[1]
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NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT RD TRP-275.
DOI=10.1038/ng1097-185; PubMed=9326939 [NCBI, ExPASy, EBI, Israel, Japan]
Mihalik S.J.,
Morrell J.C.,
Kim D.,
Sachsteder K.A.,
Watkins P.A.,
Gould S.J.;
"Identification of PAHX, a Refsum disease gene.";
Nat. Genet. 17:185-189(1997).
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[2]
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NUCLEOTIDE SEQUENCE, AND VARIANT RD HIS-269.
DOI=10.1038/ng1097-190; PubMed=9326940 [NCBI, ExPASy, EBI, Israel, Japan]
Jansen G.A.,
Ofman R.,
Ferdinandusse S.,
Ijlst L.,
Muijsers A.O.,
Skjeldal O.H.,
Stokke O.,
Jakobs C.,
Besley G.T.N.,
Wraith J.E.,
Wanders R.J.A.;
"Refsum disease is caused by mutations in the phytanoyl-CoA hydroxylase gene.";
Nat. Genet. 17:190-193(1997).
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[3]
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NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Leukemia;
DOI=10.1073/pnas.96.5.2104; PubMed=10051602 [NCBI, ExPASy, EBI, Israel, Japan]
Chambraud B.,
Radanyi C.,
Camonis J.H.,
Rajkowski K.,
Schumacher M.,
Baulieu E.-E.;
"Immunophilins, Refsum disease, and lupus nephritis: the peroxisomal enzyme phytanoyl-CoA alpha-hydroxylase is a new FKBP-associated protein.";
Proc. Natl. Acad. Sci. U.S.A. 96:2104-2109(1999).
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[4]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS RD SER-29; SER-173; LYS-176; GLY-177; ALA-192 INS; ARG-193; GLN-197; PHE-199; SER-204; TYR-220; GLN-245; SER-257; HIS-269; GLN-275 AND TRP-275.
DOI=10.1093/hmg/9.8.1195; PubMed=10767344 [NCBI, ExPASy, EBI, Israel, Japan]
Jansen G.A.,
Hogenhout E.M.,
Ferdinandusse S.,
Waterham H.R.,
Ofman R.,
Jakobs C.,
Skjeldal O.H.,
Wanders R.J.A.;
"Human phytanoyl-CoA hydroxylase: resolution of the gene structure and the molecular basis of Refsum's disease.";
Hum. Mol. Genet. 9:1195-1200(2000).
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[5]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02462; PubMed=15164054 [NCBI, ExPASy, EBI, Israel, Japan]
Deloukas P.,
Earthrowl M.E.,
Grafham D.V.,
Rubenfield M.,
French L.,
Steward C.A.,
Sims S.K.,
Jones M.C.,
Searle S.,
Scott C.,
Howe K.,
Hunt S.E.,
Andrews T.D.,
Gilbert J.G.R.,
Swarbreck D.,
Ashurst J.L.,
Taylor A.,
Battles J.,
Bird C.P., ![]()
Ainscough R.,
Almeida J.P.,
Ashwell R.I.S.,
Ambrose K.D.,
Babbage A.K.,
Bagguley C.L.,
Bailey J.,
Banerjee R.,
Bates K.,
Beasley H.,
Bray-Allen S.,
Brown A.J.,
Brown J.Y.,
Burford D.C.,
Burrill W.,
Burton J.,
Cahill P.,
Camire D.,
Carter N.P.,
Chapman J.C.,
Clark S.Y.,
Clarke G.,
Clee C.M.,
Clegg S.,
Corby N.,
Coulson A.,
Dhami P.,
Dutta I.,
Dunn M.,
Faulkner L.,
Frankish A.,
Frankland J.A.,
Garner P.,
Garnett J.,
Gribble S.,
Griffiths C.,
Grocock R.,
Gustafson E.,
Hammond S.,
Harley J.L.,
Hart E.,
Heath P.D.,
Ho T.P.,
Hopkins B.,
Horne J.,
Howden P.J.,
Huckle E.,
Hynds C.,
Johnson C.,
Johnson D.,
Kana A.,
Kay M.,
Kimberley A.M.,
Kershaw J.K.,
Kokkinaki M.,
Laird G.K.,
Lawlor S.,
Lee H.M.,
Leongamornlert D.A.,
Laird G.,
Lloyd C.,
Lloyd D.M.,
Loveland J.,
Lovell J.,
McLaren S.,
McLay K.E.,
McMurray A.,
Mashreghi-Mohammadi M.,
Matthews L.,
Milne S.,
Nickerson T.,
Nguyen M.,
Overton-Larty E.,
Palmer S.A.,
Pearce A.V.,
Peck A.I.,
Pelan S.,
Phillimore B.,
Porter K.,
Rice C.M.,
Rogosin A.,
Ross M.T.,
Sarafidou T.,
Sehra H.K.,
Shownkeen R.,
Skuce C.D.,
Smith M.,
Standring L.,
Sycamore N.,
Tester J.,
Thorpe A.,
Torcasso W.,
Tracey A.,
Tromans A.,
Tsolas J.,
Wall M.,
Walsh J.,
Wang H.,
Weinstock K.,
West A.P.,
Willey D.L.,
Whitehead S.L.,
Wilming L.,
Wray P.W.,
Young L.,
Chen Y.,
Lovering R.C.,
Moschonas N.K.,
Siebert R.,
Fechtel K.,
Bentley D.,
Durbin R.M.,
Hubbard T.,
Doucette-Stamm L.,
Beck S.,
Smith D.R.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
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[6]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[7]
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INTERACTION WITH PHYHIP.
DOI=10.1016/S0169-328X(99)00304-6; PubMed=10686344 [NCBI, ExPASy, EBI, Israel, Japan]
Lee Z.H.,
Kim H.-H.,
Ahn K.Y.,
Seo K.H.,
Kim J.K.,
Bae C.S.,
Kim K.K.;
"Identification of a brain specific protein that associates with a Refsum disease gene product, phytanoyl-CoA alpha-hydroxylase.";
Brain Res. Mol. Brain Res. 75:237-247(2000).
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[8]
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X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 31-338 IN COMPLEX WITH IRON AND ALPHA-KETOGLUTARATE, AND COFACTOR.
DOI=10.1074/jbc.M507528200; PubMed=16186124 [NCBI, ExPASy, EBI, Israel, Japan]
McDonough M.A.,
Kavanagh K.L.,
Butler D.,
Searls T.,
Oppermann U.,
Schofield C.J.;
"Structure of human phytanoyl-CoA 2-hydroxylase identifies molecular mechanisms of Refsum disease.";
J. Biol. Chem. 280:41101-41110(2005).
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[9]
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REVIEW ON VARIANTS RD.
DOI=10.1002/humu.10315; PubMed=14974078 [NCBI, ExPASy, EBI, Israel, Japan]
Jansen G.A.,
Waterham H.R.,
Wanders R.J.A.;
"Molecular basis of Refsum disease: sequence variations in phytanoyl-CoA hydroxylase (PHYH) and the PTS2 receptor (PEX7).";
Hum. Mutat. 23:209-218(2004).
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[10]
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VARIANT RD SER-204.
PubMed=10709665 [NCBI, ExPASy, EBI, Israel, Japan]
Jansen G.A.,
Ferdinandusse S.,
Hogenhout E.M.,
Verhoeven N.M.,
Jakobs C.,
Wanders R.J.A.;
"Phytanoyl-CoA hydroxylase deficiency. Enzymological and molecular basis of classical Refsum disease.";
Adv. Exp. Med. Biol. 466:371-376(1999).
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