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Biology and Biochemistry

D-Index
60
Citations
9076
World Ranking
12220
National Ranking
5219

Research.com Recognitions

  • 2009 - Fellow of the American Association for the Advancement of Science (AAAS)

Overview

Harry A. Dailey is affiliated with the University of Georgia in the United States and has contributed extensively to the fields of biochemistry, genetics, and molecular biology, with a particular focus on heme biosynthesis and related metabolic processes.

The main research areas encompass porphyrin metabolism and disorders, heme oxygenase-1 and carbon monoxide, hemoglobin structure and function, folate and B vitamins research, neonatal health and biochemistry, iron metabolism and disorders, and metal-catalyzed oxygenation mechanisms.

Recent papers authored or coauthored by Dailey include:

  • "Ferrochelatase: Mapping the Intersection of Iron and Porphyrin Metabolism in the Mitochondria" (2022), published in Frontiers in Cell and Developmental Biology
  • "Human aminolevulinate synthase structure reveals a eukaryotic-specific autoinhibitory loop regulating substrate binding and product release" (2020), published in Nature Communications
  • "A primer on heme biosynthesis" (2022), published in Biological Chemistry
  • "Mitochondrial contact site and cristae organizing system (MICOS) machinery supports heme biosynthesis by enabling optimal performance of ferrochelatase" (2021), published in Redox Biology
  • "New Avenues of Heme Synthesis Regulation" (2022), published in International Journal of Molecular Sciences

Frequent coauthors associated with Dailey's research include:

  • Amy E. Medlock
  • Amit R. Reddi
  • Chibuike David
  • Robert B. Piel
  • William N. Lanzilotta

Publications have appeared in venues such as:

  • International Journal of Molecular Sciences
  • bioRxiv (Cold Spring Harbor Laboratory)
  • Frontiers in Cell and Developmental Biology
  • Nature Communications
  • Biological Chemistry

Dailey's work predominantly falls within the subfields of molecular biology, cell biology, rheumatology, pediatrics, perinatology and child health, and hematology. This interdisciplinary approach reflects the integration of molecular pathways and clinical aspects of related disorders.

In 2009, Harry A. Dailey was recognized as a Fellow of the American Association for the Advancement of Science (AAAS), an acknowledgment within the scientific community.

Best Publications

  • Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product.

    Harry A. Dailey;Tamara A. Dailey;Svetlana Gerdes;Dieter Jahn

  • Human ferrochelatase is an iron-sulfur protein.

    Harry A. Dailey;Michael G. Finnegan;Michael K. Johnson

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

    Chia-Kuei Wu;Harry A. Dailey;John P. Rose;Amy Burden

  • One ring to rule them all: Trafficking of heme and heme synthesis intermediates in the metazoans

    Iqbal Hamza;Harry A. Dailey

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

    Peter N. Meissner;Tamara A. Dailey;Richard J. Hift;Mel Ziman

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

    Wen Chen;Harry A. Dailey;Barry H. Paw

  • Function of the [2Fe−2S] Cluster in Mammalian Ferrochelatase: A Possible Role as a Nitric Oxide Sensor†

    Vera M. Sellers;Michael K. Johnson;Harry A. Dailey

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

    Harry A. Dailey;Svetlana Gerdes;Tamara A. Dailey;Joseph S. Burch

  • Terminal steps of haem biosynthesis.

    H. A. Dailey

  • HUMAN PROTOPORPHYRINOGEN OXIDASE : EXPRESSION, PURIFICATION, AND CHARACTERIZATION OF THE CLONED ENZYME

    Tamara A. Dailey;Harry A. Dailey

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

    G C Ferreira;T L Andrew;S W Karr;H A Dailey

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

    Chia-Kuei Wu;Tamara A. Dailey;Harry A. Dailey;Bi-Cheng Wang

  • Erythroid Heme Biosynthesis and Its Disorders

    Harry A. Dailey;Peter N. Meissner

  • Identification of the mitochondrial heme metabolism complex

    Amy E. Medlock;Mesafint T. Shiferaw;Jason R. Marcero;Ajay A. Vashisht

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

    Harry A. Dailey;Philipp Strittmatter

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

    Florian D. Schubot;Chun-Jung Chen;John P. Rose;Tamara A. Dailey

  • Regulation of heme biosynthesis in Escherichia coli.

    S.I. Woodard;H.A. Dailey

  • 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

    Manisha Balwani;Dana Doheny;David F. Bishop;Irina Nazarenko

  • Orientation of ferrochelatase in bovine liver mitochondria.

    Bertille M. Harbin;Harry A. Dailey

  • Identification of an FAD Superfamily Containing Protoporphyrinogen Oxidases, Monoamine Oxidases, and Phytoene Desaturase EXPRESSION AND CHARACTERIZATION OF PHYTOENE DESATURASE OFMYXOCOCCUS XANTHUS

    Tamara A. Dailey;Harry A. Dailey

Frequent Co-Authors

Barry H. Paw
Barry H. Paw Brigham and Women's Hospital
John D. Phillips
John D. Phillips University of Utah
Jerry Kaplan
Jerry Kaplan University of Utah
Bi-Cheng Wang
Bi-Cheng Wang University of Georgia
Alan B. Cantor
Alan B. Cantor Harvard University
Daniel E. Bauer
Daniel E. Bauer Harvard University
Diane M. Ward
Diane M. Ward University of Utah
Michael K. Johnson
Michael K. Johnson University of Georgia
Stuart H. Orkin
Stuart H. Orkin Harvard University

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