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{{Infobox_gene}}
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'''Poly (ADP-ribose) glycohydrolase''' is an [[enzyme]] that in humans is encoded by the ''PARG'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: Poly (ADP-ribose) glycohydrolase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=retrieve&list_uids=8505| accessdate = 2011-11-08 <!-- T12:08:44.097-08:00 --> }}</ref><ref name="pmid9115250">{{cite journal |vauthors=Lin W, Amé JC, Aboul-Ela N, Jacobson EL, Jacobson MK | title = Isolation and characterization of the cDNA encoding bovine poly(ADP-ribose) glycohydrolase | journal = J. Biol. Chem. | volume = 272 | issue = 18 | pages = 11895–901 |date=May 1997 | pmid = 9115250 | doi = 10.1074/jbc.272.18.11895}}</ref><ref name="pmid10449915">{{cite journal |vauthors=Amé JC, Apiou F, Jacobson EL, Jacobson MK | title = Assignment of the poly(ADP-ribose) glycohydrolase gene (PARG) to human chromosome 10q11.23 and mouse chromosome 14B by in situ hybridization | journal = Cytogenet. Cell Genet. | volume = 85 | issue = 3-4 | pages = 269–70 | year = 1999 | pmid = 10449915 | doi = 10.1159/000015310}}</ref>
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| require_manual_inspection = no
Poly (ADP-ribose) glycohydrolase (PARG) is the major enzyme responsible for the [[catabolism]] of poly ([[adenosine diphosphate ribose|ADP-ribose]]), a reversible covalent-modifier of chromosomal proteins.  The protein is found in many tissues and may be subject to [[proteolysis]] generating smaller, active products.<ref name="entrez">{{cite web | title = Entrez Gene: Poly (ADP-ribose) glycohydrolase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=retrieve&list_uids=8505| accessdate = 2011-11-08 <!-- T12:08:44.097-08:00 --> }}</ref>
| update_protein_box = yes
 
| update_summary = yes
==References==
| update_citations = yes
{{reflist}}
 
==Further reading ==
{{refbegin | 2}}
*{{Cite journal
| last1 = Affar | first1 = E. B.
| last2 = Germain | first2 = M.
| last3 = Winstall | first3 = E.
| last4 = Vodenicharov | first4 = M.
| last5 = Shah | first5 = R. G.
| last6 = Salvesen | first6 = G. S.
| last7 = Poirier | first7 = G. G.
| doi = 10.1074/jbc.M007269200
| title = Caspase-3-mediated Processing of Poly(ADP-ribose) Glycohydrolase during Apoptosis
| journal = Journal of Biological Chemistry
| volume = 276
| issue = 4
| pages = 2935–2942
| year = 2000
| pmid = 11053413
}}
*{{Cite journal
| last1 = Ohashi | first1 = S.
| last2 = Kanai | first2 = M.
| last3 = Hanai | first3 = S.
| last4 = Uchiumi | first4 = F.
| last5 = Maruta | first5 = H.
| last6 = Tanuma | first6 = S.
| last7 = Miwa | first7 = M.
| title = Subcellular localization of poly(ADP-ribose) glycohydrolase in mammalian cells
| journal = Biochemical and Biophysical Research Communications
| volume = 307
| issue = 4
| pages = 915–921
| year = 2003
| pmid = 12878198 | doi=10.1016/S0006-291X(03)01272-5
}}
*{{Cite journal
| last1 = Meyer | first1 = R. G.
| last2 = Meyer-Ficca | first2 = M. L.
| last3 = Jacobson | first3 = E. L.
| last4 = Jacobson | first4 = M. K.
| title = Human poly(ADP-ribose) glycohydrolase (PARG) gene and the common promoter sequence it shares with inner mitochondrial membrane translocase 23 (TIM23)
| journal = Gene
| volume = 314
| pages = 181–190
| year = 2003
| pmid = 14527731 | doi=10.1016/S0378-1119(03)00738-8
}}
*{{Cite journal
| last1 = Golovanov | first1 = A. P.
| last2 = Barillà | first2 = D.
| last3 = Golovanova | first3 = M.
| last4 = Hayes | first4 = F.
| last5 = Lian | first5 = L. Y.
| title = ParG, a protein required for active partition of bacterial plasmids, has a dimeric ribbon-helix-helix structure
| journal = Molecular Microbiology
| volume = 50
| issue = 4
| pages = 1141–1153
| year = 2003
| pmid = 14622405 | doi=10.1046/j.1365-2958.2003.03750.x
}}
*{{Cite journal
| last1 = Keil | first1 = C.
| last2 = Petermann | first2 = E.
| last3 = Oei | first3 = S. L.
| doi = 10.1016/j.abb.2004.02.024
| title = Tannins elevate the level of poly(ADP–ribose) in HeLa cell extracts
| journal = Archives of Biochemistry and Biophysics
| volume = 425
| issue = 1
| pages = 115–121
| year = 2004
| pmid = 15081900
}}
*{{Cite journal
| last1 = Meyer-Ficca | first1 = M. L.
| last2 = Meyer | first2 = R. G.
| last3 = Coyle | first3 = D. L.
| last4 = Jacobson | first4 = E. L.
| last5 = Jacobson | first5 = M. K.
| doi = 10.1016/j.yexcr.2004.03.050
| title = Human poly(ADP-ribose) glycohydrolase is expressed in alternative splice variants yielding isoforms that localize to different cell compartments
| journal = Experimental Cell Research
| volume = 297
| issue = 2
| pages = 521–532
| year = 2004
| pmid = 15212953
}}
}}
 
*{{Cite journal
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
  | last1 = Putt | first1 = K. S.
{{GNF_Protein_box
  | last2 = Hergenrother | first2 = P. J.
  | image =
  | doi = 10.1016/j.ab.2004.04.032
| image_source =
  | title = A nonradiometric, high-throughput assay for poly(ADP-ribose) glycohydrolase (PARG): Application to inhibitor identification and evaluation
  | PDB =  
  | journal = Analytical Biochemistry
| Name = Poly (ADP-ribose) glycohydrolase
  | volume = 333
  | HGNCid = 8605
  | issue = 2
  | Symbol = PARG
  | pages = 256–264
| AltSymbols =; PARG99
  | year = 2004
| OMIM = 603501
  | pmid = 15450800
| ECnumber = 
| Homologene = 50532
| MGIid = 1347094
| Function = {{GNF_GO|id=GO:0004649 |text = poly(ADP-ribose) glycohydrolase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005829 |text = cytosol}}
| Process = {{GNF_GO|id=GO:0006974 |text = response to DNA damage stimulus}} {{GNF_GO|id=GO:0016045 |text = detection of bacterium}}
  | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 8505
    | Hs_Ensembl =  
    | Hs_RefseqProtein = XP_942709
    | Hs_RefseqmRNA = XM_937616
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr =
    | Hs_GenLoc_start =  
    | Hs_GenLoc_end =
    | Hs_Uniprot =  
    | Mm_EntrezGene = 26430
    | Mm_Ensembl = ENSMUSG00000021911
    | Mm_RefseqmRNA = NM_011960
    | Mm_RefseqProtein = NP_036090
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 14
    | Mm_GenLoc_start = 31030980
    | Mm_GenLoc_end = 31126556
    | Mm_Uniprot = Q3TUI8
  }}
}}
}}
'''Poly (ADP-ribose) glycohydrolase''', also known as '''PARG''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PARG poly (ADP-ribose) glycohydrolase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8505| accessdate = }}</ref>
*{{Cite journal
 
| last1 = Bonicalzi | first1 = M. -E.
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
| last2 = Haince | first2 = J. -F.
{{PBB_Summary
  | last3 = Droit | first3 = A.
| section_title =  
| last4 = Poirier | first4 = G. G.
| summary_text = Poly(ADP-ribose) glycohydrolase (PARG) is the major enzyme responsible for the catabolism of poly(ADP-ribose), a reversible covalent-modifier of chromosomal proteins.  The protein is found in many tissues and may be subject to proteolysis generating smaller, active products.<ref name="entrez">{{cite web | title = Entrez Gene: PARG poly (ADP-ribose) glycohydrolase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8505| accessdate = }}</ref>
| title = Poly-ADP-ribosylation in health and disease
| doi = 10.1007/s00018-004-4505-1
| journal = CMLS Cellular and Molecular Life Sciences
| volume = 62
| issue = 7–8
| pages = 739–750
| year = 2005
| pmid = 15868399
}}
}}
 
*{{Cite journal
==References==
  | last1 = Bonicalzi | first1 = M. È.
{{reflist|2}}
  | last2 = Gagné | first2 = J. P.
==Further reading==
  | last3 = Gagné | first3 = P.
{{refbegin | 2}}
  | last4 = Ouellet | first4 = M. È.
{{PBB_Further_reading
  | last5 = Hendzel | first5 = M. J.
| citations =
  | last6 = Poirier | first6 = G. G.
*{{cite journal  | author=Bonicalzi ME, Haince JF, Droit A, Poirier GG |title=Regulation of poly(ADP-ribose) metabolism by poly(ADP-ribose) glycohydrolase: where and when? |journal=Cell. Mol. Life Sci. |volume=62 |issue= 7-8 |pages= 739-50 |year= 2005 |pmid= 15868399 |doi= 10.1007/s00018-004-4505-1 }}
  | title = Poly(ADP-ribose) glycohydrolase is a component of the FMRP-associated messenger ribonucleoparticles
*{{cite journal | author=Uchida K, Suzuki H, Maruta H, ''et al.'' |title=Preferential degradation of protein-bound (ADP-ribose)n by nuclear poly(ADP-ribose) glycohydrolase from human placenta. |journal=J. Biol. Chem. |volume=268 |issue= 5 |pages= 3194-200 |year= 1993 |pmid= 8428996 |doi=  }}
  | doi = 10.1042/BJ20050792
*{{cite journal | author=Lin W, Amé JC, Aboul-Ela N, ''et al.'' |title=Isolation and characterization of the cDNA encoding bovine poly(ADP-ribose) glycohydrolase. |journal=J. Biol. Chem. |volume=272 |issue= 18 |pages= 11895-901 |year= 1997 |pmid= 9115250 |doi=  }}
  | journal = Biochemical Journal
*{{cite journal | author=Winstall E, Affar EB, Shah R, ''et al.'' |title=Poly(ADP-ribose) glycohydrolase is present and active in mammalian cells as a 110-kDa protein. |journal=Exp. Cell Res. |volume=246 |issue= 2 |pages= 395-8 |year= 1999 |pmid= 9925755 |doi= 10.1006/excr.1998.4321 }}
  | volume = 392
*{{cite journal | author=Amé JC, Apiou F, Jacobson EL, Jacobson MK |title=Assignment of the poly(ADP-ribose) glycohydrolase gene (PARG) to human chromosome 10q11.23 and mouse chromosome 14B by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=85 |issue= 3-4 |pages= 269-70 |year= 1999 |pmid= 10449915 |doi=  }}
  | issue = 3
*{{cite journal  | author=Affar EB, Germain M, Winstall E, ''et al.'' |title=Caspase-3-mediated processing of poly(ADP-ribose) glycohydrolase during apoptosis. |journal=J. Biol. Chem. |volume=276 |issue= 4 |pages= 2935-42 |year= 2001 |pmid= 11053413 |doi= 10.1074/jbc.M007269200 }}
  | pages = 499–509
*{{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 }}
  | pmc = 1316289
*{{cite journal  | author=Ohashi S, Kanai M, Hanai S, ''et al.'' |title=Subcellular localization of poly(ADP-ribose) glycohydrolase in mammalian cells. |journal=Biochem. Biophys. Res. Commun. |volume=307 |issue= 4 |pages= 915-21 |year= 2003 |pmid= 12878198 |doi=  }}
  | year = 2005
*{{cite journal | author=Meyer RG, Meyer-Ficca ML, Jacobson EL, Jacobson MK |title=Human poly(ADP-ribose) glycohydrolase (PARG) gene and the common promoter sequence it shares with inner mitochondrial membrane translocase 23 (TIM23). |journal=Gene |volume=314 |issue=  |pages= 181-90 |year= 2003 |pmid= 14527731 |doi=  }}
  | pmid = 16117724
*{{cite journal  | author=Golovanov AP, Barillà D, Golovanova M, ''et al.'' |title=ParG, a protein required for active partition of bacterial plasmids, has a dimeric ribbon-helix-helix structure. |journal=Mol. Microbiol. |volume=50 |issue= 4 |pages= 1141-53 |year= 2004 |pmid= 14622405 |doi=  }}
*{{cite journal  | author=Keil C, Petermann E, Oei SL |title=Tannins elevate the level of poly(ADP-ribose) in HeLa cell extracts. |journal=Arch. Biochem. Biophys. |volume=425 |issue= 1 |pages= 115-21 |year= 2004 |pmid= 15081900 |doi= 10.1016/j.abb.2004.02.024 }}
*{{cite journal | author=Meyer-Ficca ML, Meyer RG, Coyle DL, ''et al.'' |title=Human poly(ADP-ribose) glycohydrolase is expressed in alternative splice variants yielding isoforms that localize to different cell compartments. |journal=Exp. Cell Res. |volume=297 |issue= 2 |pages= 521-32 |year= 2004 |pmid= 15212953 |doi= 10.1016/j.yexcr.2004.03.050 }}
*{{cite journal | author=Beausoleil SA, Jedrychowski M, Schwartz D, ''et al.'' |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130-5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101 }}
*{{cite journal | author=Putt KS, Hergenrother PJ |title=A nonradiometric, high-throughput assay for poly(ADP-ribose) glycohydrolase (PARG): application to inhibitor identification and evaluation. |journal=Anal. Biochem. |volume=333 |issue= 2 |pages= 256-64 |year= 2005 |pmid= 15450800 |doi= 10.1016/j.ab.2004.04.032 }}
*{{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=Gagné JP, Bonicalzi ME, Gagné P, ''et al.'' |title=Poly(ADP-ribose) glycohydrolase is a component of the FMRP-associated messenger ribonucleoparticles. |journal=Biochem. J. |volume=392 |issue= Pt 3 |pages= 499-509 |year= 2006 |pmid= 16117724 |doi= 10.1042/BJ20050792 }}
*{{cite journal | author=Blenn C, Althaus FR, Malanga M |title=Poly(ADP-ribose) glycohydrolase silencing protects against H2O2-induced cell death. |journal=Biochem. J. |volume=396 |issue= 3 |pages= 419-29 |year= 2006 |pmid= 16526943 |doi= 10.1042/BJ20051696 }}
*{{cite journal | author=Keil C, Gröbe T, Oei SL |title=MNNG-induced cell death is controlled by interactions between PARP-1, poly(ADP-ribose) glycohydrolase, and XRCC1. |journal=J. Biol. Chem. |volume=281 |issue= 45 |pages= 34394-405 |year= 2006 |pmid= 16963444 |doi= 10.1074/jbc.M606470200 }}
*{{cite journal | author=Meyer RG, Meyer-Ficca ML, Whatcott CJ, ''et al.'' |title=Two small enzyme isoforms mediate mammalian mitochondrial poly(ADP-ribose) glycohydrolase (PARG) activity. |journal=Exp. Cell Res. |volume=313 |issue= 13 |pages= 2920-36 |year= 2007 |pmid= 17509564 |doi= 10.1016/j.yexcr.2007.03.043 }}
}}
}}
{{refend}}
{{refend}}


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Latest revision as of 17:33, 7 September 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

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RefSeq (protein)

n/a

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

Poly (ADP-ribose) glycohydrolase is an enzyme that in humans is encoded by the PARG gene.[1][2][3]

Poly (ADP-ribose) glycohydrolase (PARG) is the major enzyme responsible for the catabolism of poly (ADP-ribose), a reversible covalent-modifier of chromosomal proteins. The protein is found in many tissues and may be subject to proteolysis generating smaller, active products.[1]

References

  1. ↑ 1.0 1.1 "Entrez Gene: Poly (ADP-ribose) glycohydrolase". Retrieved 2011-11-08.
  2. ↑ Lin W, Amé JC, Aboul-Ela N, Jacobson EL, Jacobson MK (May 1997). "Isolation and characterization of the cDNA encoding bovine poly(ADP-ribose) glycohydrolase". J. Biol. Chem. 272 (18): 11895–901. doi:10.1074/jbc.272.18.11895. PMID 9115250.
  3. ↑ Amé JC, Apiou F, Jacobson EL, Jacobson MK (1999). "Assignment of the poly(ADP-ribose) glycohydrolase gene (PARG) to human chromosome 10q11.23 and mouse chromosome 14B by in situ hybridization". Cytogenet. Cell Genet. 85 (3–4): 269–70. doi:10.1159/000015310. PMID 10449915.

Further reading

  • Affar, E. B.; Germain, M.; Winstall, E.; Vodenicharov, M.; Shah, R. G.; Salvesen, G. S.; Poirier, G. G. (2000). "Caspase-3-mediated Processing of Poly(ADP-ribose) Glycohydrolase during Apoptosis". Journal of Biological Chemistry. 276 (4): 2935–2942. doi:10.1074/jbc.M007269200. PMID 11053413.
  • Ohashi, S.; Kanai, M.; Hanai, S.; Uchiumi, F.; Maruta, H.; Tanuma, S.; Miwa, M. (2003). "Subcellular localization of poly(ADP-ribose) glycohydrolase in mammalian cells". Biochemical and Biophysical Research Communications. 307 (4): 915–921. doi:10.1016/S0006-291X(03)01272-5. PMID 12878198.
  • Meyer, R. G.; Meyer-Ficca, M. L.; Jacobson, E. L.; Jacobson, M. K. (2003). "Human poly(ADP-ribose) glycohydrolase (PARG) gene and the common promoter sequence it shares with inner mitochondrial membrane translocase 23 (TIM23)". Gene. 314: 181–190. doi:10.1016/S0378-1119(03)00738-8. PMID 14527731.
  • Golovanov, A. P.; Barillà, D.; Golovanova, M.; Hayes, F.; Lian, L. Y. (2003). "ParG, a protein required for active partition of bacterial plasmids, has a dimeric ribbon-helix-helix structure". Molecular Microbiology. 50 (4): 1141–1153. doi:10.1046/j.1365-2958.2003.03750.x. PMID 14622405.
  • Keil, C.; Petermann, E.; Oei, S. L. (2004). "Tannins elevate the level of poly(ADP–ribose) in HeLa cell extracts". Archives of Biochemistry and Biophysics. 425 (1): 115–121. doi:10.1016/j.abb.2004.02.024. PMID 15081900.
  • Meyer-Ficca, M. L.; Meyer, R. G.; Coyle, D. L.; Jacobson, E. L.; Jacobson, M. K. (2004). "Human poly(ADP-ribose) glycohydrolase is expressed in alternative splice variants yielding isoforms that localize to different cell compartments". Experimental Cell Research. 297 (2): 521–532. doi:10.1016/j.yexcr.2004.03.050. PMID 15212953.
  • Putt, K. S.; Hergenrother, P. J. (2004). "A nonradiometric, high-throughput assay for poly(ADP-ribose) glycohydrolase (PARG): Application to inhibitor identification and evaluation". Analytical Biochemistry. 333 (2): 256–264. doi:10.1016/j.ab.2004.04.032. PMID 15450800.
  • Bonicalzi, M. -E.; Haince, J. -F.; Droit, A.; Poirier, G. G. (2005). "Poly-ADP-ribosylation in health and disease". CMLS Cellular and Molecular Life Sciences. 62 (7–8): 739–750. doi:10.1007/s00018-004-4505-1. PMID 15868399.
  • Bonicalzi, M. È.; Gagné, J. P.; Gagné, P.; Ouellet, M. È.; Hendzel, M. J.; Poirier, G. G. (2005). "Poly(ADP-ribose) glycohydrolase is a component of the FMRP-associated messenger ribonucleoparticles". Biochemical Journal. 392 (3): 499–509. doi:10.1042/BJ20050792. PMC 1316289. PMID 16117724.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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