ACP2: Difference between revisions

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Latest revision as of 19:14, 8 November 2017

Lysosomal acid phosphatase is an enzyme that in humans is encoded by the ACP2 gene.^[1]^[2]

Lysosomal acid phosphatase is composed of two subunits, alpha and beta, and is chemically and genetically distinct from red cell acid phosphatase. Lysosomal acid phosphatase 2 is a member of a family of distinct isoenzymes which hydrolyze orthophosphoric monoesters to alcohol and phosphate. Acid phosphatase deficiency is caused by mutations in the ACP2 (beta subunit) and ACP3 (alpha subunit) genes.^[2]

References

↑ Shows TB, Brown JA, Lalley PA (Dec 1976). "Assignment and linear order of human acid phosphatase-2, esterase A4, and lactate dehydrogenase A genes on chromosome 11". Cytogenet Cell Genet. 16 (1–5): 231–4. doi:10.1159/000130598. PMID 975882.
↑ ^2.0 ^2.1 "Entrez Gene: ACP2 acid phosphatase 2, lysosomal".

External links

Human ACP2 genome location and ACP2 gene details page in the UCSC Genome Browser.

Moss DW, Raymond FD, Wile DB (1995). "Clinical and biological aspects of acid phosphatase". Critical reviews in clinical laboratory sciences. 32 (4): 431–67. doi:10.3109/10408369509084690. PMID 7576159.
Gierek T, Lisiewicz T, Pilch J (1977). "Intracellular enzymatic response of lymphocytes and neutrophils in patients with cancer of the larynx". Folia Haematol. Int. Mag. Klin. Morphol. Blutforsch. 104 (2): 208–15. PMID 69583.
Jones C, Kao FT (1979). "Regional mapping of the gene for human lysosomal acid phosphatase (ACP2) using a hybrid clone panel containing segments of human chromosome 11". Hum. Genet. 45 (1): 1–10. doi:10.1007/BF00277567. PMID 730175.
Geier C, von Figura K, Pohlmann R (1989). "Structure of the human lysosomal acid phosphatase gene". Eur. J. Biochem. 183 (3): 611–6. doi:10.1111/j.1432-1033.1989.tb21090.x. PMID 2776754.
Lemansky P, Gieselmann V, Hasilik A, von Figura K (1985). "Synthesis and transport of lysosomal acid phosphatase in normal and I-cell fibroblasts". J. Biol. Chem. 260 (15): 9023–30. PMID 3160696.
Pohlmann R, Krentler C, Schmidt B, et al. (1989). "Human lysosomal acid phosphatase: cloning, expression and chromosomal assignment". EMBO J. 7 (8): 2343–50. PMC 457099. PMID 3191910.
Waheed A, Van Etten RL (1985). "Biosynthesis and processing of lysosomal acid phosphatase in cultured human cells". Arch. Biochem. Biophys. 243 (1): 274–83. doi:10.1016/0003-9861(85)90796-9. PMID 3904632.
Nadler HL, Egan TJ (1970). "Deficiency of lysosomal acid phosphatase. A new familial metabolic disorder". N. Engl. J. Med. 282 (6): 302–7. doi:10.1056/NEJM197002052820604. PMID 5410815.
Bass DA, Lewis JC, Szejda P, et al. (1981). "Activation of lysosomal acid phosphatase of eosinophil leukocytes". Lab. Invest. 44 (5): 403–9. PMID 6164873.
Chappard D, Alexandre C, Riffat G (1983). "Histochemical identification of osteoclasts. Review of current methods and reappraisal of a simple procedure for routine diagnosis on undecalcified human iliac bone biopsies". Basic and Applied Histochemistry. 27 (2): 75–85. PMID 6193776.
Moszczyński P, Lisiewicz J (1984). "Beta-glucuronidase of lymphocytes in ontogenetic development of man". Arch. Immunol. Ther. Exp. (Warsz.). 31 (2): 171–6. PMID 6651479.
Radzun HJ, Parwaresch MR (1981). "Isoelectric focusing pattern of acid phosphatase and acid esterase in human blood cells, including thymocytes, T lymphocytes, and B lymphocytes". Exp. Hematol. 8 (6): 737–41. PMID 6970673.
Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
Whitelock RB, Fukuchi T, Zhou L, et al. (1997). "Cathepsin G, acid phosphatase, and alpha 1-proteinase inhibitor messenger RNA levels in keratoconus corneas". Invest. Ophthalmol. Vis. Sci. 38 (2): 529–34. PMID 9040486.
Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
Obermüller S, Kiecke C, von Figura K, Höning S (2002). "The tyrosine motifs of Lamp 1 and LAP determine their direct and indirect targeting to lysosomes". J. Cell Sci. 115 (Pt 1): 185–94. PMID 11801736.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.

This article on a gene on human chromosome 11 is a stub. You can help Wikipedia by expanding it.

[pmid975882-1] Shows TB, Brown JA, Lalley PA (Dec 1976). "Assignment and linear order of human acid phosphatase-2, esterase A4, and lactate dehydrogenase A genes on chromosome 11". Cytogenet Cell Genet. 16 (1–5): 231–4. doi:10.1159/000130598. PMID 975882.

[entrez-2] 2.0 ^2.1 "Entrez Gene: ACP2 acid phosphatase 2, lysosomal".

[1]

[2]

@@ Line 1: / Line 1: @@
+{{Infobox_gene}}
+'''Lysosomal acid phosphatase''' is an [[enzyme]] that in humans is encoded by the ''ACP2'' [[gene]].<ref name="pmid975882">{{cite journal | vauthors = Shows TB, Brown JA, Lalley PA | title = Assignment and linear order of human acid phosphatase-2, esterase A4, and lactate dehydrogenase A genes on chromosome 11 | journal = Cytogenet Cell Genet | volume = 16 | issue = 1-5 | pages = 231–4 |date=Dec 1976 | pmid = 975882 | pmc =  | doi =10.1159/000130598  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ACP2 acid phosphatase 2, lysosomal| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=53| accessdate = }}</ref>
+'''Lysosomal [[acid phosphatase]]''' is composed of two subunits, alpha and beta, and is chemically and genetically distinct from [[red cell acid phosphatase]]. Lysosomal acid phosphatase 2 is a member of a family of distinct isoenzymes which hydrolyze [[orthophosphoric monoester]]s to [[alcohol]] and [[phosphate]]. [[Acid phosphatase deficiency]] is caused by [[mutation]]s in the ACP2 (beta subunit) and [[ACP3]] (alpha subunit) genes.<ref name="entrez"/>
+==References==
+{{reflist}}
+==External links==
+* {{UCSC gene info|ACP2}}
+==Further reading==
+{{refbegin | 2}}
+{{PBB_Further_reading
+| citations =
+*{{cite journal  | vauthors=Moss DW, Raymond FD, Wile DB |title=Clinical and biological aspects of acid phosphatase. |journal=Critical reviews in clinical laboratory sciences |volume=32 |issue= 4 |pages= 431–67 |year= 1995 |pmid= 7576159 |doi=10.3109/10408369509084690  }}
+*{{cite journal  | vauthors=Gierek T, Lisiewicz T, Pilch J |title=Intracellular enzymatic response of lymphocytes and neutrophils in patients with cancer of the larynx. |journal=Folia Haematol. Int. Mag. Klin. Morphol. Blutforsch. |volume=104 |issue= 2 |pages= 208–15 |year= 1977 |pmid= 69583 |doi=  }}
+*{{cite journal  | vauthors=Jones C, Kao FT |title=Regional mapping of the gene for human lysosomal acid phosphatase (ACP2) using a hybrid clone panel containing segments of human chromosome 11. |journal=Hum. Genet. |volume=45 |issue= 1 |pages= 1–10 |year= 1979 |pmid= 730175 |doi=10.1007/BF00277567  }}
+*{{cite journal  | vauthors=Geier C, von Figura K, Pohlmann R |title=Structure of the human lysosomal acid phosphatase gene. |journal=Eur. J. Biochem. |volume=183 |issue= 3 |pages= 611–6 |year= 1989 |pmid= 2776754 |doi=10.1111/j.1432-1033.1989.tb21090.x  }}
+*{{cite journal  | vauthors=Lemansky P, Gieselmann V, Hasilik A, von Figura K |title=Synthesis and transport of lysosomal acid phosphatase in normal and I-cell fibroblasts. |journal=J. Biol. Chem. |volume=260 |issue= 15 |pages= 9023–30 |year= 1985 |pmid= 3160696 |doi=  }}
+*{{cite journal  | vauthors=Pohlmann R, Krentler C, Schmidt B |title=Human lysosomal acid phosphatase: cloning, expression and chromosomal assignment. |journal=EMBO J. |volume=7 |issue= 8 |pages= 2343–50 |year= 1989 |pmid= 3191910 |doi=  | pmc=457099  |display-authors=etal}}
+*{{cite journal  | vauthors=Waheed A, Van Etten RL |title=Biosynthesis and processing of lysosomal acid phosphatase in cultured human cells. |journal=Arch. Biochem. Biophys. |volume=243 |issue= 1 |pages= 274–83 |year= 1985 |pmid= 3904632 |doi=10.1016/0003-9861(85)90796-9  }}
+*{{cite journal  | vauthors=Nadler HL, Egan TJ |title=Deficiency of lysosomal acid phosphatase. A new familial metabolic disorder. |journal=N. Engl. J. Med. |volume=282 |issue= 6 |pages= 302–7 |year= 1970 |pmid= 5410815 |doi=10.1056/NEJM197002052820604  }}
+*{{cite journal  | vauthors=Bass DA, Lewis JC, Szejda P |title=Activation of lysosomal acid phosphatase of eosinophil leukocytes. |journal=Lab. Invest. |volume=44 |issue= 5 |pages= 403–9 |year= 1981 |pmid= 6164873 |doi=  |display-authors=etal}}
+*{{cite journal  | vauthors=Chappard D, Alexandre C, Riffat G |title=Histochemical identification of osteoclasts. Review of current methods and reappraisal of a simple procedure for routine diagnosis on undecalcified human iliac bone biopsies. |journal=Basic and Applied Histochemistry |volume=27 |issue= 2 |pages= 75–85 |year= 1983 |pmid= 6193776 |doi=  }}
+*{{cite journal  | vauthors=Moszczyński P, Lisiewicz J |title=Beta-glucuronidase of lymphocytes in ontogenetic development of man. |journal=Arch. Immunol. Ther. Exp. (Warsz.) |volume=31 |issue= 2 |pages= 171–6 |year= 1984 |pmid= 6651479 |doi=  }}
+*{{cite journal  | vauthors=Radzun HJ, Parwaresch MR |title=Isoelectric focusing pattern of acid phosphatase and acid esterase in human blood cells, including thymocytes, T lymphocytes, and B lymphocytes. |journal=Exp. Hematol. |volume=8 |issue= 6 |pages= 737–41 |year= 1981 |pmid= 6970673 |doi=  }}
+*{{cite journal  | vauthors=Andersson B, Wentland MA, Ricafrente JY |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107–13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 |display-authors=etal}}
+*{{cite journal  | vauthors=Whitelock RB, Fukuchi T, Zhou L |title=Cathepsin G, acid phosphatase, and alpha 1-proteinase inhibitor messenger RNA levels in keratoconus corneas. |journal=Invest. Ophthalmol. Vis. Sci. |volume=38 |issue= 2 |pages= 529–34 |year= 1997 |pmid= 9040486 |doi=  |display-authors=etal}}
+*{{cite journal  | vauthors=Yu W, Andersson B, Worley KC |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353–8 |year= 1997 |pmid= 9110174 |doi=  10.1101/gr.7.4.353| pmc=139146  |display-authors=etal}}
+*{{cite journal  | vauthors=Obermüller S, Kiecke C, von Figura K, Höning S |title=The tyrosine motifs of Lamp 1 and LAP determine their direct and indirect targeting to lysosomes. |journal=J. Cell Sci. |volume=115 |issue= Pt 1 |pages= 185–94 |year= 2002 |pmid= 11801736 |doi=  }}
+*{{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  | vauthors=Gerhard DS, Wagner L, Feingold EA |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  | pmc=528928 |display-authors=etal}}
+}}
+{{refend}}
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+| update_summary = no
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-<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
+[[Category:Human proteins]]
-{{GNF_Protein_box
- | image =
- | image_source =
- | PDB =
- | Name = Acid phosphatase 2, lysosomal
- | HGNCid = 123
- | Symbol = ACP2
- | AltSymbols =;
- | OMIM = 171650
- | ECnumber =
- | Homologene = 1217
- | MGIid = 87882
- | GeneAtlas_image1 = PBB_GE_ACP2_202767_at_tn.png
- | Function = {{GNF_GO|id=GO:0003993 |text = acid phosphatase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
- | Component = {{GNF_GO|id=GO:0005765 |text = lysosomal membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
- | Process = {{GNF_GO|id=GO:0001501 |text = skeletal development}} {{GNF_GO|id=GO:0007040 |text = lysosome organization and biogenesis}}
- | Orthologs = {{GNF_Ortholog_box
-    | Hs_EntrezGene = 53
-    | Hs_Ensembl = ENSG00000134575
-    | Hs_RefseqProtein = NP_001601
-    | Hs_RefseqmRNA = NM_001610
-    | Hs_GenLoc_db =
-    | Hs_GenLoc_chr = 11
-    | Hs_GenLoc_start = 47217429
-    | Hs_GenLoc_end = 47226939
-    | Hs_Uniprot = P11117
-    | Mm_EntrezGene = 11432
-    | Mm_Ensembl = ENSMUSG00000002103
-    | Mm_RefseqmRNA = NM_007387
-    | Mm_RefseqProtein = NP_031413
-    | Mm_GenLoc_db =
-    | Mm_GenLoc_chr = 2
-    | Mm_GenLoc_start = 91003758
-    | Mm_GenLoc_end = 91013613
-    | Mm_Uniprot = Q3U4F3
-  }}
-}}
-'''Acid phosphatase 2, lysosomal''', also known as '''ACP2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ACP2 acid phosphatase 2, lysosomal| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=53| accessdate = }}</ref>
-<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
-{{PBB_Summary
-| section_title =
-| summary_text = Lysosomal acid phosphatase is comprised of two subunits, alpha and beta, and is chemically and genetically distinct from red cell acid phosphatase. Lysosomal acid phosphatase 2 is a member of a family of distinct isoenzymes which hydrolyze orthophosphoric monoesters to alcohol and phosphate. Acid phosphatase deficiency is caused by mutations in the ACP2 (beta subunit) and ACP3 (alpha subunit) genes.<ref name="entrez">{{cite web | title = Entrez Gene: ACP2 acid phosphatase 2, lysosomal| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=53| accessdate = }}</ref>
-}}
-==References==
-{{reflist|2}}
-==Further reading==
-{{refbegin | 2}}
-{{PBB_Further_reading
-| citations =
-*{{cite journal  | author=Moss DW, Raymond FD, Wile DB |title=Clinical and biological aspects of acid phosphatase. |journal=Critical reviews in clinical laboratory sciences |volume=32 |issue= 4 |pages= 431-67 |year= 1995 |pmid= 7576159 |doi=  }}
-*{{cite journal  | author=Gierek T, Lisiewicz T, Pilch J |title=Intracellular enzymatic response of lymphocytes and neutrophils in patients with cancer of the larynx. |journal=Folia Haematol. Int. Mag. Klin. Morphol. Blutforsch. |volume=104 |issue= 2 |pages= 208-15 |year= 1977 |pmid= 69583 |doi=  }}
-*{{cite journal  | author=Jones C, Kao FT |title=Regional mapping of the gene for human lysosomal acid phosphatase (ACP2) using a hybrid clone panel containing segments of human chromosome 11. |journal=Hum. Genet. |volume=45 |issue= 1 |pages= 1-10 |year= 1979 |pmid= 730175 |doi=  }}
-*{{cite journal  | author=Shows TB, Brown JA, Lalley PA |title=Assignment and linear order of human acid phosphatase-2, esterase A4, and lactate dehydrogenase A genes on chromosome 11. |journal=Cytogenet. Cell Genet. |volume=16 |issue= 1-5 |pages= 231-4 |year= 1976 |pmid= 975882 |doi=  }}
-*{{cite journal  | author=Geier C, von Figura K, Pohlmann R |title=Structure of the human lysosomal acid phosphatase gene. |journal=Eur. J. Biochem. |volume=183 |issue= 3 |pages= 611-6 |year= 1989 |pmid= 2776754 |doi=  }}
-*{{cite journal  | author=Lemansky P, Gieselmann V, Hasilik A, von Figura K |title=Synthesis and transport of lysosomal acid phosphatase in normal and I-cell fibroblasts. |journal=J. Biol. Chem. |volume=260 |issue= 15 |pages= 9023-30 |year= 1985 |pmid= 3160696 |doi=  }}
-*{{cite journal  | author=Pohlmann R, Krentler C, Schmidt B, ''et al.'' |title=Human lysosomal acid phosphatase: cloning, expression and chromosomal assignment. |journal=EMBO J. |volume=7 |issue= 8 |pages= 2343-50 |year= 1989 |pmid= 3191910 |doi=  }}
-*{{cite journal  | author=Waheed A, Van Etten RL |title=Biosynthesis and processing of lysosomal acid phosphatase in cultured human cells. |journal=Arch. Biochem. Biophys. |volume=243 |issue= 1 |pages= 274-83 |year= 1985 |pmid= 3904632 |doi=  }}
-*{{cite journal  | author=Nadler HL, Egan TJ |title=Deficiency of lysosomal acid phosphatase. A new familial metabolic disorder. |journal=N. Engl. J. Med. |volume=282 |issue= 6 |pages= 302-7 |year= 1970 |pmid= 5410815 |doi=  }}
-*{{cite journal  | author=Bass DA, Lewis JC, Szejda P, ''et al.'' |title=Activation of lysosomal acid phosphatase of eosinophil leukocytes. |journal=Lab. Invest. |volume=44 |issue= 5 |pages= 403-9 |year= 1981 |pmid= 6164873 |doi=  }}
-*{{cite journal  | author=Chappard D, Alexandre C, Riffat G |title=Histochemical identification of osteoclasts. Review of current methods and reappraisal of a simple procedure for routine diagnosis on undecalcified human iliac bone biopsies. |journal=Basic and applied histochemistry |volume=27 |issue= 2 |pages= 75-85 |year= 1983 |pmid= 6193776 |doi=  }}
-*{{cite journal  | author=Moszczyński P, Lisiewicz J |title=Beta-glucuronidase of lymphocytes in ontogenetic development of man. |journal=Arch. Immunol. Ther. Exp. (Warsz.) |volume=31 |issue= 2 |pages= 171-6 |year= 1984 |pmid= 6651479 |doi=  }}
-*{{cite journal  | author=Radzun HJ, Parwaresch MR |title=Isoelectric focusing pattern of acid phosphatase and acid esterase in human blood cells, including thymocytes, T lymphocytes, and B lymphocytes. |journal=Exp. Hematol. |volume=8 |issue= 6 |pages= 737-41 |year= 1981 |pmid= 6970673 |doi=  }}
-*{{cite journal  | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107-13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
-*{{cite journal  | author=Whitelock RB, Fukuchi T, Zhou L, ''et al.'' |title=Cathepsin G, acid phosphatase, and alpha 1-proteinase inhibitor messenger RNA levels in keratoconus corneas. |journal=Invest. Ophthalmol. Vis. Sci. |volume=38 |issue= 2 |pages= 529-34 |year= 1997 |pmid= 9040486 |doi=  }}
-*{{cite journal  | author=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353-8 |year= 1997 |pmid= 9110174 |doi=  }}
-*{{cite journal  | author=Obermüller S, Kiecke C, von Figura K, Höning S |title=The tyrosine motifs of Lamp 1 and LAP determine their direct and indirect targetting to lysosomes. |journal=J. Cell. Sci. |volume=115 |issue= Pt 1 |pages= 185-94 |year= 2002 |pmid= 11801736 |doi=  }}
-*{{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  | 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 }}
-}}
-{{refend}}
-{{protein-stub}}
+{{gene-11-stub}}
-{{WikiDoc Sources}}

ACP2: Difference between revisions

Latest revision as of 19:14, 8 November 2017

References

External links

Further reading

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