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{{Infobox_gene}}
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'''AMP deaminase 3''' is an [[enzyme]] that in humans is encoded by the ''AMPD3'' [[gene]].<ref name="pmid1400401">{{cite journal | vauthors = Mahnke-Zizelman DK, Sabina RL | title = Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third AMPD gene exhibiting alternatively spliced 5'-exons | journal = J Biol Chem | volume = 267 | issue = 29 | pages = 20866–77 |date=Nov 1992 | pmid = 1400401 | pmc =  | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: AMPD3 adenosine monophosphate deaminase (isoform E)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=272| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Adenosine monophosphate deaminase (isoform E)
| HGNCid = 470
| Symbol = AMPD3
| AltSymbols =;
| OMIM = 102772
| ECnumber = 
| Homologene = 408
| MGIid = 1096344
| GeneAtlas_image1 = PBB_GE_AMPD3_207992_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_AMPD3_209491_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003876 |text = AMP deaminase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component =  
  | Process = {{GNF_GO|id=GO:0006196 |text = AMP catabolic process}} {{GNF_GO|id=GO:0009117 |text = nucleotide metabolic process}} {{GNF_GO|id=GO:0009168 |text = purine ribonucleoside monophosphate biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 272
    | Hs_Ensembl = ENSG00000133805
    | Hs_RefseqProtein = NP_000471
    | Hs_RefseqmRNA = NM_000480
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 10428800
    | Hs_GenLoc_end = 10485702
    | Hs_Uniprot = Q01432
    | Mm_EntrezGene = 11717
    | Mm_Ensembl = ENSMUSG00000005686
    | Mm_RefseqmRNA = NM_009667
    | Mm_RefseqProtein = NP_033797
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 7
    | Mm_GenLoc_start = 110563781
    | Mm_GenLoc_end = 110603586
    | Mm_Uniprot = Q8CFR4
  }}
}}
'''Adenosine monophosphate deaminase (isoform E)''', also known as '''AMPD3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: AMPD3 adenosine monophosphate deaminase (isoform E)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=272| accessdate = }}</ref>


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{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = This gene encodes a member of the AMP deaminase gene family. The encoded protein is a highly regulated enzyme that catalyzes the hydrolytic deamination of adenosine monophosphate to inosine monophosphate, a branch point in the adenylate catabolic pathway. This gene encodes the erythrocyte (E) isoforms, whereas other family members encode isoforms that predominate in muscle (M) and liver (L) cells. Mutations in this gene lead to the clinically asymptomatic, autosomal recessive condition erythrocyte AMP deaminase deficiency. Alternatively spliced transcript variants encoding different isoforms of this gene have been described.<ref name="entrez">{{cite web | title = Entrez Gene: AMPD3 adenosine monophosphate deaminase (isoform E)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=272| accessdate = }}</ref>
| summary_text = This gene encodes a member of the [[AMP deaminase]] gene family. The encoded protein is a highly regulated enzyme that catalyzes the hydrolytic deamination of adenosine monophosphate to inosine monophosphate, a branch point in the adenylate catabolic pathway. This gene encodes the erythrocyte (E) isoforms, whereas other family members encode isoforms that predominate in muscle (M) and liver (L) cells. Mutations in this gene lead to the clinically asymptomatic, autosomal recessive condition erythrocyte AMP deaminase deficiency. Alternatively spliced transcript variants encoding different isoforms of this gene have been described.<ref name="entrez"/>
}}
}}
==Model organisms==
{| class="wikitable sortable collapsible collapsed" border="1" cellpadding="2" style="float: right;" |
|+ ''Ampd3'' knockout mouse phenotype
|-
! Characteristic!! Phenotype
|-
| [[Homozygote]] viability || bgcolor="#488ED3"|Normal
|-
| Homozygous Fertility || bgcolor="#488ED3"|Normal
|-
| Body weight || bgcolor="#488ED3"|Normal
|-
| [[Open Field (animal test)|Anxiety]] || bgcolor="#488ED3"|Normal
|-
| Neurological assessment || bgcolor="#488ED3"|Normal
|-
| Grip strength || bgcolor="#488ED3"|Normal
|-
| [[Hot plate test|Hot plate]] || bgcolor="#488ED3"|Normal
|-
| [[Dysmorphology]] || bgcolor="#488ED3"|Normal
|-
| [[Indirect calorimetry]] || bgcolor="#488ED3"|Normal
|-
| [[Glucose tolerance test]] || bgcolor="#488ED3"|Normal
|-
| [[Auditory brainstem response]] || bgcolor="#488ED3"|Normal
|-
| [[Dual-energy X-ray absorptiometry|DEXA]] || bgcolor="#488ED3"|Normal
|-
| [[Radiography]] || bgcolor="#488ED3"|Normal
|-
| Body temperature || bgcolor="#488ED3"|Normal
|-
| Eye morphology || bgcolor="#488ED3"|Normal
|-
| [[Clinical chemistry]] || bgcolor="#488ED3"|Normal
|-
| [[Blood plasma|Plasma]] [[immunoglobulin]]s || bgcolor="#C40000"|Abnormal
|-
| [[Haematology]] || bgcolor="#488ED3"|Normal
|-
| [[Peripheral blood lymphocyte]]s || bgcolor="#C40000"|Abnormal<ref name="Peripheral blood lymphocytes">{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MANH/peripheral-blood-lymphocytes/ |title=Peripheral blood lymphocytes data for Ampd3 |publisher=Wellcome Trust Sanger Institute}}</ref>
|-
| [[Micronucleus test]] || bgcolor="#488ED3"|Normal
|-
| Heart weight || bgcolor="#488ED3"|Normal
|-
| Tail epidermis wholemount || bgcolor="#488ED3"|Normal
|-
| Skin Histopathology || bgcolor="#488ED3"|Normal
|-
| Brain histopathology || bgcolor="#C40000"|Abnormal
|-
| Eye Histopathology || bgcolor="#488ED3"|Normal
|-
| MicroCT & Quantitative Faxitron || bgcolor="#C40000"|Abnormal
|-
| ''[[Salmonella]]'' infection || bgcolor="#488ED3"|Normal<ref name="''Salmonella'' infection">{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MANH/salmonella-challenge/ |title=''Salmonella'' infection data for Ampd3 |publisher=Wellcome Trust Sanger Institute}}</ref>
|-
| ''[[Citrobacter]]'' infection || bgcolor="#488ED3"|Normal<ref name="''Citrobacter'' infection">{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MANH/citrobacter-challenge/ |title=''Citrobacter'' infection data for Ampd3 |publisher=Wellcome Trust Sanger Institute}}</ref>
|-
| colspan=2; style="text-align: center;" | All tests and analysis from<ref name="mgp_reference">{{cite journal | doi = 10.1111/j.1755-3768.2010.4142.x | title = The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice | year = 2010 | author = Gerdin AK | journal = Acta Ophthalmologica | volume = 88 | pages =  925–7 }}</ref><ref>[http://www.sanger.ac.uk/mouseportal/ Mouse Resources Portal], Wellcome Trust Sanger Institute.</ref>
|}
[[Model organism]]s have been used in the study of AMPD3 function. A conditional [[knockout mouse]] line, called ''Ampd3<sup>tm2a(KOMP)Wtsi</sup>''<ref name="allele_ref">{{cite web |url=http://www.knockoutmouse.org/martsearch/search?query=Ampd3 |title=International Knockout Mouse Consortium}}</ref><ref name="mgi_allele_ref">{{cite web |url=http://www.informatics.jax.org/searchtool/Search.do?query=MGI:4364610 |title=Mouse Genome Informatics}}</ref> was generated as part of the [[International Knockout Mouse Consortium]] program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.<ref name="pmid21677750">{{Cite journal
| last1 = Skarnes |first1 =W. C.
| doi = 10.1038/nature10163
| last2 = Rosen | first2 = B.
| last3 = West | first3 = A. P.
| last4 = Koutsourakis | first4 = M.
| last5 = Bushell | first5 = W.
| last6 = Iyer | first6 = V.
| last7 = Mujica | first7 = A. O.
| last8 = Thomas | first8 = M.
| last9 = Harrow | first9 = J.
| last10 = Cox | first10 = T.
| last11 = Jackson | first11 = D.
| last12 = Severin | first12 = J.
| last13 = Biggs | first13 = P.
| last14 = Fu | first14 = J.
| last15 = Nefedov | first15 = M.
| last16 = De Jong | first16 = P. J.
| last17 = Stewart | first17 = A. F.
| last18 = Bradley | first18 = A.
| title = A conditional knockout resource for the genome-wide study of mouse gene function
| journal = Nature
| volume = 474
| issue = 7351
| pages = 337–342
| year = 2011
| pmid = 21677750
| pmc =3572410
}}</ref><ref name="mouse_library">{{cite journal | doi = 10.1038/474262a | title = Mouse library set to be knockout | year = 2011 | author = Dolgin E | journal = Nature | volume = 474 | issue = 7351 | pages = 262–3 | pmid = 21677718 }}</ref><ref name="mouse_for_all_reasons">{{cite journal | doi = 10.1016/j.cell.2006.12.018 | title = A Mouse for All Reasons | year = 2007 | journal = Cell | volume = 128 | pages = 9–13 | pmid = 17218247 |vauthors =Collins FS, Rossant J, Wurst W| issue = 1 }}</ref>
Male and female animals underwent a standardized [[phenotypic screen]] to determine the effects of deletion.<ref name="mgp_reference" /><ref name="pmid21722353">{{cite journal| vauthors=van der Weyden L, White JK, Adams DJ, Logan DW| title=The mouse genetics toolkit: revealing function and mechanism. | journal=Genome Biol | year= 2011 | volume= 12 | issue= 6 | pages= 224 | pmid=21722353 | doi=10.1186/gb-2011-12-6-224  | pmc=3218837}}</ref> Twenty eight tests were carried out on [[mutant]] mice and four significant abnormalities were observed.<ref name="mgp_reference" /> Mutant animals had increased IgG1 levels, increased [[trabecular bone]] thickness, decreased B cell numbers / increased granulocyte number and unusual brain histopathology (the thickness of the [[stratum radiatum]] was reduced and the dorsal [[3rd ventricle]] area was increased).<ref name="mgp_reference" />


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|AMPD3}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Zydowo MM |title=Regulatory effects of the lipid-cytosolic enzyme interaction: AMP deaminase. |journal=Acta Biochim. Pol. |volume=40 |issue= 4 |pages= 429-32 |year= 1994 |pmid= 8140814 |doi=  }}
*{{cite journal  | author=Zydowo MM |title=Regulatory effects of the lipid-cytosolic enzyme interaction: AMP deaminase. |journal=Acta Biochim. Pol. |volume=40 |issue= 4 |pages= 429–32 |year= 1994 |pmid= 8140814 |doi=  }}
*{{cite journal  | author=Mahnke-Zizelman DK, Sabina RL |title=Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third AMPD gene exhibiting alternatively spliced 5'-exons. |journal=J. Biol. Chem. |volume=267 |issue= 29 |pages= 20866-77 |year= 1992 |pmid= 1400401 |doi=  }}
*{{cite journal  | vauthors=Yamada Y, Goto H, Ogasawara N |title=Cloning and nucleotide sequence of the cDNA encoding human erythrocyte-specific AMP deaminase. |journal=Biochim. Biophys. Acta |volume=1171 |issue= 1 |pages= 125–8 |year= 1992 |pmid= 1420359 |doi=  10.1016/0167-4781(92)90153-Q}}
*{{cite journal  | author=Yamada Y, Goto H, Ogasawara N |title=Cloning and nucleotide sequence of the cDNA encoding human erythrocyte-specific AMP deaminase. |journal=Biochim. Biophys. Acta |volume=1171 |issue= 1 |pages= 125-8 |year= 1992 |pmid= 1420359 |doi=  }}
*{{cite journal  | vauthors=Ogasawara N, Goto H, Yamada Y |title=Deficiency of AMP deaminase in erythrocytes. |journal=Hum. Genet. |volume=75 |issue= 1 |pages= 15–8 |year= 1987 |pmid= 3804327 |doi= 10.1007/BF00273831 |display-authors=etal}}
*{{cite journal  | author=Ogasawara N, Goto H, Yamada Y, ''et al.'' |title=Deficiency of AMP deaminase in erythrocytes. |journal=Hum. Genet. |volume=75 |issue= 1 |pages= 15-8 |year= 1987 |pmid= 3804327 |doi= }}
*{{cite journal  | vauthors=Yamada Y, Goto H, Murase T, Ogasawara N |title=Molecular basis for human erythrocyte AMP deaminase deficiency: screening for the major point mutation and identification of other mutations. |journal=Hum. Mol. Genet. |volume=3 |issue= 12 |pages= 2243–5 |year= 1995 |pmid= 7881427 |doi=10.1093/hmg/3.12.2243 }}
*{{cite journal  | author=Yamada Y, Goto H, Murase T, Ogasawara N |title=Molecular basis for human erythrocyte AMP deaminase deficiency: screening for the major point mutation and identification of other mutations. |journal=Hum. Mol. Genet. |volume=3 |issue= 12 |pages= 2243-5 |year= 1995 |pmid= 7881427 |doi=  }}
*{{cite journal  | vauthors=Yamada Y, Goto H, Ogasawara N |title=A point mutation responsible for human erythrocyte AMP deaminase deficiency. |journal=Hum. Mol. Genet. |volume=3 |issue= 2 |pages= 331–4 |year= 1994 |pmid= 8004104 |doi=10.1093/hmg/3.2.331 }}
*{{cite journal  | author=Yamada Y, Goto H, Ogasawara N |title=A point mutation responsible for human erythrocyte AMP deaminase deficiency. |journal=Hum. Mol. Genet. |volume=3 |issue= 2 |pages= 331-4 |year= 1994 |pmid= 8004104 |doi=  }}
*{{cite journal  | vauthors=Mahnke-Zizelman DK, Eddy R, Shows TB, Sabina RL |title=Characterization of the human AMPD3 gene reveals that 5' exon usage is subject to transcriptional control by three tandem promoters and alternative splicing. |journal=Biochim. Biophys. Acta |volume=1306 |issue= 1 |pages= 75–92 |year= 1996 |pmid= 8611627 |doi=  10.1016/0167-4781(95)00231-6}}
*{{cite journal  | author=Mahnke-Zizelman DK, Eddy R, Shows TB, Sabina RL |title=Characterization of the human AMPD3 gene reveals that 5' exon useage is subject to transcriptional control by three tandem promoters and alternative splicing. |journal=Biochim. Biophys. Acta |volume=1306 |issue= 1 |pages= 75-92 |year= 1996 |pmid= 8611627 |doi=  }}
*{{cite journal  | vauthors=Fortuin FD, Morisaki T, Holmes EW |title=Subunit composition of AMPD varies in response to changes in AMPD1 and AMPD3 gene expression in skeletal muscle. |journal=Proc. Assoc. Am. Physicians |volume=108 |issue= 4 |pages= 329–33 |year= 1997 |pmid= 8863347 |doi=  }}
*{{cite journal  | author=Fortuin FD, Morisaki T, Holmes EW |title=Subunit composition of AMPD varies in response to changes in AMPD1 and AMPD3 gene expression in skeletal muscle. |journal=Proc. Assoc. Am. Physicians |volume=108 |issue= 4 |pages= 329-33 |year= 1997 |pmid= 8863347 |doi=  }}
*{{cite journal  | vauthors=Mahnke-Zizelman DK, D'cunha J, Wojnar JM |title=Regulation of rat AMP deaminase 3 (isoform C) by development and skeletal muscle fibre type. |journal=Biochem. J. |volume=326 |issue=  2|pages= 521–9 |year= 1997 |pmid= 9291127 |doi=  | pmc=1218700  |display-authors=etal}}
*{{cite journal  | author=Mahnke-Zizelman DK, D'cunha J, Wojnar JM, ''et al.'' |title=Regulation of rat AMP deaminase 3 (isoform C) by development and skeletal muscle fibre type. |journal=Biochem. J. |volume=326 ( Pt 2) |issue=  |pages= 521-9 |year= 1997 |pmid= 9291127 |doi=  }}
*{{cite journal  | vauthors=Yamada Y, Goto H, Wakamatsu N, Ogasawara N |title=A rare case of complete human erythrocyte AMP deaminase deficiency due to two novel missense mutations in AMPD3. |journal=Hum. Mutat. |volume=17 |issue= 1 |pages= 78 |year= 2001 |pmid= 11139257 |doi= 10.1002/1098-1004(2001)17:1<78::AID-HUMU21>3.0.CO;2-B }}
*{{cite journal  | author=Yamada Y, Goto H, Wakamatsu N, Ogasawara N |title=A rare case of complete human erythrocyte AMP deaminase deficiency due to two novel missense mutations in AMPD3. |journal=Hum. Mutat. |volume=17 |issue= 1 |pages= 78 |year= 2001 |pmid= 11139257 |doi= 10.1002/1098-1004(2001)17:1<78::AID-HUMU21>3.0.CO;2-B }}
*{{cite journal  | vauthors=Mahnke-Zizelman DK, Sabina RL |title=N-terminal sequence and distal histidine residues are responsible for pH-regulated cytoplasmic membrane binding of human AMP deaminase isoform E. |journal=J. Biol. Chem. |volume=277 |issue= 45 |pages= 42654–62 |year= 2003 |pmid= 12213808 |doi= 10.1074/jbc.M203473200 }}
*{{cite journal  | author=Mahnke-Zizelman DK, Sabina RL |title=N-terminal sequence and distal histidine residues are responsible for pH-regulated cytoplasmic membrane binding of human AMP deaminase isoform E. |journal=J. Biol. Chem. |volume=277 |issue= 45 |pages= 42654-62 |year= 2003 |pmid= 12213808 |doi= 10.1074/jbc.M203473200 }}
*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |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=139241 |display-authors=etal}}
*{{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=Tomikura Y, Hisatome I, Tsuboi M |title=Coordinate induction of AMP deaminase in human atrium with mitochondrial DNA deletion. |journal=Biochem. Biophys. Res. Commun. |volume=302 |issue= 2 |pages= 372–6 |year= 2003 |pmid= 12604357 |doi=10.1016/S0006-291X(03)00160-8 |display-authors=etal}}
*{{cite journal  | author=Tomikura Y, Hisatome I, Tsuboi M, ''et al.'' |title=Coordinate induction of AMP deaminase in human atrium with mitochondrial DNA deletion. |journal=Biochem. Biophys. Res. Commun. |volume=302 |issue= 2 |pages= 372-6 |year= 2003 |pmid= 12604357 |doi=  }}
*{{cite journal  | vauthors=Mahnke DK, Sabina RL |title=Calcium activates erythrocyte AMP deaminase [isoform E (AMPD3)] through a protein-protein interaction between calmodulin and the N-terminal domain of the AMPD3 polypeptide. |journal=Biochemistry |volume=44 |issue= 14 |pages= 5551–9 |year= 2005 |pmid= 15807549 |doi= 10.1021/bi048121p }}
*{{cite journal  | author=Mahnke DK, Sabina RL |title=Calcium activates erythrocyte AMP deaminase [isoform E (AMPD3)] through a protein-protein interaction between calmodulin and the N-terminal domain of the AMPD3 polypeptide. |journal=Biochemistry |volume=44 |issue= 14 |pages= 5551-9 |year= 2005 |pmid= 15807549 |doi= 10.1021/bi048121p }}
*{{cite journal  | vauthors=Sabina RL, Waldenström A, Ronquist G |title=The contribution of Ca+ calmodulin activation of human erythrocyte AMP deaminase (isoform E) to the erythrocyte metabolic dysregulation of familial phosphofructokinase deficiency. |journal=Haematologica |volume=91 |issue= 5 |pages= 652–5 |year= 2006 |pmid= 16670071 |doi=  }}
*{{cite journal  | author=Sabina RL, Waldenström A, Ronquist G |title=The contribution of Ca+ calmodulin activation of human erythrocyte AMP deaminase (isoform E) to the erythrocyte metabolic dysregulation of familial phosphofructokinase deficiency. |journal=Haematologica |volume=91 |issue= 5 |pages= 652-5 |year= 2006 |pmid= 16670071 |doi=  }}
}}
}}
{{refend}}
{{refend}}


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[[Category:Genes mutated in mice]]

Latest revision as of 18:00, 29 August 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

AMP deaminase 3 is an enzyme that in humans is encoded by the AMPD3 gene.[1][2]

This gene encodes a member of the AMP deaminase gene family. The encoded protein is a highly regulated enzyme that catalyzes the hydrolytic deamination of adenosine monophosphate to inosine monophosphate, a branch point in the adenylate catabolic pathway. This gene encodes the erythrocyte (E) isoforms, whereas other family members encode isoforms that predominate in muscle (M) and liver (L) cells. Mutations in this gene lead to the clinically asymptomatic, autosomal recessive condition erythrocyte AMP deaminase deficiency. Alternatively spliced transcript variants encoding different isoforms of this gene have been described.[2]

Model organisms

Model organisms have been used in the study of AMPD3 function. A conditional knockout mouse line, called Ampd3tm2a(KOMP)Wtsi[8][9] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.[10][11][12]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[6][13] Twenty eight tests were carried out on mutant mice and four significant abnormalities were observed.[6] Mutant animals had increased IgG1 levels, increased trabecular bone thickness, decreased B cell numbers / increased granulocyte number and unusual brain histopathology (the thickness of the stratum radiatum was reduced and the dorsal 3rd ventricle area was increased).[6]

References

  1. ↑ Mahnke-Zizelman DK, Sabina RL (Nov 1992). "Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third AMPD gene exhibiting alternatively spliced 5'-exons". J Biol Chem. 267 (29): 20866–77. PMID 1400401.
  2. ↑ 2.0 2.1 "Entrez Gene: AMPD3 adenosine monophosphate deaminase (isoform E)".
  3. ↑ "Peripheral blood lymphocytes data for Ampd3". Wellcome Trust Sanger Institute.
  4. ↑ "Salmonella infection data for Ampd3". Wellcome Trust Sanger Institute.
  5. ↑ "Citrobacter infection data for Ampd3". Wellcome Trust Sanger Institute.
  6. ↑ 6.0 6.1 6.2 6.3 Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
  7. ↑ Mouse Resources Portal, Wellcome Trust Sanger Institute.
  8. ↑ "International Knockout Mouse Consortium".
  9. ↑ "Mouse Genome Informatics".
  10. ↑ Skarnes, W. C.; Rosen, B.; West, A. P.; Koutsourakis, M.; Bushell, W.; Iyer, V.; Mujica, A. O.; Thomas, M.; Harrow, J.; Cox, T.; Jackson, D.; Severin, J.; Biggs, P.; Fu, J.; Nefedov, M.; De Jong, P. J.; Stewart, A. F.; Bradley, A. (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
  11. ↑ Dolgin E (2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  12. ↑ Collins FS, Rossant J, Wurst W (2007). "A Mouse for All Reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
  13. ↑ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biol. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.

External links

Further reading

  • Zydowo MM (1994). "Regulatory effects of the lipid-cytosolic enzyme interaction: AMP deaminase". Acta Biochim. Pol. 40 (4): 429–32. PMID 8140814.
  • Yamada Y, Goto H, Ogasawara N (1992). "Cloning and nucleotide sequence of the cDNA encoding human erythrocyte-specific AMP deaminase". Biochim. Biophys. Acta. 1171 (1): 125–8. doi:10.1016/0167-4781(92)90153-Q. PMID 1420359.
  • Ogasawara N, Goto H, Yamada Y, et al. (1987). "Deficiency of AMP deaminase in erythrocytes". Hum. Genet. 75 (1): 15–8. doi:10.1007/BF00273831. PMID 3804327.
  • Yamada Y, Goto H, Murase T, Ogasawara N (1995). "Molecular basis for human erythrocyte AMP deaminase deficiency: screening for the major point mutation and identification of other mutations". Hum. Mol. Genet. 3 (12): 2243–5. doi:10.1093/hmg/3.12.2243. PMID 7881427.
  • Yamada Y, Goto H, Ogasawara N (1994). "A point mutation responsible for human erythrocyte AMP deaminase deficiency". Hum. Mol. Genet. 3 (2): 331–4. doi:10.1093/hmg/3.2.331. PMID 8004104.
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