PARK7

PARK7
Dostupne strukture
PDB	Pretraga ortologa: PDBe RCSB
Spisak PDB ID kodova
	1J42, 1P5F, 1PDV, 1PDW, 1PE0, 1Q2U, 1SOA, 1UCF, 2OR3, 2R1T, 2R1U, 2R1V, 2RK3, 2RK4, 2RK6, 3B36, 3B38, 3B3A, 3BWE, 3CY6, 3CYF, 3CZ9, 3CZA, 3EZG, 3F71, 3SF8, 4BTE, 4MNT, 4MTC, 4N0M, 4N12, 4OGF, 4OQ4, 4P2G, 4P34, 4P35, 4P36, 4ZGG, 4RKW, 4RKY, 4S0Z
Identifikatori
Aliasi	PARK7
Vanjski ID-jevi	OMIM: 602533 MGI: 2135637 HomoloGene: 38295 GeneCards: PARK7
Lokacija gena (čovjek)
Hrom.	Hromosom 1 (čovjek)
Kraj	7,985,505 bp
Lokacija gena (miš)
Hrom.	Hromosom 4 (miš)
Kraj	150,998,894 bp
Obrazac RNK ekspresije
	Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija	• signaling receptor binding; • GO:0019974 cytokine binding; • cupric ion binding; • transcription factor binding; • L-dopa decarboxylase activator activity; • GO:0070122 peptidase activity; • kinase binding; • tyrosine 3-monooxygenase activator activity; • vezivanje enzima; • mRNA binding; • protein homodimerization activity; • scaffold protein binding; • small protein activating enzyme binding; • single-stranded DNA binding; • ubiquitin-like protein conjugating enzyme binding; • GO:0001948, GO:0016582 vezivanje za proteine; • peroxiredoxin activity; • double-stranded DNA binding; • copper ion binding; • mercury ion binding; • GO:0001105 transcription coactivator activity; • oxidoreductase activity, acting on peroxide as acceptor; • androgen receptor binding; • superoxide dismutase copper chaperone activity; • vezivanje sa RNK; • vezivanje identičnih proteina; • ubiquitin-specific protease binding; • hydrolase activity; • cuprous ion binding; • cadherin binding; • protein deglycase activity; • GO:0032403 protein-containing complex binding;
Ćelijska komponenta	• citoplazma; • citosol; • membrana; • mitochondrial intermembrane space; • mitohondrija; • neuron projection; • jedro; • mitochondrial respiratory chain complex I; • Endoplazmatski retikulum; • Lipidni splav; • Hromatin; • Egzosom; • ćelijska membrana; • mitochondrial matrix; • cell body; • PML body; • presynapse; • perinuklearno područje citoplazme; • Akson; • nukleoplazma;
Biološki proces	• GO:1904089 negative regulation of neuron apoptotic process; • positive regulation of transcription regulatory region DNA binding; • negative regulation of protein sumoylation; • negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; • negative regulation of protein binding; • synaptic transmission, dopaminergic; • positive regulation of interleukin-8 production; • negative regulation of proteasomal ubiquitin-dependent protein catabolic process; • Ras protein signal transduction; • cellular response to glyoxal; • negative regulation of protein acetylation; • positive regulation of reactive oxygen species biosynthetic process; • positive regulation of oxidative phosphorylation uncoupler activity; • positive regulation of protein kinase B signaling; • GO:1903363 negative regulation of protein catabolic process; • adult locomotory behavior; • regulation of neuron apoptotic process; • negative regulation of extrinsic apoptotic signaling pathway; • negative regulation of cell death; • glycolate biosynthetic process; • positive regulation of protein homodimerization activity; • negative regulation of gene expression; • single fertilization; • positive regulation of peptidyl-serine phosphorylation; • positive regulation of mitochondrial electron transport, NADH to ubiquinone; • negative regulation of hydrogen peroxide-induced neuron intrinsic apoptotic signaling pathway; • negative regulation of oxidative stress-induced cell death; • inflammatory response; • negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; • regulation of supramolecular fiber organization; • negative regulation of neuron death; • GO:0033128 negative regulation of protein phosphorylation; • negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; • negative regulation of protein kinase activity; • negative regulation of oxidative stress-induced neuron death; • membrane depolarization; • protein stabilization; • mitochondrion organization; • positive regulation of DNA-binding transcription factor activity; • negative regulation of death-inducing signaling complex assembly; • negative regulation of apoptotic process; • Proteoliza; • negative regulation of protein K48-linked deubiquitination; • dopamine uptake involved in synaptic transmission; • positive regulation of tyrosine 3-monooxygenase activity; • positive regulation of L-dopa decarboxylase activity; • negative regulation of hydrogen peroxide-induced neuron death; • regulation of inflammatory response; • regulation of androgen receptor signaling pathway; • negative regulation of hydrogen peroxide-induced cell death; • positive regulation of autophagy of mitochondrion; • response to hydrogen peroxide; • detoxification of copper ion; • positive regulation of superoxide dismutase activity; • positive regulation of dopamine biosynthetic process; • positive regulation of protein localization to nucleus; • positive regulation of L-dopa biosynthetic process; • activation of protein kinase B activity; • membrane hyperpolarization; • detoxification of mercury ion; • negative regulation of TRAIL-activated apoptotic signaling pathway; • cellular oxidant detoxification; • negative regulation of ubiquitin-specific protease activity; • Autofagija; • GO:0072353 cellular response to reactive oxygen species; • regulation of mitochondrial membrane potential; • negative regulation of protein ubiquitination; • hydrogen peroxide metabolic process; • GO:1901313 positive regulation of gene expression; • negative regulation of protein export from nucleus; • negative regulation of ubiquitin-protein transferase activity; • positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; • cellular response to oxidative stress; • positive regulation of androgen receptor activity; • positive regulation of pyrroline-5-carboxylate reductase activity; • GO:0003257, GO:0010735, GO:1901228, GO:1900622, GO:1904488 positive regulation of transcription by RNA polymerase II; • cellular response to hydrogen peroxide; • methylglyoxal metabolic process; • lactate biosynthetic process; • peptidyl-cysteine deglycation; • peptidyl-arginine deglycation; • peptidyl-lysine deglycation; • protein deglycation, glyoxal removal; • protein deglycation, methylglyoxal removal; • glutathione deglycation; • glyoxal metabolic process; • negative regulation of nitrosative stress-induced intrinsic apoptotic signaling pathway; • positive regulation of acute inflammatory response to antigenic stimulus; • protein deglycosylation; • positive regulation of NAD(P)H oxidase activity; • GO:0100026 Popravka DNK; • cellular response to DNA damage stimulus; • insulin secretion; • glucose homeostasis; • guanine deglycation; • guanine deglycation, methylglyoxal removal; • guanine deglycation, glyoxal removal; • negative regulation of reactive oxygen species biosynthetic process;
	Izvori:Amigo / QuickGO
Ortolozi
	11315
	57320
	ENSG00000116288
	ENSMUSG00000028964
	Q99497
	Q99LX0
	NM_001123377; NM_007262
	NM_020569
	NP_001116849; NP_009193
	NP_065594
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Protein-deglikaza DJ-1, znana i kao protein 7 Parkinsonove bolesti, jest protein/enzim koji je kod ljudi kodiran genom PARK7 sa hromosoma 1.^[5]

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 189 aminokiselina, a molekulska težina 19.891 Da.^[6]

C: Cistein

D: Asparaginska kiselina

E: Glutaminska kiselina

F: Fenilalanin

G: Glicin

H: Histidin

I: Izoleucin

K: Lizin

L: Leucin

M: Metionin

N: Asparagin

P: Prolin

Q: Glutamin

R: Arginin

S: Serin

T: Treonin

V: Valin

W: Triptofan

Y: Tirozin

10	20	30	40	50
MASKRALVIL	AKGAEEMETV	IPVDVMRRAG	IKVTVAGLAG	KDPVQCSRDV
VICPDASLED	AKKEGPYDVV	VLPGGNLGAQ	NLSESAAVKE	ILKEQENRKG
LIAAICAGPT	ALLAHEIGFG	SKVTTHPLAK	DKMMNGGHYT	YSENRVEKDG
LILTSRGPGT	SFEFALAIVE	ALNGKEVAAQ	VKAPLVLKD

Struktura

Gen

Gen PARK7, također poznat kao DJ-1, kodira protein iz porodice peptidaza C56. Ljudski gen PARK7 ima osam egzona i nalazi se na hromozomskom pojasu 1p36.23.^[5]

Protein

Ljudska proteinska deglikaza DJ-1 je veličine 20 kDa i sastoji se od 189 aminokiselina sa ukupno sedam β-lanaca i devet α-heliksa i prisutna je kao dimer.^[7]^[8]^[9] Proteinske strukture ljudskog proteina DJ-1, šaperona Hsp31Escherichia coli, YhbO i YajL i proteaze Archaea evolucijski su konzervirane.^[10]

Funkcija

U oksidativnom stanju, protein deglikaza DJ-1 inhibira agregaciju α-sinukleina putem svoje prateće aktivnosti,^[11]^[12] funkcionifajući na taj način kao redoks-senzitivni šaperon i kao senzor za oksidativnog stresa. U skladu s tim, DJ-1 očigledno štiti neurone od oksidativnog stresa i ćelijske smrti.^[5] Paralelno, protein DJ-1 djeluje kao pozitivan regulator transkripcije zavisne od androgenoreceptorski ovisne transkripcije. DJ-1 se eksprimira u neurvmojoj retini, mrežnjsčnom pigmentnom sloju i njenom epitelu kod sisara, gdje ima neuroprotektivnu ulogu protiv oksidativnog stresa i u fiziološkim i u patološkim stanjima.^[13]^[14]

Pokazalo se da pirolokvnolin-kvinon (PQQ) smanjuje samooksidaciju DJ-1 proteina, što je rani korak u nastanku nekih oblika Parkinsonove bolesti.^[15]

Pokazalo se da funkcionalni DJ-1 protein veže metale i štiti od citotoksičnosti izazvane metalima bakar i živa.^[16]

Klinički značaj

Defekti ovog gena uzrok su autosomno recesivnog ranog početka Parkinsonova bolest 7.^[5]^[17]

Interakcije

Pokazalo se da je PARK7 u interakciji sa:

CASK,^[18]
EFCAB6,^[19] i
PIAS2.^[20]

Također pogledajte

Parkinsonova bolest

Reference

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000116288 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000028964 - Ensembl, maj 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b ^c ^d "Entrez Gene: PARK7".
^ "UniProt, Q99497" (jezik: eng.). Pristupljeno 3. 12. 2021.CS1 održavanje: nepoznati jezik (link)
^ "Uniprot: Q99497 - PARK7_HUMAN".
^ Honbou K, Suzuki NN, Horiuchi M, Niki T, Taira T, Ariga H, Inagaki F (Aug 2003). "The crystal structure of DJ-1, a protein related to male fertility and Parkinson's disease". The Journal of Biological Chemistry. 278 (33): 31380–4. doi:10.1074/jbc.M305878200. PMID 12796482.
^ Tao X, Tong L (Aug 2003). "Crystal structure of human DJ-1, a protein associated with early onset Parkinson's disease". The Journal of Biological Chemistry. 278 (33): 31372–9. doi:10.1074/jbc.M304221200. PMID 12761214.
^ Lee SJ, Kim SJ, Kim IK, Ko J, Jeong CS, Kim GH, Park C, Kang SO, Suh PG, Lee HS, Cha SS (Nov 2003). "Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain". The Journal of Biological Chemistry. 278 (45): 44552–9. doi:10.1074/jbc.M304517200. PMID 12939276.
^ Shendelman S, Jonason A, Martinat C, Leete T, Abeliovich A (Nov 2004). "DJ-1 is a redox-dependent molecular chaperone that inhibits alpha-synuclein aggregate formation". PLOS Biology. 2 (11): e362. doi:10.1371/journal.pbio.0020362. PMC 521177. PMID 15502874.
^ Zhou W, Zhu M, Wilson MA, Petsko GA, Fink AL (Mar 2006). "The oxidation state of DJ-1 regulates its chaperone activity toward alpha-synuclein". Journal of Molecular Biology. 356 (4): 1036–48. doi:10.1016/j.jmb.2005.12.030. PMID 16403519.
^ Martín-Nieto, José; Uribe, Mary Luz; Esteve-Rudd, Julián; Herrero, María Trinidad; Campello, Laura (2019). "A role for DJ-1 against oxidative stress in the mammalian retina". Neuroscience Letters (jezik: engleski). 708: 134361. doi:10.1016/j.neulet.2019.134361. hdl:10045/94474. PMID 31276729. S2CID 195813073.
^ Shadrach, Karen G.; Rayborn, Mary E.; Hollyfield, Joe G.; Bonilha, Vera L. (2013). Shi, Xianglin (ured.). "DJ-1-Dependent Regulation of Oxidative Stress in the Retinal Pigment Epithelium (RPE)". PLOS ONE (jezik: engleski). 8 (7): e67983. Bibcode:2013PLoSO...867983S. doi:10.1371/journal.pone.0067983. PMC 3699467. PMID 23844142.
^ Nunome K, Miyazaki S, Nakano M, Iguchi-Ariga S, Ariga H (Jul 2008). "Pyrroloquinoline quinone prevents oxidative stress-induced neuronal death probably through changes in oxidative status of DJ-1". Biological & Pharmaceutical Bulletin. 31 (7): 1321–6. doi:10.1248/bpb.31.1321. hdl:2115/53726. PMID 18591768.
^ Björkblom B, Adilbayeva A, Maple-Grødem J, Piston D, Ökvist M, Xu XM, Brede C, Larsen JP, Møller SG (2013). "Parkinson disease protein DJ-1 binds metals and protects against metal-induced cytotoxicity". Journal of Biological Chemistry. 288 (31): 22809–20. doi:10.1074/jbc.M113.482091. PMC 3829365. PMID 23792957.
^ Bonifati V, Rizzu P, van Baren MJ, Schaap O, Breedveld GJ, Krieger E, Dekker MC, Squitieri F, Ibanez P, Joosse M, van Dongen JW, Vanacore N, van Swieten JC, Brice A, Meco G, van Duijn CM, Oostra BA, Heutink P (Jan 2003). "Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism". Science. 299 (5604): 256–9. Bibcode:2003Sci...299..256B. doi:10.1126/science.1077209. PMID 12446870. S2CID 27186691.
^ Mukherjee K, Slawson JB, Christmann BL, Griffith LC (2014). "Neuron-specific protein interactions of Drosophila CASK-β are revealed by mass spectrometry". Frontiers in Molecular Neuroscience. 7: 58. doi:10.3389/fnmol.2014.00058. PMC 4075472. PMID 25071438.
^ Niki T, Takahashi-Niki K, Taira T, Iguchi-Ariga SM, Ariga H (Feb 2003). "DJBP: a novel DJ-1-binding protein, negatively regulates the androgen receptor by recruiting histone deacetylase complex, and DJ-1 antagonizes this inhibition by abrogation of this complex". Molecular Cancer Research. 1 (4): 247–61. PMID 12612053.
^ Takahashi K, Taira T, Niki T, Seino C, Iguchi-Ariga SM, Ariga H (Oct 2001). "DJ-1 positively regulates the androgen receptor by impairing the binding of PIASx alpha to the receptor". The Journal of Biological Chemistry. 276 (40): 37556–63. doi:10.1074/jbc.M101730200. PMID 11477070.

Dopunska literatura

Cookson MR (Jan 2003). "Pathways to Parkinsonism". Neuron. 37 (1): 7–10. doi:10.1016/S0896-6273(02)01166-2. PMID 12526767. S2CID 14513509.
Bonifati V, Oostra BA, Heutink P (Mar 2004). "Linking DJ-1 to neurodegeneration offers novel insights for understanding the pathogenesis of Parkinson's disease". Journal of Molecular Medicine. 82 (3): 163–74. doi:10.1007/s00109-003-0512-1. PMID 14712351. S2CID 32685319.
Le W, Appel SH (Feb 2004). "Mutant genes responsible for Parkinson's disease". Current Opinion in Pharmacology. 4 (1): 79–84. doi:10.1016/j.coph.2003.09.005. PMID 15018843.
Abou-Sleiman PM, Healy DG, Wood NW (Oct 2004). "Causes of Parkinson's disease: genetics of DJ-1". Cell and Tissue Research. 318 (1): 185–8. doi:10.1007/s00441-004-0922-6. PMID 15503154. S2CID 9453283.
Pankratz N, Foroud T (Apr 2004). "Genetics of Parkinson disease". NeuroRx. 1 (2): 235–42. doi:10.1602/neurorx.1.2.235. PMC 534935. PMID 15717024.
Heutink P (2006). "PINK-1 and DJ-1--new genes for autosomal recessive Parkinson's disease". Journal of Neural Transmission. Supplementum. Journal of Neural Transmission. Supplementa. 70 (70): 215–9. doi:10.1007/978-3-211-45295-0_33. ISBN 978-3-211-28927-3. PMID 17017532.
Lev N, Roncevic D, Roncevich D, Ickowicz D, Melamed E, Offen D (2007). "Role of DJ-1 in Parkinson's disease". Journal of Molecular Neuroscience. 29 (3): 215–25. doi:10.1385/JMN:29:3:215. PMID 17085780. S2CID 85481215.
Nagakubo D, Taira T, Kitaura H, Ikeda M, Tamai K, Iguchi-Ariga SM, Ariga H (Feb 1997). "DJ-1, a novel oncogene which transforms mouse NIH3T3 cells in cooperation with ras". Biochemical and Biophysical Research Communications. 231 (2): 509–13. doi:10.1006/bbrc.1997.6132. PMID 9070310.
Taira T, Takahashi K, Kitagawa R, Iguchi-Ariga SM, Ariga H (Jan 2001). "Molecular cloning of human and mouse DJ-1 genes and identification of Sp1-dependent activation of the human DJ-1 promoter". Gene. 263 (1–2): 285–92. doi:10.1016/S0378-1119(00)00590-4. PMID 11223268.
van Duijn CM, Dekker MC, Bonifati V, Galjaard RJ, Houwing-Duistermaat JJ, Snijders PJ, Testers L, Breedveld GJ, Horstink M, Sandkuijl LA, van Swieten JC, Oostra BA, Heutink P (Sep 2001). "Park7, a novel locus for autosomal recessive early-onset parkinsonism, on chromosome 1p36". American Journal of Human Genetics. 69 (3): 629–34. doi:10.1086/322996. PMC 1235491. PMID 11462174.
Takahashi K, Taira T, Niki T, Seino C, Iguchi-Ariga SM, Ariga H (Oct 2001). "DJ-1 positively regulates the androgen receptor by impairing the binding of PIASx alpha to the receptor". The Journal of Biological Chemistry. 276 (40): 37556–63. doi:10.1074/jbc.M101730200. PMID 11477070.
Bonifati V, Rizzu P, van Baren MJ, Schaap O, Breedveld GJ, Krieger E, Dekker MC, Squitieri F, Ibanez P, Joosse M, van Dongen JW, Vanacore N, van Swieten JC, Brice A, Meco G, van Duijn CM, Oostra BA, Heutink P (Jan 2003). "Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism". Science. 299 (5604): 256–9. Bibcode:2003Sci...299..256B. doi:10.1126/science.1077209. PMID 12446870. S2CID 27186691.
Bonifati V, Dekker MC, Vanacore N, Fabbrini G, Squitieri F, Marconi R, Antonini A, Brustenghi P, Dalla Libera A, De Mari M, Stocchi F, Montagna P, Gallai V, Rizzu P, van Swieten JC, Oostra B, van Duijn CM, Meco G, Heutink P (Sep 2002). "Autosomal recessive early onset parkinsonism is linked to three loci: PARK2, PARK6, and PARK7". Neurological Sciences. 23 Suppl 2: S59-60. doi:10.1007/s100720200069. PMID 12548343. S2CID 13625056.
Niki T, Takahashi-Niki K, Taira T, Iguchi-Ariga SM, Ariga H (Feb 2003). "DJBP: a novel DJ-1-binding protein, negatively regulates the androgen receptor by recruiting histone deacetylase complex, and DJ-1 antagonizes this inhibition by abrogation of this complex". Molecular Cancer Research. 1 (4): 247–61. PMID 12612053.
Tao X, Tong L (Aug 2003). "Crystal structure of human DJ-1, a protein associated with early onset Parkinson's disease". The Journal of Biological Chemistry. 278 (33): 31372–9. doi:10.1074/jbc.M304221200. PMID 12761214.
Honbou K, Suzuki NN, Horiuchi M, Niki T, Taira T, Ariga H, Inagaki F (Aug 2003). "The crystal structure of DJ-1, a protein related to male fertility and Parkinson's disease". The Journal of Biological Chemistry. 278 (33): 31380–4. doi:10.1074/jbc.M305878200. PMID 12796482.
Dekker M, Bonifati V, van Swieten J, Leenders N, Galjaard RJ, Snijders P, Horstink M, Heutink P, Oostra B, van Duijn C (Jul 2003). "Clinical features and neuroimaging of PARK7-linked parkinsonism". Movement Disorders. 18 (7): 751–7. doi:10.1002/mds.10422. PMID 12815653. S2CID 44253517.
Miller DW, Ahmad R, Hague S, Baptista MJ, Canet-Aviles R, McLendon C, Carter DM, Zhu PP, Stadler J, Chandran J, Klinefelter GR, Blackstone C, Cookson MR (Sep 2003). "L166P mutant DJ-1, causative for recessive Parkinson's disease, is degraded through the ubiquitin-proteasome system". The Journal of Biological Chemistry. 278 (38): 36588–95. doi:10.1074/jbc.M304272200. PMID 12851414.

Vanjski linkovi

Q99497

Ovaj članak uključuje tekst iz Nacionalne medicinske biblioteke Sjedinjenih Država, koji je u javnom vlasništvu.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000116288 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000028964 - Ensembl, maj 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-5] "Entrez Gene: PARK7".

[UniProt-6] "UniProt, Q99497" (jezik: eng.). Pristupljeno 3. 12. 2021.CS1 održavanje: nepoznati jezik (link)

[7] "Uniprot: Q99497 - PARK7_HUMAN".

[8] Honbou K, Suzuki NN, Horiuchi M, Niki T, Taira T, Ariga H, Inagaki F (Aug 2003). "The crystal structure of DJ-1, a protein related to male fertility and Parkinson's disease". The Journal of Biological Chemistry. 278 (33): 31380–4. doi:10.1074/jbc.M305878200. PMID 12796482.

[9] Tao X, Tong L (Aug 2003). "Crystal structure of human DJ-1, a protein associated with early onset Parkinson's disease". The Journal of Biological Chemistry. 278 (33): 31372–9. doi:10.1074/jbc.M304221200. PMID 12761214.

[10] Lee SJ, Kim SJ, Kim IK, Ko J, Jeong CS, Kim GH, Park C, Kang SO, Suh PG, Lee HS, Cha SS (Nov 2003). "Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain". The Journal of Biological Chemistry. 278 (45): 44552–9. doi:10.1074/jbc.M304517200. PMID 12939276.

[11] Shendelman S, Jonason A, Martinat C, Leete T, Abeliovich A (Nov 2004). "DJ-1 is a redox-dependent molecular chaperone that inhibits alpha-synuclein aggregate formation". PLOS Biology. 2 (11): e362. doi:10.1371/journal.pbio.0020362. PMC 521177. PMID 15502874.

[12] Zhou W, Zhu M, Wilson MA, Petsko GA, Fink AL (Mar 2006). "The oxidation state of DJ-1 regulates its chaperone activity toward alpha-synuclein". Journal of Molecular Biology. 356 (4): 1036–48. doi:10.1016/j.jmb.2005.12.030. PMID 16403519.

[13] Martín-Nieto, José; Uribe, Mary Luz; Esteve-Rudd, Julián; Herrero, María Trinidad; Campello, Laura (2019). "A role for DJ-1 against oxidative stress in the mammalian retina". Neuroscience Letters (jezik: engleski). 708: 134361. doi:10.1016/j.neulet.2019.134361. hdl:10045/94474. PMID 31276729. S2CID 195813073.

[14] Shadrach, Karen G.; Rayborn, Mary E.; Hollyfield, Joe G.; Bonilha, Vera L. (2013). Shi, Xianglin (ured.). "DJ-1-Dependent Regulation of Oxidative Stress in the Retinal Pigment Epithelium (RPE)". PLOS ONE (jezik: engleski). 8 (7): e67983. Bibcode:2013PLoSO...867983S. doi:10.1371/journal.pone.0067983. PMC 3699467. PMID 23844142.

[15] Nunome K, Miyazaki S, Nakano M, Iguchi-Ariga S, Ariga H (Jul 2008). "Pyrroloquinoline quinone prevents oxidative stress-induced neuronal death probably through changes in oxidative status of DJ-1". Biological & Pharmaceutical Bulletin. 31 (7): 1321–6. doi:10.1248/bpb.31.1321. hdl:2115/53726. PMID 18591768.

[pmid23792957-16] Björkblom B, Adilbayeva A, Maple-Grødem J, Piston D, Ökvist M, Xu XM, Brede C, Larsen JP, Møller SG (2013). "Parkinson disease protein DJ-1 binds metals and protects against metal-induced cytotoxicity". Journal of Biological Chemistry. 288 (31): 22809–20. doi:10.1074/jbc.M113.482091. PMC 3829365. PMID 23792957.

[pmid_12446870-17] Bonifati V, Rizzu P, van Baren MJ, Schaap O, Breedveld GJ, Krieger E, Dekker MC, Squitieri F, Ibanez P, Joosse M, van Dongen JW, Vanacore N, van Swieten JC, Brice A, Meco G, van Duijn CM, Oostra BA, Heutink P (Jan 2003). "Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism". Science. 299 (5604): 256–9. Bibcode:2003Sci...299..256B. doi:10.1126/science.1077209. PMID 12446870. S2CID 27186691.

[pmid25071438-18] Mukherjee K, Slawson JB, Christmann BL, Griffith LC (2014). "Neuron-specific protein interactions of Drosophila CASK-β are revealed by mass spectrometry". Frontiers in Molecular Neuroscience. 7: 58. doi:10.3389/fnmol.2014.00058. PMC 4075472. PMID 25071438.

[pmid12612053-19] Niki T, Takahashi-Niki K, Taira T, Iguchi-Ariga SM, Ariga H (Feb 2003). "DJBP: a novel DJ-1-binding protein, negatively regulates the androgen receptor by recruiting histone deacetylase complex, and DJ-1 antagonizes this inhibition by abrogation of this complex". Molecular Cancer Research. 1 (4): 247–61. PMID 12612053.

[pmid11477070-20] Takahashi K, Taira T, Niki T, Seino C, Iguchi-Ariga SM, Ariga H (Oct 2001). "DJ-1 positively regulates the androgen receptor by impairing the binding of PIASx alpha to the receptor". The Journal of Biological Chemistry. 276 (40): 37556–63. doi:10.1074/jbc.M101730200. PMID 11477070.

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p r u Enzimi
Teme	Aktivno mjesto Alosterna regulacija Difuzijski limitirani enzim EC broj Enzimska kataliza Inhibicija enzimskih reakcija Kinetika enzima Koenzim Kooperativnost Lineweaver–Burkov dijagram Michaelis–Mentenova kinetika Mjesto vezanja Spisak enzima
Tipovi	EC1 Oksidoreduktaze/spisak EC2 Transferaze/spisak EC3 Hidrolaze/spisak EC4 Lijaze/spisak EC5 Izomeraze/spisak EC6 Ligaze/spisak