Molecular cloning and sequence analysis of cDNA encoding human ferrochelatase.Nakahashi Y., Taketani S., Okuda M., Inoue K., Tokunaga R.View abstractCited forNUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLN-96CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCBiochem. Biophys. Res. Commun. 173:748-755 (1990)Cited in1
Ferrochelatase: complete human gene sequence, amplifiable polymorphisms and molecular study of 12 families with erythropoietic protoporphyria.Gouya L.M., Martin C., Deybach J.-C., Puy H.V.Cited forNUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-96CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)Submission Submitted to EMBL/GenBank/DDBJ databases (OCT-1999)Cited in1
Cloning of human full-length CDSs in BD Creator(TM) system donor vector.Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D.[...], Farmer A.Cited forNUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)Submission Submitted to EMBL/GenBank/DDBJ databases (OCT-2004)Cited in99+
Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H.[...], Sugano S.View abstractCited forNUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2)TissuePlacenta, TracheaCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNat. Genet. 36:40-45 (2004)Cited in99+99+
No title available.Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H.[...], Venter J.C.Cited forNUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)Submission Submitted to EMBL/GenBank/DDBJ databases (JUL-2005)Cited in99+
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).The MGC Project TeamView abstractCited forNUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)TissueTestisCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCGenome Res. 14:2121-2127 (2004)Cited in99+99+
A single promoter directs both housekeeping and erythroid preferential expression of the human ferrochelatase gene.Tugores A., Magness S.T., Brenner D.A.View abstractCited forNUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 269:30789-30797 (1994)Cited in1
Molecular analysis of ferrochelatase gene in erythropoietic protoporphyria.Di Pierro E., Martinez di Montemuros F., Moriondo V., Cappellini M.D.Cited forNUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)Submission Submitted to EMBL/GenBank/DDBJ databases (MAR-2002)Cited in11
Mammalian ferrochelatase. Expression and characterization of normal and two human protoporphyric ferrochelatases.Dailey H.A., Sellers V.M., Dailey T.A.View abstractCited forCHARACTERIZATION, MUTAGENESIS, FUNCTION, CATALYTIC ACTIVITY, COFACTORCategoriesFunction, Disease & VariantsSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 269:390-395 (1994)Cited in2
Site-directed mutagenesis and spectroscopic characterization of human ferrochelatase: identification of residues coordinating the [2Fe-2S] cluster.Crouse B.R., Sellers V.M., Finnegan M.G., Dailey H.A., Johnson M.K.View abstractCited forIDENTIFICATION OF CYSTEINES COORDINATING THE 2FE-2S CLUSTERSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCBiochemistry 35:16222-16229 (1996)Cited in1Mapped to13
Evidence that the fourth ligand to the 2Fe-2S cluster in animal ferrochelatase is a cysteine. Characterization of the enzyme from Drosophila melanogaster.Sellers V.M., Wang K.-F., Johnson M.K., Dailey H.A.View abstractCited forIDENTIFICATION OF CYSTEINES COORDINATING THE 2FE-2S CLUSTERSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 273:22311-22316 (1998)Cited in2
Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.View abstractCited forIDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCBMC Syst. Biol. 5:17-17 (2011)Cited in99+99+
An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.View abstractCited forIDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]TissueLiverCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Proteomics 96:253-262 (2014)Cited in99+99+Mapped to2
N-terminome analysis of the human mitochondrial proteome.Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.View abstractCited forIDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCProteomics 15:2519-2524 (2015)Cited in99+99+
A Novel Role for Progesterone Receptor Membrane Component 1 (PGRMC1): A Partner and Regulator of Ferrochelatase.Piel R.B. III, Shiferaw M.T., Vashisht A.A., Marcero J.R., Praissman J.L., Phillips J.D., Wohlschlegel J.A., Medlock A.E.View abstractCited forFUNCTION, INTERACTION WITH PGRMC1, MUTAGENESIS OF PHE-110, CATALYTIC ACTIVITYCategoriesFunction, Disease & Variants, InteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCBiochemistry 55:5204-5217 (2016)Cited in4Mapped to16
Dimeric ferrochelatase bridges ABCB7 and ABCB10 homodimers in an architecturally defined molecular complex required for heme biosynthesis.Maio N., Kim K.S., Holmes-Hampton G., Singh A., Rouault T.A.View abstractCited forINTERACTION WITH ABCB7 AND ABCB10, SUBUNITCategoriesInteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCHaematologica 104:1756-1767 (2019)Cited in6Mapped to22
The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis.Wu C.-K., Dailey H.A., Rose J.P., Burden A., Sellers V.M., Wang B.-C.View abstractCited forX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)CategoriesStructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNat. Struct. Biol. 8:156-160 (2001)Cited in1
Substrate interactions with human ferrochelatase.Medlock A., Swartz L., Dailey T.A., Dailey H.A., Lanzilotta W.N.View abstractCited forX-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 65-423 ALONE AND IN COMPLEX WITH PROTOPORPHYRIN IX, SUBUNIT, IRON-SULFUR CLUSTERCategoriesInteraction, StructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCProc. Natl. Acad. Sci. U.S.A. 104:1789-1793 (2007)Cited in1Mapped to5
Erythropoietic protoporphyria.Cox T.M.View abstractCited forREVIEW ON VARIANTS EPP1CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Inherit. Metab. Dis. 20:258-269 (1997)Cited in1
Human erythropoietic protoporphyria: two point mutations in the ferrochelatase gene.Lamoril J., Boulechfar S., de Verneuil H., Grandchamp B., Nordmann Y., Deybach J.-C.View abstractCited forVARIANTS EPP1 CYS-55 AND ILE-267CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCBiochem. Biophys. Res. Commun. 181:594-599 (1991)Cited in1
A molecular defect in human protoporphyria.Brenner D.A., Didier J.M., Frasier F., Christensen S.R., Evans G.A., Dailey H.A.View abstractCited forVARIANT EPP1 SER-417CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCAm. J. Hum. Genet. 50:1203-1210 (1992)Cited in1
Recessive inheritance of erythropoietic protoporphyria with liver failure.Sarkany R.P.E., Alexander G.J.M.A., Cox T.M.View abstractCited forVARIANT EPP1 GLY-362CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCLancet 343:1394-1396 (1994)Cited in1
A novel mutation in the ferrochelatase gene associated with erythropoietic protoporphyria.Imoto S., Tanizawa Y., Sata Y., Kaku K., Oka Y.View abstractCited forVARIANT EPP1 THR-186CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCBr. J. Haematol. 94:191-197 (1996)Cited in1
Systematic analysis of molecular defects in the ferrochelatase gene from patients with erythropoietic protoporphyria.Ruefenacht U.B., Gouya L., Schneider-Yin X., Puy H., Schaefer B.W., Aquaron R., Nordmann Y., Minder E.I., Deybach J.-C.View abstractCited forVARIANTS EPP1 LYS-71; PRO-151; HIS-191; THR-192; ILE-283; LYS-288; LEU-334 AND PHE-417 DEL, CHARACTERIZATION OF VARIANTS EPP1 LYS-71; PRO-151; HIS-191; THR-192; ILE-283; LYS-288; LEU-334 AND PHE-417 DELCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCAm. J. Hum. Genet. 62:1341-1352 (1998)Cited in1
Mutations in the ferrochelatase gene of four Spanish patients with erythropoietic protoporphyria.Gouya L., Schneider-Yin X., Rufenacht U., Herrero C., Lecha M., Mascaro J.M., Puy H., Deybach J.-C., Minder E.I.View abstractCited forVARIANT EPP1 PRO-386CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Invest. Dermatol. 111:406-409 (1998)Cited in1