H. Dailey

发表

Ferrochelatase structural mutant (Fechm1Pas) in the house mouse.

J. Deybach, B. Grandchamp, X. Montagutelli, 1993, Genomics.

Identification of the Mitochondrial Heme Metabolism Complex

A. Vashisht, J. Wohlschlegel, J. Phillips, 2015, PloS one.

The mitochondrial heme metabolon: Insights into the complex(ity) of heme synthesis and distribution.

A. Medlock, H. Dailey, Robert B. Piel, 2019, Molecular genetics and metabolism.

Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product

S. Gerdes, D. Jahn, M. R. O'Brian, 2017, Microbiology and Molecular Biology Reviews.

A pi-helix switch selective for porphyrin deprotonation and product release in human ferrochelatase.

W. Lanzilotta, A. Medlock, H. Dailey, 2007, Journal of molecular biology.

Structural and functional properties of the membrane binding segment of cytochrome b5.

P. Strittmatter, H. Dailey, 1978, The Journal of biological chemistry.

Altered orientation of active site residues in variants of human ferrochelatase. Evidence for a hydrogen bond network involved in catalysis.

J. Rose, P. Horanyi, A. Medlock, 2007, Biochemistry.

The 2.0 Å structure of human ferrochelatase, the terminal enzyme of heme biosynthesis

J. Rose, Bi-Cheng Wang, H. Dailey, 2001, Nature Structural Biology.

Ferrochelatase at the millennium: structures, mechanisms and [2Fe-2S] clusters

J. Rose, B. Wang, A. Medlock, 2000, Cellular and Molecular Life Sciences CMLS.

Human ferrochelatase: crystallization, characterization of the [2Fe-2S] cluster and determination that the enzyme is a homodimer.

J. Rose, B. Wang, H. Dailey, 1999, Biochimica et biophysica acta.

Expression, purification, and characterization of recombinant mammalian ferrochelatase.

H. Dailey, V. M. Sellers, 1997, Methods in enzymology.

Regulation of heme biosynthesis in Escherichia coli.

H. Dailey, S. Woodard, Harry A. Dailey, 1995, Archives of biochemistry and biophysics.

Ferrochelatase: Mapping the Intersection of Iron and Porphyrin Metabolism in the Mitochondria

H. Dailey, C. D. Obi, Tawhid Bhuiyan, 2022, Frontiers in Cell and Developmental Biology.

Product release rather than chelation determines metal specificity for ferrochelatase.

W. Lanzilotta, A. Medlock, H. Dailey, 2009, Journal of molecular biology.

Disulfide-masked iron prochelators: Effects on cell death, proliferation, and hemoglobin production.

H. Dailey, E. Tomat, J. R. Marcero, 2018, Journal of inorganic biochemistry.

Identification of [2Fe-2S] Clusters in Microbial Ferrochelatases

H. Dailey, T. Dailey, 2002, Journal of bacteriology.

Characterization of the interaction of amphipathic cytochrome b5 with stearyl coenzyme A desaturase and NADPH:cytochrome P-450 reductase.

P. Strittmatter, H. Dailey, 1980, The Journal of biological chemistry.

Effect of sulfhydryl group modification on the activity of bovine ferrochelatase.

H. Dailey, 1984, The Journal of biological chemistry.

Discovery and Characterization of HemQ

S. Gerdes, H. Dailey, T. O. Boynton, 2010, The Journal of Biological Chemistry.

Multiple regulatory steps in erythroid heme biosynthesis.

H. Dailey, S. Woodard, 2000, Archives of biochemistry and biophysics.

Expression of human proteins at the Southeast Collaboratory for Structural Genomics

H. Dailey, M. Grady, T. Dailey, 2004, Journal of Structural and Functional Genomics.

The immunometabolite itaconate inhibits heme synthesis and remodels cellular metabolism in erythroid precursors

J. Phillips, A. Medlock, H. Dailey, 2021, Blood advances.

A primer on heme biosynthesis

H. Dailey, Amy E. Medlock, 2022, Biological chemistry.

Autosomal recessive erythropoietic protoporphyria in the United Kingdom: prevalence and relationship to liver disease

M. Badminton, G. Elder, H. Dailey, 2004, Journal of Medical Genetics.

Discovery of a Gene Involved in a Third Bacterial Protoporphyrinogen Oxidase Activity through Comparative Genomic Analysis and Functional Complementation

S. Gerdes, E. Neidle, J. Phillips, 2011, Applied and Environmental Microbiology.

A molecular defect in human protoporphyria.

D. Brenner, G. Evans, H. Dailey, 1992, American journal of human genetics.

Protoporphyrinogen Oxidase of Myxococcus xanthus

H. Dailey, T. Dailey, 1996, The Journal of Biological Chemistry.

Heme biosynthesis in mammalian systems: Evidence of a schiff base linkage between the pyridoxal 5′‐phosphate cofactor and a lysine residue in 5‐aminolevulinate synthase

G. C. Ferreira, H. Dailey, P. Neame, 1993, Protein science : a publication of the Protein Society.

Expression and characterization of the terminal heme synthetic enzymes from the hyperthermophile Aquifex aeolicus.

H. Dailey, T. Dailey, K. Wang, 2001, FEMS microbiology letters.

New Avenues of Heme Synthesis Regulation

A. Medlock, H. Dailey, 2022, International journal of molecular sciences.

Rapid and sensitive quantitation of heme in hemoglobinized cells.

H. Dailey, J. R. Marcero, Robert B. Piel III, 2016, BioTechniques.

Identification of Escherichia coli HemG as a novel, menadione-dependent flavodoxin with protoporphyrinogen oxidase activity.

H. Dailey, T. O. Boynton, T. Dailey, 2009, Biochemistry.

A continuous fluorimetric assay for protoporphyrinogen oxidase by monitoring porphyrin accumulation.

M. Shepherd, H. Dailey, 2005, Analytical biochemistry.

Production and characterization of erythropoietic protoporphyric heterodimeric ferrochelatases.

H. Dailey, Wided Najahi-Missaoui, 2005, Blood.

Purification of and Kinetic Studies on a Cloned Protoporphyrinogen Oxidase from the Aerobic BacteriumBacillus subtilis

A. Corrigall, P. Meissner, M. Ziman, 1998 .

Identification of an FAD Superfamily Containing Protoporphyrinogen Oxidases, Monoamine Oxidases, and Phytoene Desaturase

H. Dailey, T. Dailey, 1998, The Journal of Biological Chemistry.

Enzymes of heme biosynthesis

H. Dailey, 1997, JBIC Journal of Biological Inorganic Chemistry.

Human protoporphyrinogen oxidase: Expression, purification, and characterization of the cloned enzyme

H. Dailey, T. Dailey, 1996, Protein science : a publication of the Protein Society.

Cloning, sequence, and expression of mouse protoporphyrinogen oxidase.

P. Meissner, H. Dailey, T. Dailey, 1995, Archives of biochemistry and biophysics.

In situ conversion of coproporphyrinogen to heme by murine mitochondria: Terminal steps of the heme biosynthetic pathway

H. Dailey, S. Woodard, Karen L. Proulx, 1993, Protein science : a publication of the Protein Society.

Exogenously Scavenged and Endogenously Synthesized Heme Are Differentially Utilized by Mycobacterium tuberculosis

H. Yang, H. Dailey, P. Jain, 2022, Microbiology spectrum.

The terminal heme synthetic enzyme, Coproheme Decarboxylase, coordinates heme synthesis and uptake in response to iron in Mycobacteria

M. Niederweis, H. Yang, H. Dailey, 2021, bioRxiv.

Ferrochelatase forms an oligomeric complex with mitoferrin-1 and Abcb10 for erythroid heme biosynthesis.

B. Paw, H. Dailey, Wen Chen, 2010, Blood.

A new class of [2Fe-2S]-cluster-containing protoporphyrin (IX) ferrochelatases.

M. Shepherd, H. Dailey, T. Dailey, 2006, The Biochemical journal.

Purification of and kinetic studies on a cloned protoporphyrinogen oxidase from the aerobic bacterium Bacillus subtilis.

A. Corrigall, P. Meissner, M. Ziman, 1998, Archives of biochemistry and biophysics.

Expression of a cloned protoporphyrinogen oxidase.

P. Meissner, H. Dailey, T. Dailey, 1994, The Journal of biological chemistry.

Biosynthesis of heme and chlorophylls

H. Dailey, 1990 .

Ferrochelatase from Rhodopseudomonas sphaeroides: substrate specificity and role of sulfhydryl and arginyl residues

H. Dailey, J. Fleming, B. M. Harbin, 1986, Journal of bacteriology.

Ferric iron reductase of Rhodopseudomonas sphaeroides

H. Dailey, M. Moody, 1985, Journal of bacteriology.

Siderophore utilization and iron uptake by Rhodopseudomonas sphaeroides.

H. Dailey, M. Moody, 1984, Archives of biochemistry and biophysics.

Purification and characterization of membrane-bound ferrochelatase from Rhodopseudomonas sphaeroides.

H. Dailey, 1982, The Journal of biological chemistry.

Purification and characterization of the membrane-bound ferrochelatase from Spirillum itersonii

H. Dailey, 1977, Journal of bacteriology.

Ferrochelatase activity in wild-type and mutant strains of Spirillum itersonii. Solubilization with chaotropic reagents.

H. Dailey, J. Lascelles, 1974, Archives of biochemistry and biophysics.

A R59W mutation in human protoporphyrinogen oxidase results in decreased enzyme activity and is prevalent in South Africans with variegate porphyria

A. Corrigall, P. Meissner, M. Ziman, 1996, Nature Genetics.

Protein Production and Crystallization at SECSG – An Overview

Ashit K Shah, J. Rose, C. Luan, 2005, Journal of Structural and Functional Genomics.

Terminal steps of haem biosynthesis.

H. Dailey, 2001, Biochemical Society Transactions.

Interaction of free porphyrins and metalloporphyrins with mouse ferrochelatase. A model for the active site of ferrochelatase.

H. Dailey, C. S. Jones, S. Karr, 1989, Biochimica et biophysica acta.

Spectroscopic examination of the active site of bovine ferrochelatase.

H. Dailey, 1985, Biochemistry.

Evidence That the Fourth Ligand to the [2Fe-2S] Cluster in Animal Ferrochelatase Is a Cysteine

H. Dailey, Michael K. Johnson, V. M. Sellers, 1998, The Journal of Biological Chemistry.

Orientation of the carboxyl and NH2 termini of the membrane-binding segment of cytochrome b5 on the same side of phospholipid bilayers.

P. Strittmatter, H. Dailey, 1981, The Journal of biological chemistry.

The role of COOH-terminal anionic residues in binding cytochrome b5 to phospholipid vesicles and biological membranes.

P. Strittmatter, H. Dailey, 1981, The Journal of biological chemistry.

Identification and characterization of solvent-filled channels in human ferrochelatase.

W. Lanzilotta, A. Medlock, H. Dailey, 2012, Biochemistry.

Human Coproporphyrinogen Oxidase Is Not a Metalloprotein*

A. Medlock, H. Dailey, 1996, The Journal of Biological Chemistry.

Regulation of Mammalian Heme Biosynthesis

A. Medlock, H. Dailey, 2009 .

Biphasic ordered induction of heme synthesis in differentiating murine erythroleukemia cells: role of erythroid 5-aminolevulinate synthase

H. Dailey, H. Lake-Bullock, 1993, Molecular and cellular biology.

Crystal structure of the transcription factor sc‐mtTFB offers insights into mitochondrial transcription

J. Rose, B. Wang, H. Dailey, 2001, Protein science : a publication of the Protein Society.

Human ferrochelatase is an iron-sulfur protein.

H. Dailey, Michael K. Johnson, M. G. Finnegan, 1994, Biochemistry.

One ring to rule them all: trafficking of heme and heme synthesis intermediates in the metazoans.

I. Hamza, H. Dailey, 2012, Biochimica et biophysica acta.

Variegate porphyria in South Africa, 1688-1996--new developments in an old disease.

A. Corrigall, P. Meissner, M. Ziman, 1997, South African medical journal = Suid-Afrikaanse tydskrif vir geneeskunde.

Expression, purification, and characteristics of mammalian protoporphyrinogen oxidase.

H. Dailey, T. Dailey, 1997, Methods in enzymology.

Purification and characterization of murine protoporphyrinogen oxidase.

H. Dailey, S. Karr, 1987, Biochemistry.

Characteristics of murine protoporphyrinogen oxidase

H. Dailey, Karen L. Proulx, K. Proulx, 1992, Protein science : a publication of the Protein Society.

Mammalian ferrochelatase. Expression and characterization of normal and two human protoporphyric ferrochelatases.

H. Dailey, T. Dailey, V. M. Sellers, 1994, The Journal of biological chemistry.

The crystal structure of augmenter of liver regeneration: A mammalian FAD‐dependent sulfhydryl oxidase

J. Rose, H. Dailey, Chia-Kuei Wu, 2003, Protein science : a publication of the Protein Society.

Iron transport and its relation to heme biosynthesis in Rhodopseudomonas sphaeroides

H. Dailey, M. Moody, 1985, Journal of bacteriology.

Erythroid heme biosynthesis and its disorders.

P. Meissner, H. Dailey, 2013, Cold Spring Harbor perspectives in medicine.

The Molecular Basis of b-Thalassemia

D. Schaer, H. Dailey, C. Thom, 2013 .

Metal Inhibition of Ferrochelatase

H. Dailey, 1987, Annals of the New York Academy of Sciences.

Yeast ferrochelatase: Expression in a baculovirus system and purification of the expression protein

H. Dailey, M. Eldridge, 1992, Protein science : a publication of the Protein Society.

Reduction of iron and synthesis of protoheme by Spirillum itersonii and other organisms

H. Dailey, J. Lascelles, 1977, Journal of bacteriology.

A new mutation of the ALAS2 gene in a large family with X-linked sideroblastic anemia

B. Grandchamp, H. Dailey, J. Briere, 1995, Human Genetics.

sphaeroides.iron reductase of Rhodopseudomonas

H. Dailey, M. Moody, 2013 .

Ferric IronReductase ofRhodopseudomonas sphaeroides

H. Dailey, Mark D. MOODYt, 1985 .

[48] Purification and characterization of bacterial ferrochelatase

H. Dailey, 1986 .

Purification and characterization of mammalian and chicken ferrochelatase.

H. Dailey, J. Fleming, B. M. Harbin, 1986, Methods in enzymology.

Purification and characterization of chicken erythrocyte ferrochelatase.

H. Dailey, J. Hanson, 1984, The Biochemical journal.

Bovine ferrochelatase. Kinetic analysis of inhibition by N-methylprotoporphyrin, manganese, and heme.

H. Dailey, J. Fleming, 1983, The Journal of biological chemistry.

An Intercellular Heme-Trafficking Protein Delivers Maternal Heme to the Embryo during Development in C. elegans

I. Hamza, H. Dailey, Caiyong Chen, 2011, Cell.

Aerobic ferrisiderophore reductase assay and activity stain for native polyacrylamide gels.

H. Dailey, M. Moody, 1983, Analytical biochemistry.

Expression of mammalian 5-aminolevulinate synthase in Escherichia coli. Overproduction, purification, and characterization.

G. C. Ferreira, H. Dailey, 1993, The Journal of biological chemistry.

Erythropoietin signaling regulates heme biosynthesis

B. Paw, H. Lodish, S. Orkin, 2016, eLife.

Proteomic Analysis of Ferrochelatase Interactome in Erythroid and Non-Erythroid Cells

J. Wohlschlegel, H. Dailey, C. D. Obi, 2023, Life.

Iron Deficiency Anemia : A Common and Curable Disease

D. Schaer, H. Dailey, C. Thom, 2013 .

Mitochondrial contact site and cristae organizing system (MICOS) machinery supports heme biosynthesis by enabling optimal performance of ferrochelatase

J. Wohlschlegel, W. Lanzilotta, I. Bohovych, 2021, bioRxiv.

Heme Utilization in the Caenorhabditis elegans Hypodermal Cells Is Facilitated by Heme-responsive Gene-2*

M. Krause, I. Hamza, H. Dailey, 2012, The Journal of Biological Chemistry.

Substrate interactions with human ferrochelatase

W. Lanzilotta, A. Medlock, H. Dailey, 2007, Proceedings of the National Academy of Sciences.

Use of recombinant human ferrochelatase as a sensitive bioassay for N-alkylprotoporphyrin IX formed after interaction of porphyrinogenic xenobiotics with rat liver microsomes.

S. Wong, H. Dailey, G. S. Marks, 2000, Canadian journal of physiology and pharmacology.

N-Methylprotoporphyrin is a more potent inhibitor of recombinant human than of recombinant chicken ferrochelatase.

H. Dailey, G. S. Marks, J. T. Gamble, 2000, Drug metabolism and disposition: the biological fate of chemicals.

Cloning and characterization of Gallus and Xenopus ferrochelatases: presence of the [2Fe-2S] cluster in nonmammalian ferrochelatase.

H. Dailey, A. Day, B. Parsons, 1998, Archives of biochemistry and biophysics.

Function of the [2FE-2S] cluster in mammalian ferrochelatase: a possible role as a nitric oxide sensor.

H. Dailey, V. M. Sellers, M. Johnson, 1996, Biochemistry.

Organization of the terminal two enzymes of the heme biosynthetic pathway. Orientation of protoporphyrinogen oxidase and evidence for a membrane complex.

G. C. Ferreira, H. Dailey, T. Andrew, 1988, The Journal of biological chemistry.

TMEM14C is required for erythroid mitochondrial heme metabolism.

Jerry Kaplan, Harvey F Lodish, Daniel E Bauer, 2014, The Journal of clinical investigation.

Effect of Cellular Location on the Function of Ferrochelatase (*)

H. Dailey, A R Prasad, H A Dailey, 1995, The Journal of Biological Chemistry.

The Escherichia coli Protein YfeX Functions as a Porphyrinogen Oxidase, Not a Heme Dechelatase

S. Gerdes, J. Phillips, E. Stabb, 2011, mBio.

Mitochondrial Atpif1 Regulates Heme Synthesis in Developing Erythroblasts

B. Paw, B. Ebert, M. Fleming, 2011 .

Orientation of ferrochelatase in bovine liver mitochondria.

H. Dailey, B. M. Harbin, 1985, Biochemistry.

Molecular characterization of homozygous variegate porphyria.

J. Deybach, H. Puy, P. Martásek, 1998, Human molecular genetics.

heterodimeric ferrochelatases Production and characterization of erythropoietic protoporphyric

H. Dailey, Wided Najahi-Missaoui, 2010 .

Examination of Ferrochelatase Mutations That Cause Erythropoietic Protoporphyria

H. Dailey, T. Dailey, V. M. Sellers, 1998 .

Loss-of-Function Ferrochelatase and Gain-of-Function Erythroid-Specific 5-Aminolevulinate Synthase Mutations Causing Erythropoietic Protoporphyria and X-Linked Protoporphyria in North American Patients Reveal Novel Mutations and a High Prevalence of X-Linked Protoporphyria

H. Bonkovsky, R. Desnick, I. Nazarenko, 2013, Molecular Medicine.

Protoporphyria Examination of Ferrochelatase Mutations That Cause Erythropoietic

H. Dailey, T. Dailey, V. M. Sellers, 2013 .

Examination of ferrochelatase mutations that cause erythropoietic protoporphyria.

H. Dailey, T. Dailey, V. M. Sellers, 1998, Blood.

Human ferrochelatase: characterization of substrate-iron binding and proton-abstracting residues.

H. Dailey, Chia-Kuei Wu, T. Dailey, 2001, Biochemistry.

Loss of hepatocyte β-catenin protects mice from experimental porphyria-associated liver injury.

M. Omary, J. Locker, Sucha Singh, 2019, Journal of hepatology.

Inhibition of ferrochelatase during differentiation of murine erythroleukaemia cells.

H. Dailey, A. Fadigan, 1987, The Biochemical journal.

The primary structure of the nonpolar segment of bovine cytochrome b5.

P. Strittmatter, P. Fleming, H. Dailey, 1978, The Journal of biological chemistry.

Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway that does not use protoporphyrin

S. Gerdes, J. Phillips, H. Dailey, 2015, Proceedings of the National Academy of Sciences.

Glutamine via α-ketoglutarate dehydrogenase provides succinyl-CoA for heme synthesis during erythropoiesis.

J. Phillips, A. Medlock, H. Dailey, 2018, Blood.

Erythroid 5-aminolevulinate synthase is required for erythroid differentiation in mouse embryonic stem cells.

H. Dailey, X. Yin, Xiaohong Yin, 1998, Blood cells, molecules & diseases.

Insight into the Function of Active Site Residues in the Catalytic Mechanism of Human Ferrochelatase.

W. Lanzilotta, A. Medlock, H. Dailey, 2021, The Biochemical journal.

Characterization of a human and mouse tetrapyrrole-binding protein.

H. Dailey, T. Dailey, B. Jacob Blackmon, 2002, Archives of biochemistry and biophysics.

Modification and identification of cytochrome b5 carboxyl groups involved in protein-protein interaction with cytochrome b5 reductase.

P. Strittmatter, H. Dailey, 1979, The Journal of biological chemistry.

Generation of resistance to the diphenyl ether herbicide acifluorfen by MEL cells.

H. Dailey, A. R. Prasad, 1995, Biochemical and biophysical research communications.

Membrane-bound respiratory of Spirillum itersonii

H. Dailey, 1976, Journal of bacteriology.

The Southeast Collaboratory for Structural Genomics: a high-throughput gene to structure factory.

Ming Luo, John P Rose, Bi-Cheng Wang, 2003, Accounts of chemical research.

Purification, crystallization and preliminary X-ray analysis of Drosophila melanogaster ferrochelatase.

J. Rose, B. Wang, H. Dailey, 1999, Acta crystallographica. Section D, Biological crystallography.

Direct measurement of metal ion chelation in the active site of human ferrochelatase.

J. D. Reid, C. Hunter, H. Dailey, 2007, Biochemistry.

Differential interaction of porphyrins used in photoradiation therapy with ferrochelatase.

H. Dailey, H A Dailey, A Smith, 1984, The Biochemical journal.

The HemQ coprohaem decarboxylase generates reactive oxygen species: implications for the evolution of classical haem biosynthesis

M. Shepherd, H. Dailey, Charlie Hobbs, 2016, The Biochemical journal.

HemQ: An iron-coproporphyrin oxidative decarboxylase for protoheme synthesis in Firmicutes and Actinobacteria.

S. Gerdes, H. Dailey, 2015, Archives of biochemistry and biophysics.

Interdomain lateral gene transfer of an essential ferrochelatase gene in human parasitic nematodes

B. Slatko, J. Foster, Sanjay Kumar, 2013, Proceedings of the National Academy of Sciences.

Essential Structural Features and Orientation of Cytochrome b5 in Membranes

P. Strittmatter, H. Dailey, 1982 .

Illuminating the black box of B12 biosynthesis

H. Dailey, 2013, Proceedings of the National Academy of Sciences.

Antibacterial photosensitization through activation of coproporphyrinogen oxidase

J. L. Jenkins, Eric P. Skaar, Jeremy B. Ford, 2017, Proceedings of the National Academy of Sciences.

Ironing out the distribution of [2Fe-2S] motifs in ferrochelatases

A. Medlock, H. Dailey, R. S. Weerth, 2021, The Journal of biological chemistry.

Characteristics of human protoporphyrinogen oxidase in controls and variegate porphyrias.

H. Dailey, T. Dailey, 1997, Cellular and molecular biology.

A mouse model for South African (R59W) variegate porphyria: construction and initial characterization.

A. Corrigall, P. Meissner, A. Medlock, 2002, Cellular and molecular biology.

Multiple mechanisms for the regulation of haem synthesis during erythroid cell differentiation. Possible role for coproporphyrinogen oxidase.

H. Dailey, S. Woodard, L. Conder, 1991, The Biochemical journal.

Examination of the activity of carboxyl-terminal chimeric constructs of human and yeast ferrochelatases.

A. Medlock, H. Dailey, 2000, Biochemistry.

Corrigendum: Mitochondrial Atpif1 regulates haem synthesis in developing erythroblasts

B. Paw, B. Ebert, M. Fleming, 2013, Nature.

Production and characterization of erythropoietic protoporphyric heterodimeric ferrochelatases

H. Dailey, Wided Najahi-Missaoui, 2005 .

Author response: Erythropoietin signaling regulates heme biosynthesis

B. Paw, H. Lodish, S. Orkin, 2017 .

Proteomics - from protein sequence to function

H. Dailey, Harry A. Dailey, 2001, Human Genetics.

Human aminolevulinate synthase structure reveals a eukaryotic-specific autoinhibitory loop regulating substrate binding and product release

G. A. Bezerra, Gopalakrishnan Bulusu, R. Desnick, 2020, Nature Communications.

Heme Utilization in the Caenorhabditis elegans Hypodermal Cells Is Facilitated by Heme-responsive Gene-2*

M. Krause, I. Hamza, H. Dailey, 2012, The Journal of Biological Chemistry.

Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product

S. Gerdes, D. Jahn, M. R. O'Brian, 2017, Microbiology and Molecular Biology Reviews.

Exploiting Differences in Heme Biosynthesis between Bacterial Species to Screen for Novel Antimicrobials

H. Dailey, T. Dailey, H. Bergonia, 2023, Biomolecules.

reactive oxygen species: implications for the

M. Shepherd, H. Dailey, Charlie Hobbs, 2022 .

Antibacterial photosensitization through activation of coproporphyrinogen oxidase

J. L. Jenkins, Pedro L. Teixeira, Eric P. Skaar, 2017, Proceedings of the National Academy of Sciences.

Discovery of a Gene Involved in a Third Bacterial Protoporphyrinogen Oxidase Activity through Comparative Genomic Analysis and Functional Complementation

S. Gerdes, E. Neidle, J. Phillips, 2011, Applied and Environmental Microbiology.

Mitochondrial Atpif1 regulates heme synthesis in developing erythroblasts

B. Paw, N. Danial, H. Dailey, 2012, Nature.

A primer on heme biosynthesis

H. Dailey, Amy E. Medlock, 2022, Biological chemistry.

Examination of mitochondrial protein targeting of haem synthetic enzymes: in vivo identification of three functional haem-responsive motifs in 5-aminolaevulinate synthase.

H. Dailey, T. Dailey, J. Woodruff, 2005, The Biochemical journal.

Identification of E. coli HemG as a novel, menadione-dependent flavodoxin with protoporphyrinogen oxidase activity

H. Dailey, T. O. Boynton, T. Dailey, 2009 .