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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
'''Nicotinamide mononucleotide adenylyltransferase 1''' is an [[enzyme]] that in humans is encoded by the ''NMNAT1'' [[gene]].<ref name="pmid11248244">{{cite journal |vauthors=Schweiger M, Hennig K, Lerner F, Niere M, Hirsch-Kauffmann M, Specht T, Weise C, Oei SL, Ziegler M | title = Characterization of recombinant human nicotinamide mononucleotide adenylyl transferase (NMNAT), a nuclear enzyme essential for NAD synthesis | journal = FEBS Lett | volume = 492 | issue = 1–2 | pages = 95–100 |date=Mar 2001 | pmid = 11248244 | pmc =  | doi =10.1016/S0014-5793(01)02180-9  }}</ref><ref name="pmid11027696">{{cite journal |vauthors=Emanuelli M, Carnevali F, Saccucci F, Pierella F, Amici A, Raffaelli N, Magni G | title = Molecular cloning, chromosomal localization, tissue mRNA levels, bacterial expression, and enzymatic properties of human NMN adenylyltransferase | journal = J Biol Chem | volume = 276 | issue = 1 | pages = 406–12 |date=Feb 2001 | pmid = 11027696 | pmc = | doi = 10.1074/jbc.M008700200 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: NMNAT1 nicotinamide nucleotide adenylyltransferase 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=64802| accessdate = }}</ref> It is a member of the [[nicotinamide-nucleotide adenylyltransferase]]s.
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- 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_NMNAT1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1gzu.
| PDB = {{PDB2|1gzu}}, {{PDB2|1kku}}, {{PDB2|1kqn}}, {{PDB2|1kqo}}, {{PDB2|1kr2}}
| Name = Nicotinamide nucleotide adenylyltransferase 1
| HGNCid = 17877
| Symbol = NMNAT1
| AltSymbols =; NMNAT; PNAT-1; PNAT1
| OMIM = 608700
| ECnumber = 2.7.7.1
| Homologene = 39074
| MGIid = 1913704
| Function = {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0000309 |text = nicotinamide-nucleotide adenylyltransferase activity}} {{GNF_GO|id=GO:0004515 |text = nicotinate-nucleotide adenylyltransferase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0009058 |text = biosynthetic process}} {{GNF_GO|id=GO:0009435 |text = NAD biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 64802
    | Hs_Ensembl = ENSG00000173614
    | Hs_RefseqProtein = NP_073624
    | Hs_RefseqmRNA = NM_022787
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 9926073
    | Hs_GenLoc_end = 9968143
    | Hs_Uniprot = Q9HAN9
    | Mm_EntrezGene = 66454
    | Mm_Ensembl = ENSMUSG00000028992
    | Mm_RefseqmRNA = NM_133435
    | Mm_RefseqProtein = NP_597679
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 148312409
    | Mm_GenLoc_end = 148329096
    | Mm_Uniprot = Q3V449
  }}
}}
'''Nicotinamide nucleotide adenylyltransferase 1''', also known as '''NMNAT1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NMNAT1 nicotinamide nucleotide adenylyltransferase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=64802| accessdate = }}</ref> It is a member of the [[Nicotinamide-nucleotide adenylyltransferase]]s.


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The coenzyme [[nicotinamide adenine dinucleotide|NAD]] and its derivatives are involved in hundreds of metabolic [[redox]] reactions and are utilized in protein [[ADP-ribosylation]], [[histone]] [[deacetylation]], and in some [[calcium in biology|Ca<sup>2+</sup>]] signaling pathways. NMNAT (EC 2.7.7.1) is a central enzyme in NAD biosynthesis, catalyzing the condensation of nicotinamide mononucleotide (NMN) or nicotinic acid mononucleotide (NaMN) with the AMP moiety of ATP to form NAD or NaAD.<ref name="entrez"/>
{{PBB_Summary
 
| section_title =
NMNAT1 is the most widely expressed of three [[orthologous]] genes with nicotinamide-nucleotide adenylyltransferase (NMNAT) activity. Genetically engineered mice lacking NMNAT1 die during early embryogenesis, indicating a critical role of this gene in organismal viability.{{citation needed|date=August 2013}} In contrast, mice lacking [[NMNAT2]], which is expressed predominantly in neural tissues, complete development but die shortly after birth. However, NMNAT1 is dispensable for cell viability, as homozygous deletion of this gene occurs in glioblastoma tumors and cell lines. NMNAT enzymatic activity is probably essential at the cellular level, as complete ablation of NMNAT activity in model organisms leads to cellular inviability.<ref>{{cite journal  |vauthors=Muller FL, Colla S, Aquilanti E, etal |title=Passenger deletions generate therapeutic vulnerabilities in cancer |journal=Nature |volume=488 |issue=7411 |pages=337–42 |date=August 2012 |pmid=22895339 |pmc=3712624 |doi=10.1038/nature11331 |url=}}</ref>
| summary_text = The coenzyme NAD and its derivatives are involved in hundreds of metabolic redox reactions and are utilized in protein ADP-ribosylation, histone deacetylation, and in some Ca(2+) signaling pathways. NMNAT (EC 2.7.7.1) is a central enzyme in NAD biosynthesis, catalyzing the condensation of nicotinamide mononucleotide (NMN) or nicotinic acid mononucleotide (NaMN) with the AMP moiety of ATP to form NAD or NaAD (Zhang et al., 2003).[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: NMNAT1 nicotinamide nucleotide adenylyltransferase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=64802| accessdate = }}</ref>
 
}}
==Clinical relevance==
Mutations in this gene have been shown associated to retinal degeneration pathologies, like [[Leber's congenital amaurosis]].<ref name="pmid22842230">{{cite journal | vauthors = Koenekoop RK, Wang H, Majewski J, Wang X, Lopez I, Ren H, Chen Y, Li Y, Fishman GA, Genead M, Schwartzentruber J, Solanki N, Traboulsi EI, Cheng J, Logan CV, McKibbin M, Hayward BE, Parry DA, Johnson CA, Nageeb M, Poulter JA, Mohamed MD, Jafri H, Rashid Y, Taylor GR, Keser V, Mardon G, Xu H, Inglehearn CF, Fu Q, Toomes C, Chen R |others = Finding of Rare Disease Genes (FORGE) Canada Consortium | title = Mutations in NMNAT1 cause Leber congenital amaurosis and identify a new disease pathway for retinal degeneration | journal = Nat. Genet. | volume = 44 | issue = 9 | pages = 1035–9 |date=September 2012 | pmid = 22842230 | pmc = 3657614 | doi = 10.1038/ng.2356 }}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{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 }}
| citations =
*{{cite journal   |vauthors=Garavaglia S, D'Angelo I, Emanuelli M, etal |title=Structure of human NMN adenylyltransferase. A key nuclear enzyme for NAD homeostasis |journal=J. Biol. Chem. |volume=277 |issue= 10 |pages= 8524–30 |year= 2002 |pmid= 11751893 |doi= 10.1074/jbc.M111589200 }}
*{{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=Werner E, Ziegler M, Lerner F, etal |title=Crystallization and preliminary X-ray analysis of human nicotinamide mononucleotide adenylyltransferase (NMNAT) |journal=Acta Crystallogr. D |volume=58 |issue= Pt 1 |pages= 140–2 |year= 2002 |pmid= 11752792 |doi=10.1107/S0907444901017437 }}
*{{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=Zhou T, Kurnasov O, Tomchick DR, etal |title=Structure of human nicotinamide/nicotinic acid mononucleotide adenylyltransferase. Basis for the dual substrate specificity and activation of the oncolytic agent tiazofurin |journal=J. Biol. Chem. |volume=277 |issue= 15 |pages= 13148–54 |year= 2002 |pmid= 11788603 |doi= 10.1074/jbc.M111469200 }}
*{{cite journal  | author=Emanuelli M, Carnevali F, Saccucci F, ''et al.'' |title=Molecular cloning, chromosomal localization, tissue mRNA levels, bacterial expression, and enzymatic properties of human NMN adenylyltransferase. |journal=J. Biol. Chem. |volume=276 |issue= 1 |pages= 406-12 |year= 2001 |pmid= 11027696 |doi= 10.1074/jbc.M008700200 }}
*{{cite journal   |vauthors=Fernando FS, Conforti L, Tosi S, etal |title=Human homologue of a gene mutated in the slow Wallerian degeneration (C57BL/Wld(s)) mouse |journal=Gene |volume=284 |issue= 1–2 |pages= 23–9 |year= 2002 |pmid= 11891043 |doi=10.1016/S0378-1119(02)00394-3 }}
*{{cite journal  | author=Schweiger M, Hennig K, Lerner F, ''et al.'' |title=Characterization of recombinant human nicotinamide mononucleotide adenylyl transferase (NMNAT), a nuclear enzyme essential for NAD synthesis. |journal=FEBS Lett. |volume=492 |issue= 1-2 |pages= 95-100 |year= 2001 |pmid= 11248244 |doi= }}
*{{cite journal   |vauthors=Werner E, Ziegler M, Lerner F, etal |title=Crystal structure of human nicotinamide mononucleotide adenylyltransferase in complex with NMN |journal=FEBS Lett. |volume=516 |issue= 1–3 |pages= 239–44 |year= 2002 |pmid= 11959140 |doi=10.1016/S0014-5793(02)02556-5 }}
*{{cite journal | author=Garavaglia S, D'Angelo I, Emanuelli M, ''et al.'' |title=Structure of human NMN adenylyltransferase. A key nuclear enzyme for NAD homeostasis. |journal=J. Biol. Chem. |volume=277 |issue= 10 |pages= 8524-30 |year= 2002 |pmid= 11751893 |doi= 10.1074/jbc.M111589200 }}
*{{cite journal   |vauthors=Raffaelli N, Sorci L, Amici A, etal |title=Identification of a novel human nicotinamide mononucleotide adenylyltransferase |journal=Biochem. Biophys. Res. Commun. |volume=297 |issue= 4 |pages= 835–40 |year= 2002 |pmid= 12359228 |doi=10.1016/S0006-291X(02)02285-4  }}
*{{cite journal | author=Werner E, Ziegler M, Lerner F, ''et al.'' |title=Crystallization and preliminary X-ray analysis of human nicotinamide mononucleotide adenylyltransferase (NMNAT). |journal=Acta Crystallogr. D Biol. Crystallogr. |volume=58 |issue= Pt 1 |pages= 140-2 |year= 2002 |pmid= 11752792 |doi=  }}
*{{cite journal   |vauthors=Zhang X, Kurnasov OV, Karthikeyan S, etal |title=Structural characterization of a human cytosolic NMN/NaMN adenylyltransferase and implication in human NAD biosynthesis |journal=J. Biol. Chem. |volume=278 |issue= 15 |pages= 13503–11 |year= 2003 |pmid= 12574164 |doi= 10.1074/jbc.M300073200 }}
*{{cite journal | author=Zhou T, Kurnasov O, Tomchick DR, ''et al.'' |title=Structure of human nicotinamide/nicotinic acid mononucleotide adenylyltransferase. Basis for the dual substrate specificity and activation of the oncolytic agent tiazofurin. |journal=J. Biol. Chem. |volume=277 |issue= 15 |pages= 13148-54 |year= 2002 |pmid= 11788603 |doi= 10.1074/jbc.M111469200 }}
*{{cite journal   |vauthors=Yalowitz JA, Xiao S, Biju MP, etal |title=Characterization of human brain nicotinamide 5'-mononucleotide adenylyltransferase-2 and expression in human pancreas |journal=Biochem. J. |volume=377 |issue= Pt 2 |pages= 317–26 |year= 2004 |pmid= 14516279 |doi= 10.1042/BJ20030518  | pmc=1223862 }}
*{{cite journal | author=Fernando FS, Conforti L, Tosi S, ''et al.'' |title=Human homologue of a gene mutated in the slow Wallerian degeneration (C57BL/Wld(s)) mouse. |journal=Gene |volume=284 |issue= 1-2 |pages= 23-9 |year= 2002 |pmid= 11891043 |doi=  }}
*{{cite journal   |vauthors=Suzuki Y, Yamashita R, Shirota M, etal |title=Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions |journal=Genome Res. |volume=14 |issue= 9 |pages= 1711–8 |year= 2004 |pmid= 15342556 |doi= 10.1101/gr.2435604  | pmc=515316 }}
*{{cite journal | author=Werner E, Ziegler M, Lerner F, ''et al.'' |title=Crystal structure of human nicotinamide mononucleotide adenylyltransferase in complex with NMN. |journal=FEBS Lett. |volume=516 |issue= 1-3 |pages= 239-44 |year= 2002 |pmid= 11959140 |doi=  }}
*{{cite journal  |vauthors=Berger F, Lau C, Dahlmann M, Ziegler M |title=Subcellular compartmentation and differential catalytic properties of the three human nicotinamide mononucleotide adenylyltransferase isoforms |journal=J. Biol. Chem. |volume=280 |issue= 43 |pages= 36334–41 |year= 2006 |pmid= 16118205 |doi= 10.1074/jbc.M508660200 }}
*{{cite journal | author=Raffaelli N, Sorci L, Amici A, ''et al.'' |title=Identification of a novel human nicotinamide mononucleotide adenylyltransferase. |journal=Biochem. Biophys. Res. Commun. |volume=297 |issue= 4 |pages= 835-40 |year= 2002 |pmid= 12359228 |doi= }}
*{{cite journal   |vauthors=Olsen JV, Blagoev B, Gnad F, etal |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks |journal=Cell |volume=127 |issue= 3 |pages= 635–48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026 }}
*{{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=Berger F, Lau C, Ziegler M |title=Regulation of poly(ADP-ribose) polymerase 1 activity by the phosphorylation state of the nuclear NAD biosynthetic enzyme NMN adenylyl transferase 1 |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=104 |issue= 10 |pages= 3765–70 |year= 2007 |pmid= 17360427 |doi= 10.1073/pnas.0609211104 | pmc=1820658 }}
*{{cite journal | author=Zhang X, Kurnasov OV, Karthikeyan S, ''et al.'' |title=Structural characterization of a human cytosolic NMN/NaMN adenylyltransferase and implication in human NAD biosynthesis. |journal=J. Biol. Chem. |volume=278 |issue= 15 |pages= 13503-11 |year= 2003 |pmid= 12574164 |doi= 10.1074/jbc.M300073200 }}
*{{cite journal | author=Yalowitz JA, Xiao S, Biju MP, ''et al.'' |title=Characterization of human brain nicotinamide 5'-mononucleotide adenylyltransferase-2 and expression in human pancreas. |journal=Biochem. J. |volume=377 |issue= Pt 2 |pages= 317-26 |year= 2004 |pmid= 14516279 |doi= 10.1042/BJ20030518 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | author=Suzuki Y, Yamashita R, Shirota M, ''et al.'' |title=Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions. |journal=Genome Res. |volume=14 |issue= 9 |pages= 1711-8 |year= 2004 |pmid= 15342556 |doi= 10.1101/gr.2435604 }}
*{{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=Berger F, Lau C, Dahlmann M, Ziegler M |title=Subcellular compartmentation and differential catalytic properties of the three human nicotinamide mononucleotide adenylyltransferase isoforms. |journal=J. Biol. Chem. |volume=280 |issue= 43 |pages= 36334-41 |year= 2006 |pmid= 16118205 |doi= 10.1074/jbc.M508660200 }}
*{{cite journal | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal  | author=Olsen JV, Blagoev B, Gnad F, ''et al.'' |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. |journal=Cell |volume=127 |issue= 3 |pages= 635-48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026 }}
*{{cite journal  | author=Berger F, Lau C, Ziegler M |title=Regulation of poly(ADP-ribose) polymerase 1 activity by the phosphorylation state of the nuclear NAD biosynthetic enzyme NMN adenylyl transferase 1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=104 |issue= 10 |pages= 3765-70 |year= 2007 |pmid= 17360427 |doi= 10.1073/pnas.0609211104 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{PDB Gallery|geneid=64802}}
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{{gene-1-stub}}

Latest revision as of 13:06, 5 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

Nicotinamide mononucleotide adenylyltransferase 1 is an enzyme that in humans is encoded by the NMNAT1 gene.[1][2][3] It is a member of the nicotinamide-nucleotide adenylyltransferases.

Function

The coenzyme NAD and its derivatives are involved in hundreds of metabolic redox reactions and are utilized in protein ADP-ribosylation, histone deacetylation, and in some Ca2+ signaling pathways. NMNAT (EC 2.7.7.1) is a central enzyme in NAD biosynthesis, catalyzing the condensation of nicotinamide mononucleotide (NMN) or nicotinic acid mononucleotide (NaMN) with the AMP moiety of ATP to form NAD or NaAD.[3]

NMNAT1 is the most widely expressed of three orthologous genes with nicotinamide-nucleotide adenylyltransferase (NMNAT) activity. Genetically engineered mice lacking NMNAT1 die during early embryogenesis, indicating a critical role of this gene in organismal viability.[citation needed] In contrast, mice lacking NMNAT2, which is expressed predominantly in neural tissues, complete development but die shortly after birth. However, NMNAT1 is dispensable for cell viability, as homozygous deletion of this gene occurs in glioblastoma tumors and cell lines. NMNAT enzymatic activity is probably essential at the cellular level, as complete ablation of NMNAT activity in model organisms leads to cellular inviability.[4]

Clinical relevance

Mutations in this gene have been shown associated to retinal degeneration pathologies, like Leber's congenital amaurosis.[5]

References

  1. ↑ Schweiger M, Hennig K, Lerner F, Niere M, Hirsch-Kauffmann M, Specht T, Weise C, Oei SL, Ziegler M (Mar 2001). "Characterization of recombinant human nicotinamide mononucleotide adenylyl transferase (NMNAT), a nuclear enzyme essential for NAD synthesis". FEBS Lett. 492 (1–2): 95–100. doi:10.1016/S0014-5793(01)02180-9. PMID 11248244.
  2. ↑ Emanuelli M, Carnevali F, Saccucci F, Pierella F, Amici A, Raffaelli N, Magni G (Feb 2001). "Molecular cloning, chromosomal localization, tissue mRNA levels, bacterial expression, and enzymatic properties of human NMN adenylyltransferase". J Biol Chem. 276 (1): 406–12. doi:10.1074/jbc.M008700200. PMID 11027696.
  3. ↑ 3.0 3.1 "Entrez Gene: NMNAT1 nicotinamide nucleotide adenylyltransferase 1".
  4. ↑ Muller FL, Colla S, Aquilanti E, et al. (August 2012). "Passenger deletions generate therapeutic vulnerabilities in cancer". Nature. 488 (7411): 337–42. doi:10.1038/nature11331. PMC 3712624. PMID 22895339.
  5. ↑ Koenekoop RK, Wang H, Majewski J, Wang X, Lopez I, Ren H, Chen Y, Li Y, Fishman GA, Genead M, Schwartzentruber J, Solanki N, Traboulsi EI, Cheng J, Logan CV, McKibbin M, Hayward BE, Parry DA, Johnson CA, Nageeb M, Poulter JA, Mohamed MD, Jafri H, Rashid Y, Taylor GR, Keser V, Mardon G, Xu H, Inglehearn CF, Fu Q, Toomes C, Chen R (September 2012). Finding of Rare Disease Genes (FORGE) Canada Consortium. "Mutations in NMNAT1 cause Leber congenital amaurosis and identify a new disease pathway for retinal degeneration". Nat. Genet. 44 (9): 1035–9. doi:10.1038/ng.2356. PMC 3657614. PMID 22842230.

Further reading


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