase activity	GO_REF:0000038	ECO:0000323	imported automatically asserted information used in automatic assertion	UniProtKB-KW:KW-0418	F	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 Liu, S et al. (2012) Parkinson's disease-associated kinase PINK1 regulates Miro protein level and axonal transport of mitochondria. PLoS Genet. 8 e1002537 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 Julienne, H et al. (2017) Drosophila PINK1 and parkin loss-of-function mutants display a range of non-motor Parkinson's disease phenotypes. Neurobiol. Dis. 104 15-23 PubMed GONUTS page
↑ Venderova, K et al. (2009) Leucine-Rich Repeat Kinase 2 interacts with Parkin, DJ-1 and PINK-1 in a Drosophila melanogaster model of Parkinson's disease. Hum. Mol. Genet. 18 4390-404 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 ^5.4 Tsai, PI et al. (2018) PINK1 Phosphorylates MIC60/Mitofilin to Control Structural Plasticity of Mitochondrial Crista Junctions. Mol. Cell 69 744-756.e6 PubMed GONUTS page
↑ Pogson, JH et al. (2014) The complex I subunit NDUFA10 selectively rescues Drosophila pink1 mutants through a mechanism independent of mitophagy. PLoS Genet. 10 e1004815 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 Shiba-Fukushima, K et al. (2014) PINK1-mediated phosphorylation of Parkin boosts Parkin activity in Drosophila. PLoS Genet. 10 e1004391 PubMed GONUTS page
↑ Morais, VA et al. (2014) PINK1 loss-of-function mutations affect mitochondrial complex I activity via NdufA10 ubiquinone uncoupling. Science 344 203-7 PubMed GONUTS page
↑ Yacobi-Sharon, K et al. (2013) Alternative germ cell death pathway in Drosophila involves HtrA2/Omi, lysosomes, and a caspase-9 counterpart. Dev. Cell 25 29-42 PubMed GONUTS page
↑ Woodroof, HI et al. (2011) Discovery of catalytically active orthologues of the Parkinson's disease kinase PINK1: analysis of substrate specificity and impact of mutations. Open Biol 1 110012 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 ^11.3 Ziviani, E et al. (2010) Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin. Proc. Natl. Acad. Sci. U.S.A. 107 5018-23 PubMed GONUTS page
↑ Morais, VA et al. (2009) Parkinson's disease mutations in PINK1 result in decreased Complex I activity and deficient synaptic function. EMBO Mol Med 1 99-111 PubMed GONUTS page
↑ Lutz, AK et al. (2009) Loss of parkin or PINK1 function increases Drp1-dependent mitochondrial fragmentation. J. Biol. Chem. 284 22938-51 PubMed GONUTS page
↑ ^14.0 ^14.1 Whitworth, AJ et al. () Rhomboid-7 and HtrA2/Omi act in a common pathway with the Parkinson's disease factors Pink1 and Parkin. Dis Model Mech 1 168-74; discussion 173 PubMed GONUTS page
↑ ^15.0 ^15.1 Deng, H et al. (2008) The Parkinson's disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila. Proc. Natl. Acad. Sci. U.S.A. 105 14503-8 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 Yang, Y et al. (2008) Pink1 regulates mitochondrial dynamics through interaction with the fission/fusion machinery. Proc. Natl. Acad. Sci. U.S.A. 105 7070-5 PubMed GONUTS page
↑ ^17.0 ^17.1 ^17.2 ^17.3 Poole, AC et al. (2008) The PINK1/Parkin pathway regulates mitochondrial morphology. Proc. Natl. Acad. Sci. U.S.A. 105 1638-43 PubMed GONUTS page
↑ ^18.0 ^18.1 ^18.2 Park, J et al. (2006) Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin. Nature 441 1157-61 PubMed GONUTS page
↑ ^19.0 ^19.1 ^19.2 Clark, IE et al. (2006) Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin. Nature 441 1162-6 PubMed GONUTS page
↑ ^20.0 ^20.1 ^20.2 Wang, D et al. (2006) Antioxidants protect PINK1-dependent dopaminergic neurons in Drosophila. Proc. Natl. Acad. Sci. U.S.A. 103 13520-5 PubMed GONUTS page
↑ ^21.0 ^21.1 Yang, Y et al. (2006) Mitochondrial pathology and muscle and dopaminergic neuron degeneration caused by inactivation of Drosophila Pink1 is rescued by Parkin. Proc. Natl. Acad. Sci. U.S.A. 103 10793-8 PubMed GONUTS page

[PMID:22396657-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 Liu, S et al. (2012) Parkinson's disease-associated kinase PINK1 regulates Miro protein level and axonal transport of mitochondria. PLoS Genet. 8 e1002537 PubMed GONUTS page

[PMID:28435104-2] 2.0 ^2.1 ^2.2 ^2.3 Julienne, H et al. (2017) Drosophila PINK1 and parkin loss-of-function mutants display a range of non-motor Parkinson's disease phenotypes. Neurobiol. Dis. 104 15-23 PubMed GONUTS page

[PMID:19692353-3] Venderova, K et al. (2009) Leucine-Rich Repeat Kinase 2 interacts with Parkin, DJ-1 and PINK-1 in a Drosophila melanogaster model of Parkinson's disease. Hum. Mol. Genet. 18 4390-404 PubMed GONUTS page

[PMID:21873635-4] 4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:29456190-5] 5.0 ^5.1 ^5.2 ^5.3 ^5.4 Tsai, PI et al. (2018) PINK1 Phosphorylates MIC60/Mitofilin to Control Structural Plasticity of Mitochondrial Crista Junctions. Mol. Cell 69 744-756.e6 PubMed GONUTS page

[PMID:25412178-6] Pogson, JH et al. (2014) The complex I subunit NDUFA10 selectively rescues Drosophila pink1 mutants through a mechanism independent of mitophagy. PLoS Genet. 10 e1004815 PubMed GONUTS page

[PMID:24901221-7] 7.0 ^7.1 ^7.2 Shiba-Fukushima, K et al. (2014) PINK1-mediated phosphorylation of Parkin boosts Parkin activity in Drosophila. PLoS Genet. 10 e1004391 PubMed GONUTS page

[PMID:24652937-8] Morais, VA et al. (2014) PINK1 loss-of-function mutations affect mitochondrial complex I activity via NdufA10 ubiquinone uncoupling. Science 344 203-7 PubMed GONUTS page

[PMID:23523076-9] Yacobi-Sharon, K et al. (2013) Alternative germ cell death pathway in Drosophila involves HtrA2/Omi, lysosomes, and a caspase-9 counterpart. Dev. Cell 25 29-42 PubMed GONUTS page

[PMID:22645651-10] Woodroof, HI et al. (2011) Discovery of catalytically active orthologues of the Parkinson's disease kinase PINK1: analysis of substrate specificity and impact of mutations. Open Biol 1 110012 PubMed GONUTS page

[PMID:20194754-11] 11.0 ^11.1 ^11.2 ^11.3 Ziviani, E et al. (2010) Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin. Proc. Natl. Acad. Sci. U.S.A. 107 5018-23 PubMed GONUTS page

[PMID:20049710-12] Morais, VA et al. (2009) Parkinson's disease mutations in PINK1 result in decreased Complex I activity and deficient synaptic function. EMBO Mol Med 1 99-111 PubMed GONUTS page

[PMID:19546216-13] Lutz, AK et al. (2009) Loss of parkin or PINK1 function increases Drp1-dependent mitochondrial fragmentation. J. Biol. Chem. 284 22938-51 PubMed GONUTS page

[PMID:19048081-14] 14.0 ^14.1 Whitworth, AJ et al. () Rhomboid-7 and HtrA2/Omi act in a common pathway with the Parkinson's disease factors Pink1 and Parkin. Dis Model Mech 1 168-74; discussion 173 PubMed GONUTS page

[PMID:18799731-15] 15.0 ^15.1 Deng, H et al. (2008) The Parkinson's disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila. Proc. Natl. Acad. Sci. U.S.A. 105 14503-8 PubMed GONUTS page

[PMID:18443288-16] 16.0 ^16.1 ^16.2 Yang, Y et al. (2008) Pink1 regulates mitochondrial dynamics through interaction with the fission/fusion machinery. Proc. Natl. Acad. Sci. U.S.A. 105 7070-5 PubMed GONUTS page

[PMID:18230723-17] 17.0 ^17.1 ^17.2 ^17.3 Poole, AC et al. (2008) The PINK1/Parkin pathway regulates mitochondrial morphology. Proc. Natl. Acad. Sci. U.S.A. 105 1638-43 PubMed GONUTS page

[PMID:16672980-18] 18.0 ^18.1 ^18.2 Park, J et al. (2006) Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin. Nature 441 1157-61 PubMed GONUTS page

[PMID:16672981-19] 19.0 ^19.1 ^19.2 Clark, IE et al. (2006) Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin. Nature 441 1162-6 PubMed GONUTS page

[PMID:16938835-20] 20.0 ^20.1 ^20.2 Wang, D et al. (2006) Antioxidants protect PINK1-dependent dopaminergic neurons in Drosophila. Proc. Natl. Acad. Sci. U.S.A. 103 13520-5 PubMed GONUTS page

[PMID:16818890-21] 21.0 ^21.1 Yang, Y et al. (2006) Mitochondrial pathology and muscle and dopaminergic neuron degeneration caused by inactivation of Drosophila Pink1 is rescued by Parkin. Proc. Natl. Acad. Sci. U.S.A. 103 10793-8 PubMed GONUTS page

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DROME:Q0KHV6

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References

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