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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Thioredoxin-dependent peroxide reductase, mitochondrial''' is an [[enzyme]] that in humans is encoded by the ''PRDX3'' [[gene]].<ref name="pmid7733872">{{cite journal | vauthors = Tsuji K, Copeland NG, Jenkins NA, Obinata M | title = Mammalian antioxidant protein complements alkylhydroperoxide reductase (ahpC) mutation in Escherichia coli | journal = Biochem. J. | volume = 307 | issue = 2 | pages = 377–81  | date = May 1995 | pmid = 7733872 | pmc = 1136659 | doi =  10.1042/bj3070377}}</ref><ref name="pmid9363753">{{cite journal | vauthors = Watabe S, Hiroi T, Yamamoto Y, Fujioka Y, Hasegawa H, Yago N, Takahashi SY | title = SP-22 is a thioredoxin-dependent peroxide reductase in mitochondria | journal = Eur. J. Biochem. | volume = 249 | issue = 1 | pages = 52–60  | date = Dec 1997 | pmid = 9363753 | pmc =  | doi = 10.1111/j.1432-1033.1997.t01-1-00052.x }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PRDX3 peroxiredoxin 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10935| accessdate = }}</ref> It is a member of the [[peroxiredoxin]] family of antioxidant enzymes.
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_PRDX3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1zye.
| PDB = {{PDB2|1zye}}
| Name = Peroxiredoxin 3
| HGNCid = 9354
| Symbol = PRDX3
| AltSymbols =; MER5; AOP-1; AOP1; MGC104387; MGC24293; PRO1748; SP-22
| OMIM = 604769
| ECnumber = 
| Homologene = 4944
| MGIid = 88034
| GeneAtlas_image1 = PBB_GE_PRDX3_201619_at_tn.png
| Function = {{GNF_GO|id=GO:0004601 |text = peroxidase activity}} {{GNF_GO|id=GO:0008785 |text = alkyl hydroperoxide reductase activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0019901 |text = protein kinase binding}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}} {{GNF_GO|id=GO:0051920 |text = peroxiredoxin activity}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0008385 |text = IkappaB kinase complex}}
| Process = {{GNF_GO|id=GO:0051092 |text = activation of NF-kappaB transcription factor}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 10935
    | Hs_Ensembl = ENSG00000165672
    | Hs_RefseqProtein = NP_006784
    | Hs_RefseqmRNA = NM_006793
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 10
    | Hs_GenLoc_start = 120917205
    | Hs_GenLoc_end = 120928335
    | Hs_Uniprot = P30048
    | Mm_EntrezGene = 11757
    | Mm_Ensembl = ENSMUSG00000024997
    | Mm_RefseqmRNA = NM_007452
    | Mm_RefseqProtein = NP_031478
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 19
    | Mm_GenLoc_start = 60918750
    | Mm_GenLoc_end = 60929177
    | Mm_Uniprot = Q8K4K8
  }}
}}
'''Peroxiredoxin 3''', also known as '''PRDX3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PRDX3 peroxiredoxin 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10935| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
This gene encodes a protein with [[antioxidant]] function and is localized in the [[mitochondrion]]. This gene shows significant nucleotide sequence similarity to the gene coding for the C22 subunit of [[Salmonella]] typhimurium alkylhydroperoxide reductase. Expression of this gene product in ''E. coli'' deficient in the C22-subunit gene rescued resistance of the [[bacteria]] to alkylhydroperoxide. The human and mouse genes are highly conserved, and they map to the regions syntenic between mouse and human chromosomes. Sequence comparisons with recently cloned mammalian homologues suggest that these genes consist of a family that is responsible for regulation of cellular [[Cell proliferation|proliferation]], [[Cellular differentiation|differentiation]], and antioxidant functions. Two transcript variants encoding two different isoforms have been found for this gene.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a protein with antioxidant function and is localized in the mitochondrion. This gene shows significant nucleotide sequence similarity to the gene coding for the C22 subunit of Salmonella typhimurium alkylhydroperoxide reductase. Expression of this gene product in E. coli deficient in the C22-subunit gene rescued resistance of the bacteria to alkylhydroperoxide. The human and mouse genes are highly conserved, and they map to the regions syntenic between mouse and human chromosomes. Sequence comparisons with recently cloned mammalian homologues suggest that these genes consist of a family that is responsible for regulation of cellular proliferation, differentiation, and antioxidant functions. Two transcript variants encoding two different isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: PRDX3 peroxiredoxin 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10935| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
PRDX3 has been shown to [[Protein-protein interaction|interact]] with [[MAP3K13]].<ref name=pmid12492477>{{cite journal | vauthors = Masaki M, Ikeda A, Shiraki E, Oka S, Kawasaki T | title = Mixed lineage kinase LZK and antioxidant protein-1 activate NF-kappaB synergistically | journal = Eur. J. Biochem. | volume = 270 | issue = 1 | pages = 76–83  | date = Jan 2003 | pmid = 12492477 | doi = 10.1046/j.1432-1033.2003.03363.x }}</ref>
 
== Clinical significance ==
 
It has been demonstrated that serum peroxiredoxin 3 can be a valuable [[biomarker]] for the diagnosis and assessment of hepatocellular [[carcinoma]]<ref name = "Shi_2014">{{cite journal | vauthors = Shi L, Wu LL, Yang JR, Chen XF, Zhang Y, Chen ZQ, Liu CL, Chi SY, Zheng JY, Huang HX, Yu FJ, Lin XY | title = Serum peroxiredoxin3 is a useful biomarker for early diagnosis and assessment of prognosis of hepatocellular carcinoma in Chinese patients | journal = Asian Pacific Journal of Cancer Prevention | volume = 15 | issue = 7 | date = 2014 | pmid = 24815434 | pages=2979–86 | doi=10.7314/apjcp.2014.15.7.2979}}</ref>  It has been shown that peroxiredoxin proteins protect MCF-7 breast cancer cells against doxorubicin-mediated toxicity.<ref>{{cite journal | vauthors = McDonald C, Muhlbauer J, Perlmutter G, Taparra K, Phelan SA | title = Peroxiredoxin proteins protect MCF-7 breast cancer cells from doxorubicin-induced toxicity | journal = International Journal of Oncology | volume = 45 | issue = 1 | date = Jul 2014 | pmid = 24789097 | doi = 10.3892/ijo.2014.2398 | pages=219–26}}</ref> Additionally, it has been shown that peroxiredoxin 3 is overexpressed in [[prostate cancer]] and promotes cancer cell survival by defending cells against the damages incurred by [[oxidative stress]].<ref>{{cite journal | vauthors = Whitaker HC, Patel D, Howat WJ, Warren AY, Kay JD, Sangan T, Marioni JC, Mitchell J, Aldridge S, Luxton HJ, Massie C, Lynch AG, Neal DE | title = Peroxiredoxin-3 is overexpressed in prostate cancer and promotes cancer cell survival by protecting cells from oxidative stress | journal = British Journal of Cancer | volume = 109 | issue = 4 | date = Aug 2013 | pmid = 23880827 | doi = 10.1038/bjc.2013.396 | pages=983–93 | pmc=3749568}}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R | title = Human liver protein map: a reference database established by microsequencing and gel comparison | journal = Electrophoresis | volume = 13 | issue = 12 | pages = 992–1001 | year = 1992 | pmid = 1286669 | doi = 10.1002/elps.11501301201 }}
| citations =
* {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1–2 | pages = 171–4 | year = 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
*{{cite journal | author=Hochstrasser DF, Frutiger S, Paquet N, ''et al.'' |title=Human liver protein map: a reference database established by microsequencing and gel comparison. |journal=Electrophoresis |volume=13 |issue= 12 |pages= 992-1001 |year= 1993 |pmid= 1286669 |doi= }}
* {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1–2 | pages = 149–56 | year = 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
*{{cite journal  | author=Tsuji K, Copeland NG, Jenkins NA, Obinata M |title=Mammalian antioxidant protein complements alkylhydroperoxide reductase (ahpC) mutation in Escherichia coli. |journal=Biochem. J. |volume=307 ( Pt 2) |issue=  |pages= 377-81 |year= 1995 |pmid= 7733872 |doi=  }}
* {{cite journal | vauthors = Shih SF, Wu YH, Hung CH, Yang HY, Lin JY | title = Abrin triggers cell death by inactivating a thiol-specific antioxidant protein | journal = J. Biol. Chem. | volume = 276 | issue = 24 | pages = 21870–7 | year = 2001 | pmid = 11285261 | doi = 10.1074/jbc.M100571200 }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
* {{cite journal | vauthors = Suzuki H, Fukunishi Y, Kagawa I, Saito R, Oda H, Endo T, Kondo S, Bono H, Okazaki Y, Hayashizaki Y | title = Protein-protein interaction panel using mouse full-length cDNAs | journal = Genome Res. | volume = 11 | issue = 10 | pages = 1758–65 | year = 2001 | pmid = 11591653 | pmc = 311163 | doi = 10.1101/gr.180101 }}
*{{cite journal  | author=Watabe S, Hiroi T, Yamamoto Y, ''et al.'' |title=SP-22 is a thioredoxin-dependent peroxide reductase in mitochondria. |journal=Eur. J. Biochem. |volume=249 |issue= 1 |pages= 52-60 |year= 1997 |pmid= 9363753 |doi=  }}
* {{cite journal | vauthors = Kim SH, Fountoulakis M, Cairns N, Lubec G | title = Protein levels of human peroxiredoxin subtypes in brains of patients with Alzheimer's disease and Down syndrome | journal = J. Neural Transm. Suppl. | volume = | issue = 61 | pages = 223–35 | year = 2001 | pmid = 11771746 | doi = 10.1007/978-3-7091-6262-0_18 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
* {{cite journal | vauthors = Rabilloud T, Heller M, Gasnier F, Luche S, Rey C, Aebersold R, Benahmed M, Louisot P, Lunardi J | title = Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site | journal = J. Biol. Chem. | volume = 277 | issue = 22 | pages = 19396–401 | year = 2002 | pmid = 11904290 | doi = 10.1074/jbc.M106585200 }}
*{{cite journal | author=Shih SF, Wu YH, Hung CH, ''et al.'' |title=Abrin triggers cell death by inactivating a thiol-specific antioxidant protein. |journal=J. Biol. Chem. |volume=276 |issue= 24 |pages= 21870-7 |year= 2001 |pmid= 11285261 |doi= 10.1074/jbc.M100571200 }}
* {{cite journal | vauthors = Wonsey DR, Zeller KI, Dang CV | title = The c-Myc target gene PRDX3 is required for mitochondrial homeostasis and neoplastic transformation | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 99 | issue = 10 | pages = 6649–54 | year = 2002 | pmid = 12011429 | pmc = 124457 | doi = 10.1073/pnas.102523299 }}
*{{cite journal | author=Suzuki H, Fukunishi Y, Kagawa I, ''et al.'' |title=Protein-protein interaction panel using mouse full-length cDNAs. |journal=Genome Res. |volume=11 |issue= 10 |pages= 1758-65 |year= 2001 |pmid= 11591653 |doi= 10.1101/gr.180101 }}
* {{cite journal | vauthors = Wagner E, Luche S, Penna L, Chevallet M, Van Dorsselaer A, Leize-Wagner E, Rabilloud T | title = A method for detection of overoxidation of cysteines: peroxiredoxins are oxidized in vivo at the active-site cysteine during oxidative stress | journal = Biochem. J. | volume = 366 | issue = Pt 3 | pages = 777–85 | year = 2002 | pmid = 12059788 | pmc = 1222825 | doi = 10.1042/BJ20020525 }}
*{{cite journal | author=Kim SH, Fountoulakis M, Cairns N, Lubec G |title=Protein levels of human peroxiredoxin subtypes in brains of patients with Alzheimer's disease and Down syndrome. |journal=J. Neural Transm. Suppl. |volume= |issue= 61 |pages= 223-35 |year= 2002 |pmid= 11771746 |doi= }}
* {{cite journal | vauthors = Shen C, Nathan C | title = Nonredundant antioxidant defense by multiple two-cysteine peroxiredoxins in human prostate cancer cells | journal = Mol. Med. | volume = 8 | issue = 2 | pages = 95–102 | year = 2002 | pmid = 12080185 | pmc = 2039972 | doi = }}
*{{cite journal | author=Rabilloud T, Heller M, Gasnier F, ''et al.'' |title=Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site. |journal=J. Biol. Chem. |volume=277 |issue= 22 |pages= 19396-401 |year= 2002 |pmid= 11904290 |doi= 10.1074/jbc.M106585200 }}
* {{cite journal | vauthors = Masaki M, Ikeda A, Shiraki E, Oka S, Kawasaki T | title = Mixed lineage kinase LZK and antioxidant protein-1 activate NF-kappaB synergistically | journal = Eur. J. Biochem. | volume = 270 | issue = 1 | pages = 76–83 | year = 2003 | pmid = 12492477 | doi = 10.1046/j.1432-1033.2003.03363.x }}
*{{cite journal | author=Wonsey DR, Zeller KI, Dang CV |title=The c-Myc target gene PRDX3 is required for mitochondrial homeostasis and neoplastic transformation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 10 |pages= 6649-54 |year= 2002 |pmid= 12011429 |doi= 10.1073/pnas.102523299 }}
* {{cite journal | vauthors = Choi JH, Kim TN, Kim S, Baek SH, Kim JH, Lee SR, Kim JR | title = Overexpression of mitochondrial thioredoxin reductase and peroxiredoxin III in hepatocellular carcinomas | journal = Anticancer Res. | volume = 22 | issue = 6A | pages = 3331–5 | year = 2003 | pmid = 12530083 | doi =  }}
*{{cite journal | author=Wagner E, Luche S, Penna L, ''et al.'' |title=A method for detection of overoxidation of cysteines: peroxiredoxins are oxidized in vivo at the active-site cysteine during oxidative stress. |journal=Biochem. J. |volume=366 |issue= Pt 3 |pages= 777-85 |year= 2002 |pmid= 12059788 |doi= 10.1042/BJ20020525 }}
* {{cite journal | vauthors = Krapfenbauer K, Engidawork E, Cairns N, Fountoulakis M, Lubec G | title = Aberrant expression of peroxiredoxin subtypes in neurodegenerative disorders | journal = Brain Res. | volume = 967 | issue = 1–2 | pages = 152–60 | year = 2003 | pmid = 12650976 | doi = 10.1016/S0006-8993(02)04243-9 }}
*{{cite journal | author=Shen C, Nathan C |title=Nonredundant antioxidant defense by multiple two-cysteine peroxiredoxins in human prostate cancer cells. |journal=Mol. Med. |volume=8 |issue= 2 |pages= 95-102 |year= 2002 |pmid= 12080185 |doi= }}
* {{cite journal | vauthors = Chang TS, Cho CS, Park S, Yu S, Kang SW, Rhee SG | title = Peroxiredoxin III, a mitochondrion-specific peroxidase, regulates apoptotic signaling by mitochondria | journal = J. Biol. Chem. | volume = 279 | issue = 40 | pages = 41975–84 | year = 2004 | pmid = 15280382 | doi = 10.1074/jbc.M407707200 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{cite journal | vauthors = Liu L, Yang C, Yuan J, Chen X, Xu J, Wei Y, Yang J, Lin G, Yu L | title = RPK118, a PX domain-containing protein, interacts with peroxiredoxin-3 through pseudo-kinase domains | journal = Mol. Cells | volume = 19 | issue = 1 | pages = 39–45 | year = 2005 | pmid = 15750338 | doi =  }}
*{{cite journal | author=Masaki M, Ikeda A, Shiraki E, ''et al.'' |title=Mixed lineage kinase LZK and antioxidant protein-1 activate NF-kappaB synergistically. |journal=Eur. J. Biochem. |volume=270 |issue= 1 |pages= 76-83 |year= 2003 |pmid= 12492477 |doi= }}
*{{cite journal | author=Choi JH, Kim TN, Kim S, ''et al.'' |title=Overexpression of mitochondrial thioredoxin reductase and peroxiredoxin III in hepatocellular carcinomas. |journal=Anticancer Res. |volume=22 |issue= 6A |pages= 3331-5 |year= 2003 |pmid= 12530083 |doi=  }}
*{{cite journal | author=Krapfenbauer K, Engidawork E, Cairns N, ''et al.'' |title=Aberrant expression of peroxiredoxin subtypes in neurodegenerative disorders. |journal=Brain Res. |volume=967 |issue= 1-2 |pages= 152-60 |year= 2003 |pmid= 12650976 |doi=  }}
*{{cite journal  | author=Deloukas P, Earthrowl ME, Grafham DV, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 10. |journal=Nature |volume=429 |issue= 6990 |pages= 375-81 |year= 2004 |pmid= 15164054 |doi= 10.1038/nature02462 }}
*{{cite journal | author=Chang TS, Cho CS, Park S, ''et al.'' |title=Peroxiredoxin III, a mitochondrion-specific peroxidase, regulates apoptotic signaling by mitochondria. |journal=J. Biol. Chem. |volume=279 |issue= 40 |pages= 41975-84 |year= 2004 |pmid= 15280382 |doi= 10.1074/jbc.M407707200 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Liu L, Yang C, Yuan J, ''et al.'' |title=RPK118, a PX domain-containing protein, interacts with peroxiredoxin-3 through pseudo-kinase domains. |journal=Mol. Cells |volume=19 |issue= 1 |pages= 39-45 |year= 2005 |pmid= 15750338 |doi=  }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{PDB Gallery|geneid=10935}}
{{WikiDoc Sources}}
{{Peroxidases}}
 
 
{{gene-10-stub}}

Latest revision as of 18:38, 7 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Thioredoxin-dependent peroxide reductase, mitochondrial is an enzyme that in humans is encoded by the PRDX3 gene.[1][2][3] It is a member of the peroxiredoxin family of antioxidant enzymes.

Function

This gene encodes a protein with antioxidant function and is localized in the mitochondrion. This gene shows significant nucleotide sequence similarity to the gene coding for the C22 subunit of Salmonella typhimurium alkylhydroperoxide reductase. Expression of this gene product in E. coli deficient in the C22-subunit gene rescued resistance of the bacteria to alkylhydroperoxide. The human and mouse genes are highly conserved, and they map to the regions syntenic between mouse and human chromosomes. Sequence comparisons with recently cloned mammalian homologues suggest that these genes consist of a family that is responsible for regulation of cellular proliferation, differentiation, and antioxidant functions. Two transcript variants encoding two different isoforms have been found for this gene.[3]

Interactions

PRDX3 has been shown to interact with MAP3K13.[4]

Clinical significance

It has been demonstrated that serum peroxiredoxin 3 can be a valuable biomarker for the diagnosis and assessment of hepatocellular carcinoma[5] It has been shown that peroxiredoxin proteins protect MCF-7 breast cancer cells against doxorubicin-mediated toxicity.[6] Additionally, it has been shown that peroxiredoxin 3 is overexpressed in prostate cancer and promotes cancer cell survival by defending cells against the damages incurred by oxidative stress.[7]

References

  1. ↑ Tsuji K, Copeland NG, Jenkins NA, Obinata M (May 1995). "Mammalian antioxidant protein complements alkylhydroperoxide reductase (ahpC) mutation in Escherichia coli". Biochem. J. 307 (2): 377–81. doi:10.1042/bj3070377. PMC 1136659. PMID 7733872.
  2. ↑ Watabe S, Hiroi T, Yamamoto Y, Fujioka Y, Hasegawa H, Yago N, Takahashi SY (Dec 1997). "SP-22 is a thioredoxin-dependent peroxide reductase in mitochondria". Eur. J. Biochem. 249 (1): 52–60. doi:10.1111/j.1432-1033.1997.t01-1-00052.x. PMID 9363753.
  3. ↑ 3.0 3.1 "Entrez Gene: PRDX3 peroxiredoxin 3".
  4. ↑ Masaki M, Ikeda A, Shiraki E, Oka S, Kawasaki T (Jan 2003). "Mixed lineage kinase LZK and antioxidant protein-1 activate NF-kappaB synergistically". Eur. J. Biochem. 270 (1): 76–83. doi:10.1046/j.1432-1033.2003.03363.x. PMID 12492477.
  5. ↑ Shi L, Wu LL, Yang JR, Chen XF, Zhang Y, Chen ZQ, Liu CL, Chi SY, Zheng JY, Huang HX, Yu FJ, Lin XY (2014). "Serum peroxiredoxin3 is a useful biomarker for early diagnosis and assessment of prognosis of hepatocellular carcinoma in Chinese patients". Asian Pacific Journal of Cancer Prevention. 15 (7): 2979–86. doi:10.7314/apjcp.2014.15.7.2979. PMID 24815434.
  6. ↑ McDonald C, Muhlbauer J, Perlmutter G, Taparra K, Phelan SA (Jul 2014). "Peroxiredoxin proteins protect MCF-7 breast cancer cells from doxorubicin-induced toxicity". International Journal of Oncology. 45 (1): 219–26. doi:10.3892/ijo.2014.2398. PMID 24789097.
  7. ↑ Whitaker HC, Patel D, Howat WJ, Warren AY, Kay JD, Sangan T, Marioni JC, Mitchell J, Aldridge S, Luxton HJ, Massie C, Lynch AG, Neal DE (Aug 2013). "Peroxiredoxin-3 is overexpressed in prostate cancer and promotes cancer cell survival by protecting cells from oxidative stress". British Journal of Cancer. 109 (4): 983–93. doi:10.1038/bjc.2013.396. PMC 3749568. PMID 23880827.

Further reading


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