Works (35)

Updated: July 17th, 2023 21:14

2017 journal article

Thermodynamic and Kinetic Analyses of Iron Response Element (IRE)-mRNA Binding to Iron Regulatory Protein, IRP1

SCIENTIFIC REPORTS, 7.

By: M. Khan*, W. Walden*, E. Theil n & D. Goss*

MeSH headings : Aconitate Hydratase / genetics; Animals; Cations, Divalent / metabolism; Ferritins / genetics; Iron / metabolism; Iron Regulatory Protein 1 / metabolism; Kinetics; Manganese / metabolism; Protein Binding; RNA, Messenger / metabolism; Rabbits; Response Elements; Temperature
TL;DR: The observations suggest decreased RNA hydrogen bonding and changed RNA conformation upon IRP1 binding and illustrate how small, conserved, sequence differences among IRE-mRNAs selectively influence thermodynamic and kinetic selectivity of the protein/RNA interactions. (via Semantic Scholar)
Source: Web Of Science
Added: August 6, 2018

2016 journal article

Modulating the permeability of ferritin channels

RSC ADVANCES, 6(25), 21219–21227.

TL;DR: By changing the electrostatic properties of the residues at the inner edge of each channel, this work can selectively activate/deactivate Fe2+ routes, modulating the rate of iron oxidation at the ferroxidase sites. (via Semantic Scholar)
UN Sustainable Development Goal Categories
Source: Web Of Science
Added: August 6, 2018

2016 review

Solving Biology's Iron Chemistry Problem with Ferritin Protein Nanocages

[Review of ]. ACCOUNTS OF CHEMICAL RESEARCH, 49(5), 784–791.

By: E. Theil n, T. Tosha n & R. Beherat

MeSH headings : Animals; DNA / metabolism; Ferric Compounds / chemistry; Ferritins / chemistry; Ferritins / genetics; Ferritins / metabolism; Heme / metabolism; Humans; Iron / chemistry; Iron / metabolism; Oxidoreductases / chemistry; Oxidoreductases / metabolism; Oxygen / chemistry; Oxygen / metabolism; Protein Structure, Quaternary; RNA, Messenger / metabolism
TL;DR: High ferritin protein cage symmetry (3-fold and 4-fold axes) and amino acid conservation coincide with function, shown by amino acid substitution effects. (via Semantic Scholar)
UN Sustainable Development Goal Categories
Source: Web Of Science
Added: August 6, 2018

2015 journal article

Fe2+ substrate transport through ferritin protein cage ion channels influences enzyme activity and biomineralization

JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY, 20(6), 957–969.

By: R. Behera, R. Torres*, T. Tosha, J. Bradley, C. Goulding* & E. Theil n

author keywords: Ferritin; Iron oxidation; Ion channels; Crystal structure; Electrostatics; Di-iron center; Diferric peroxo; Caged iron-oxy biomineral; Oxidoreductase enzyme reactivity
MeSH headings : Amino Acid Substitution; Crystallography, X-Ray; Ferritins / metabolism; Ferritins / ultrastructure; Ferrous Compounds / metabolism; Ion Channels / metabolism; Ion Channels / ultrastructure; Iron / chemistry; Kinetics; Protein Structure, Secondary
TL;DR: The contributions of ion channel size and structure to ferritin activity reflect metal ion transport in ion channels are precisely regulated both in Ferritin protein nanocages and membranes of living cells. (via Semantic Scholar)
Source: Web Of Science
Added: August 6, 2018

2015 review

IRE mRNA riboregulators use metabolic iron (Fe2+) to control mRNA activity and iron chemistry in animals

[Review of ]. METALLOMICS, 7(1), 15–24.

By: E. Theil n

MeSH headings : Animals; Ferritins / chemistry; Ferritins / genetics; Ferritins / metabolism; Humans; Iron / chemistry; Iron / metabolism; Iron-Regulatory Proteins / chemistry; Iron-Regulatory Proteins / genetics; Iron-Regulatory Proteins / metabolism; RNA, Messenger / chemistry; RNA, Messenger / genetics; RNA, Messenger / metabolism
TL;DR: The high conservation of the primary sequence in IRE-mRNA control elements has facilitated their identification and analysis of metal-assisted riboregulator function, and expansion of RNA search analyses beyond primary will likely reveal other, metal-dependent families of mRNA riboreGulators. (via Semantic Scholar)
UN Sustainable Development Goal Categories
Source: Web Of Science
Added: August 6, 2018

2015 article

Is His54 a gating residue for the ferritin ferroxidase site?

Bernacchioni, C., Ciambellotti, S., Theil, E. C., & Turano, P. (2015, September). BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, Vol. 1854, pp. 1118–1122.

By: C. Bernacchioni, S. Ciambellotti, E. Theil* & P. Turano

author keywords: Ferritin; Ferroxidase site; Reaction kinetics; Mutagenesis
MeSH headings : Binding Sites; Ceruloplasmin / chemistry; Crystallography, X-Ray; Ferritins / chemistry; Histidine / chemistry; Histidine / metabolism; Iron / chemistry
TL;DR: The data here reported are consistent with a role for His54 as a metal ion trap that maintains the correct levels of access of iron to the active site and taking advantage of the comparative sequence analysis of other ferritins. (via Semantic Scholar)
UN Sustainable Development Goal Categories
Source: Web Of Science
Added: August 6, 2018

2014 journal article

A role for iron and oxygen chemistry in preserving soft tissues, cells and molecules from deep time

By: M. Schweitzer, W. Zheng, T. Cleland, M. Goodwin, E. Boatman, E. Theil, M. Marcus, S. Fakra

Source: NC State University Libraries
Added: August 6, 2018

2014 journal article

Coordinating subdomains of ferritin protein cages with catalysis and biomineralization viewed from the C (4) cage axes

JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY, 19(4-5), 615–622.

By: E. Theil*, P. Turano, V. Ghini*, M. Allegrozzi* & C. Bernacchioni*

author keywords: Ferritin; Protein nanocage; Ferric oxo; Di-iron protein; Nanobiomineral
MeSH headings : Catalysis; Ferric Compounds / chemistry; Ferric Compounds / metabolism; Ferritins / chemistry; Ferritins / metabolism; Iron / chemistry; Iron / metabolism; Protein Structure, Secondary
TL;DR: Conserved amino acids facilitate dissolution of ferritin-protein-caged iron biominerals in variants with altered subunit interfaces for trimers (ion channels), E130I, and external dimer surfaces (E88A) as controls, and altered tetramer sub unit interfaces (L165I and H169F). (via Semantic Scholar)
Source: Web Of Science
Added: August 6, 2018

2014 journal article

Loop Electrostatics Modulates the Intersubunit Interactions in Ferritin

ACS CHEMICAL BIOLOGY, 9(11), 2517–2525.

MeSH headings : Circular Dichroism; Electrophoresis, Polyacrylamide Gel; Ferritins / chemistry; Ferritins / genetics; Microscopy, Electron, Transmission; Mutagenesis, Site-Directed; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Static Electricity
TL;DR: It is demonstrated that the electrostatic pairing at the center of the L-loops has a specific kinetic role in the self-assembly of ferritin nanocages. (via Semantic Scholar)
UN Sustainable Development Goal Categories
Source: Web Of Science
Added: August 6, 2018

2014 journal article

Moving Fe2+ from ferritin ion channels to catalytic OH centers depends on conserved protein cage carboxylates

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 111(22), 7925–7930.

By: R. Behera & E. Theil n

author keywords: iron traffic; oxidoreductase enzyme activity; antioxidant; ferrihydrite; BioIron
MeSH headings : Animals; Antioxidants / chemistry; Antioxidants / metabolism; Anura; Catalysis; Conserved Sequence; Ferric Compounds / chemistry; Ferric Compounds / metabolism; Ferritins / chemistry; Ferritins / genetics; Ferritins / metabolism; Heme / chemistry; Heme / metabolism; Hydroxides / chemistry; Hydroxides / metabolism; Ion Channels / chemistry; Ion Channels / metabolism; Iron / chemistry; Iron / metabolism; Metals / chemistry; Metals / metabolism; Minerals / chemistry; Minerals / metabolism; Models, Chemical; Mutagenesis, Site-Directed; Oxidoreductases / chemistry; Oxidoreductases / metabolism; Protein Structure, Secondary; Protein Structure, Tertiary; Substrate Specificity; Sulfates / chemistry; Sulfates / metabolism
TL;DR: M Monitoring rapid diferric peroxo formation in WT ferritin and E57 and E136 variants showed that these conserved residues are required for enzyme activity and thus are functional links betweenferritin ion channels and enzymatic sites. (via Semantic Scholar)
UN Sustainable Development Goal Categories
6. Clean Water and Sanitation (OpenAlex)
Source: Web Of Science
Added: August 6, 2018

2014 journal article

Rapid kinetics of iron responsive element (IRE) RNA/iron regulatory protein 1 and IRE-RNA/eIF4F complexes respond differently to metal ions

NUCLEIC ACIDS RESEARCH, 42(10), 6567–6577.

By: M. Khan*, J. Ma*, W. Walden*, W. Merrick*, E. Theil* & D. Goss*

MeSH headings : Aconitate Hydratase / genetics; Aconitate Hydratase / metabolism; Animals; Eukaryotic Initiation Factor-4F / metabolism; Ferritins / genetics; Ferritins / metabolism; Iron / metabolism; Iron Regulatory Protein 1 / chemistry; Iron Regulatory Protein 1 / metabolism; Kinetics; Manganese / chemistry; Potassium / chemistry; RNA, Messenger / chemistry; RNA, Messenger / metabolism; Rabbits; Regulatory Sequences, Ribonucleic Acid
TL;DR: Rapid rates of protein/RNA complex assembly and dissociation for two IRE-RNAs with IRP1, and quantitatively different metal ion response kinetics that coincide with the different iron responses in vivo are reported, suggesting this regulatory system to respond rapidly to change in cellular iron. (via Semantic Scholar)
Source: Web Of Science
Added: August 6, 2018

2014 journal article

Spectroscopic Studies of Single and Double Variants of M Ferritin: Lack of Conversion of a Biferrous Substrate Site into a Cofactor Site for O-2 Activation

BIOCHEMISTRY, 53(3), 473–482.

By: Y. Kwak*, J. Schwartz*, S. Haldar, R. Behera, T. Tosha, E. Theil n, E. Solomon*

MeSH headings : Amino Acid Sequence; Animals; Catalytic Domain; Circular Dichroism; Ferritins / chemistry; Ferritins / genetics; Ferrous Compounds / chemistry; Histidine / chemistry; Iron / chemistry; Ligands; Models, Molecular; Mutation; Oxygen / chemistry; Oxygen / metabolism; Rana catesbeiana; Ribonucleotide Reductases / chemistry
TL;DR: Correlation of this double variant and the cofactor sites to their O2 reactivities indicates that electrostatic and steric changes in the active site and, in particular, the hydrophobic nature of a cofactor site associated with its second sphere protein environment, make important contributions to the activation of O2 by the binuclear non-heme iron enzymes. (via Semantic Scholar)
UN Sustainable Development Goal Categories
6. Clean Water and Sanitation (OpenAlex)
Source: Web Of Science
Added: August 6, 2018

2013 journal article

Ferritin: The Protein Nanocage and Iron Biomineral in Health and in Disease

INORGANIC CHEMISTRY, 52(21), 12223–12233.

By: E. Theil n

MeSH headings : Anemia / drug therapy; Animals; Catalytic Domain; Drug Delivery Systems / methods; Ferritins / chemistry; Ferritins / genetics; Ferritins / metabolism; Hemosiderin / metabolism; Humans; Iron Overload / drug therapy; Molecular Targeted Therapy / methods; Nanostructures / administration & dosage; RNA, Messenger; Transfusion Reaction
TL;DR: Current concepts of ferritin structure/function/genetic regulation are discussed and related to possible therapeutic targets such as mini-ferritin/Dps protein active sites (selective pathogen inhibition in infection), nanocage pores (iron chelation in therapeutic hypertransfusion), mRNA noncoding, IRE riboregulator, and protein nanovessels to deliver medicinal or sensor cargo are discussed. (via Semantic Scholar)
Source: Web Of Science
Added: August 6, 2018

2013 journal article

METALLOENZYMES Cage redesign explains assembly

Nature Chemical Biology, 9(3), 143–144.

By: E. Theil & P. Turano

Source: NC State University Libraries
Added: August 6, 2018

2011 article

New Dimensions of RNA in Molecular Recognition and Catalysis

Theil, E. C., & Westhof, E. (2011, December). ACCOUNTS OF CHEMICAL RESEARCH, Vol. 44, pp. 1255–1256.

By: E. Theil* & E. Westhof*

MeSH headings : Catalysis; RNA / chemistry; RNA / metabolism; RNA, Catalytic / chemistry; RNA, Catalytic / metabolism; RNA, Untranslated / chemistry; RNA, Untranslated / metabolism
UN Sustainable Development Goal Categories
Source: Web Of Science
Added: August 6, 2018

2000 journal article

Identification and characterization of the iron regulatory element in the ferritin gene of a plant (soybean)

JOURNAL OF BIOLOGICAL CHEMISTRY, 275(23), 17488–17493.

By: J. Wei n & E. Theil n

MeSH headings : Base Sequence; Ferritins / genetics; Genes, Reporter; Glucuronidase / genetics; Iron / metabolism; Iron-Regulatory Proteins; Iron-Sulfur Proteins / metabolism; Luciferases / genetics; Molecular Sequence Data; Mutagenesis, Insertional; Plant Leaves; Promoter Regions, Genetic; RNA, Messenger / genetics; RNA-Binding Proteins / metabolism; Recombinant Proteins / biosynthesis; Sequence Deletion; Soybeans / genetics
TL;DR: DNA and DNA were used to show that an 86-base pair fragment controlled iron-mediated derepression of the ferritin gene, and FRE/factor binding was abrogated by increased tissue iron, in analogy to mRNA (IRE)/iron regulatory protein in animals. (via Semantic Scholar)
Source: Web Of Science
Added: August 6, 2018

2000 journal article

Internal loop/bulge and hairpin loop of the iron-responsive element of ferritin mRNA contribute to maximal iron regulatory protein 2 binding and translational regulation in the iso-iron-responsive element/iso-iron regulatory protein family

BIOCHEMISTRY, 39(20), 6235–6242.

By: Y. Ke n, H. Sierzputowska-Gracz n, Z. Gdaniec n & E. Theil n

MeSH headings : Animals; Copper / chemistry; Ferritins / antagonists & inhibitors; Ferritins / biosynthesis; Ferritins / chemistry; Ferritins / genetics; Hot Temperature; Iron Regulatory Protein 1; Iron Regulatory Protein 2; Iron-Regulatory Proteins; Iron-Sulfur Proteins / chemistry; Iron-Sulfur Proteins / genetics; Iron-Sulfur Proteins / physiology; Lizards; Magnesium / chemistry; Multigene Family; Mutagenesis, Site-Directed; Nuclear Magnetic Resonance, Biomolecular; Nucleic Acid Conformation; Phenanthrolines / chemistry; Protein Binding / genetics; Protein Biosynthesis; Protein Denaturation; Protein Isoforms / chemistry; Protein Isoforms / genetics; RNA, Messenger / chemistry; RNA-Binding Proteins / chemistry; RNA-Binding Proteins / genetics; RNA-Binding Proteins / physiology; Rabbits; Rana catesbeiana; Repressor Proteins / genetics; Repressor Proteins / physiology; Ribonuclease T1 / chemistry
TL;DR: The lower stability and greater helix distortion in the ferritin IL/B-IRE compared to the C-bulge iso-IREs create a combinatorial set of RNA/protein interactions that control protein synthesis rates with a range of signal sensitivities. (via Semantic Scholar)
UN Sustainable Development Goal Categories
6. Clean Water and Sanitation (OpenAlex)
Source: Web Of Science
Added: August 6, 2018

2000 journal article

The ferritin iron entry and exit problem

INORGANICA CHIMICA ACTA, 297(1-2), 242–251.

By: E. Theil*, H. Takagi n, G. Small n, L. He n, A. Tipton & D. Danger n

author keywords: ferritin; iron biominerals; ferroxidation; iron/dioxygen catalysis
TL;DR: The entry and exit of Fe(II) ions in ferritin are endpoints in the process which concentrates iron as a solid (hydrated ferric oxide) to be used by living cells, suggesting a regulation-sensitive biological signal for iron exit. (via Semantic Scholar)
UN Sustainable Development Goal Categories
6. Clean Water and Sanitation (OpenAlex)
Source: Web Of Science
Added: August 6, 2018

1999 journal article

Crystal structure of bullfrog M ferritin at 2.8 angstrom resolution: analysis of subunit interactions and the binuclear metal center

JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY, 4(3), 243–256.

By: Y. Ha*, D. Shi*, G. Small n, E. Theil n & N. Allewell*

author keywords: crystallography; iron oxidation; iron storage; multisubunit proteins
MeSH headings : Amino Acid Sequence; Animals; Aspartic Acid; Binding Sites; Conserved Sequence; Crystallography, X-Ray; Ferritins / chemistry; Ferritins / metabolism; Magnesium / metabolism; Models, Molecular; Molecular Sequence Data; Protein Conformation; Rana catesbeiana; Sequence Homology, Amino Acid; Tyrosine / analysis; Tyrosine / metabolism
TL;DR: The crystal structure of the homopolymer of recombinant frog M ferritin is determined and it is suggested that Gln137 and Asp140 are a vestige of the second GluxxHis site, resulting from single nucleotide mutations of Glu and His codons and giving rise to Ala140 or Ser140 present in other eukaryotic H-type ferritins, by additional singleucleotide mutations. (via Semantic Scholar)
UN Sustainable Development Goal Categories
Source: Web Of Science
Added: August 6, 2018

1999 article

Iron regulatory element and internal loop/bulge structure for ferritin mRNA studied by cobalt(III) hexammine binding, molecular modeling, and NMR spectroscopy (vol 37, pg 1505, 1998)

Gdaniec, Z., Sierzputowska-Gracz, H., & Theil, E. C. (1999, April 27). BIOCHEMISTRY, Vol. 38, pp. 5676–5676.

By: Z. Gdaniec, H. Sierzputowska-Gracz* & E. Theil*

TL;DR: The ferritin IRE, a highly conserved mRNA translation regulatory element in animal mRNA, was studied by molecular modeling (using MC-SYM and DOCKING) and by NMR spectroscopy and is the best characterized IRE in terms of structure and function. (via Semantic Scholar)
Source: Web Of Science
Added: August 6, 2018

1998 journal article

Direct spectroscopic and kinetic evidence for the involvement of a peroxodiferric intermediate during the ferroxidase reaction in fast ferritin mineralization

BIOCHEMISTRY, 37(28), 9871–9876.

By: A. Pereira n, W. Small n, C. Krebs n, P. Tavares n, D. Edmondson n, E. Theil n, B. Huynh n

MeSH headings : Animals; Anura; Ceruloplasmin / chemistry; Ferric Compounds / chemistry; Ferritins / chemistry; Ferritins / genetics; Humans; Kinetics; Oxidation-Reduction; Recombinant Proteins / chemistry; Spectroscopy, Mossbauer
TL;DR: The proposal that a single protein site, with a structure homologous to the diiron centers in MMOH and R2, is involved in the ferritin ferroxidation step is confirmed by the observed kinetics, spectroscopic properties, and purity of the initial peroxodiferric species formed in the frog M ferritIn. (via Semantic Scholar)
UN Sustainable Development Goal Categories
Source: Web Of Science
Added: August 6, 2018

1998 journal article

Evidence for reutilization of nodule iron in soybean seed development

JOURNAL OF PLANT NUTRITION, 21(5), 913–927.

By: J. Burton n, C. Harlow n & E. Theil n

TL;DR: The 59Fe distribution as well as immunoreactive ferritin were examined throughout development in nodule, leaf, and seed tissue, and leaves, nodules, and seeds accounted for 75 to 87% of the total plant 59Fe throughout the reproductive perio... (via Semantic Scholar)
UN Sustainable Development Goal Categories
Source: Web Of Science
Added: August 6, 2018

1998 journal article

Iron regulatory element and internal loop/bulge structure for ferritin mRNA studied by cobalt(III) hexammine binding, molecular modeling, and NMR spectroscopy

BIOCHEMISTRY, 37(6), 1505–1512.

By: Z. Gdaniec n, H. Sierzputowska-Gracz n & E. Theil n

MeSH headings : Animals; Anura; Binding Sites / drug effects; Binding Sites / genetics; Chlorides / metabolism; Chlorides / pharmacology; Cobalt / metabolism; Cobalt / pharmacology; Ferritins / genetics; Indicators and Reagents; Iron-Regulatory Proteins; Iron-Sulfur Proteins / chemistry; Iron-Sulfur Proteins / drug effects; Iron-Sulfur Proteins / genetics; Iron-Sulfur Proteins / metabolism; Magnetic Resonance Spectroscopy; Models, Molecular; Nucleic Acid Conformation; Protons; RNA, Messenger / chemistry; RNA, Messenger / metabolism; RNA-Binding Proteins / chemistry; RNA-Binding Proteins / drug effects; RNA-Binding Proteins / genetics; RNA-Binding Proteins / metabolism
TL;DR: Distortion of the IRE helix by the internal loop/bulge near a conserved unpaired C required for IRP binding and adjacent to an IRP cross-linking site suggests a role for the pocket in ferritin IRE/IRP interactions. (via Semantic Scholar)
UN Sustainable Development Goal Categories
6. Clean Water and Sanitation (OpenAlex)
Source: Web Of Science
Added: August 6, 2018

1998 journal article

Localized unfolding at the junction of three ferritin subunits - A mechanism for iron release?

JOURNAL OF BIOLOGICAL CHEMISTRY, 273(30), 18685–18688.

By: H. Takagi, D. Shi, Y. Ha, N. Allewell & E. Theil*

MeSH headings : Amino Acid Substitution; Animals; Crystallography, X-Ray; Ferritins / genetics; Ferritins / metabolism; Iron / metabolism; Kinetics; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Folding; Ranidae; Spectrophotometry, Atomic; Structure-Activity Relationship
TL;DR: The junction of three ferritin subunits appears to be a dynamic aperture with a “shutter” that cytoplasmic factors might open or close to regulate iron release in vivo. (via Semantic Scholar)
UN Sustainable Development Goal Categories
6. Clean Water and Sanitation (OpenAlex)
Source: Web Of Science
Added: August 6, 2018

1998 journal article

Loops and bulge/loops in iron-responsive element isoforms influence iron regulatory protein binding - Fine-tuning of mRNA regulation?

JOURNAL OF BIOLOGICAL CHEMISTRY, 273(37), 23637–23640.

By: Y. Ke, J. Wu, E. Leibold, W. Walden & E. Theil*

MeSH headings : 5-Aminolevulinate Synthetase / genetics; Aconitate Hydratase / genetics; Animals; Base Composition; Base Sequence; Cloning, Molecular; Ferritins / genetics; Gene Expression Regulation; Iron Regulatory Protein 1; Iron Regulatory Protein 2; Iron-Regulatory Proteins; Iron-Sulfur Proteins / genetics; Iron-Sulfur Proteins / metabolism; Liver / metabolism; Nucleic Acid Conformation; RNA, Messenger / biosynthesis; RNA, Messenger / chemistry; RNA, Messenger / genetics; RNA-Binding Proteins / genetics; RNA-Binding Proteins / metabolism; Rabbits; Receptors, Transferrin / genetics; Recombinant Proteins / metabolism; Saccharomyces cerevisiae
TL;DR: The results predict mRNA-specific variation in IRE-dependent regulation in vivo and may relate to previously observed differences in iron-induced ferritin and m-aconitase synthesis in liver and cultured cells. (via Semantic Scholar)
Source: Web Of Science
Added: August 6, 2018

1998 patent

Methods of identifying transition metal complexes that selectively cleave regulatory elements of mRNA and uses thereof

Washington, DC: U.S. Patent and Trademark Office.

By: E. Theil

Source: NC State University Libraries
Added: August 6, 2018

1998 book

Principles of chemistry in biology: A teaching companion

Washington, DC: American Chemical Society; Distributed by Oxford University Press.

Elizabeth Theil

Source: NC State University Libraries
Added: August 6, 2018

1998 journal article

The iron responsive element (IRE) family of mRNA regulators: Regulation of iron transport and uptake compared in animals, plants, and microorganisms

Iron Transport and Storage in Microorganisms, Plants and Animals, 35(1998), 403–434.

By: E. Theil

Source: NC State University Libraries
Added: August 6, 2018

1997 journal article

Preliminary analysis of amphibian red cell M ferritin in a novel tetragonal unit cell

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 53, 513–523.

By: Y. Ha*, E. Theil* & N. Allewell*

TL;DR: Recombinant amphibian red cell M ferritin crystallizes in approximately 2 M (NH(4))(2)SO(4) at pH 4.6 in a space group that has not been reported previously and has a novel intermolecular interaction mediated by interdigitation of the DE loops of two molecules at the fourfold molecular axes. (via Semantic Scholar)
UN Sustainable Development Goal Categories
Source: Web Of Science
Added: August 6, 2018

1997 journal article

Rapid and parallel formation of Fe3+ multimers, including a trimer, during H-type subunit ferritin mineralization

BIOCHEMISTRY, 36(25), 7917–7927.

By: A. Pereira n, P. Tavares n, S. Lloyd n, D. Danger n, D. Edmondson n, E. Theil n, B. Huynh n

MeSH headings : Animals; Anura; Biopolymers; Electron Spin Resonance Spectroscopy; Ferric Compounds / chemistry; Ferritins / chemistry; Minerals / chemistry; Oxidation-Reduction; Recombinant Proteins / chemistry; Spectroscopy, Mossbauer
TL;DR: The subsequent decay of these multiple Fe3-oxy species to the superparamagnetic mineral suggests that Fe3+ species in different environments may be translocated as intact units from the protein shell into the ferritin cavity where the conversion to a solid mineral occurs. (via Semantic Scholar)
UN Sustainable Development Goal Categories
Source: Web Of Science
Added: August 6, 2018

1997 journal article

Sustainable solution for dietary iron deficiency through plant biotechnology and breeding to increase seed ferritin control

European Journal of Clinical Nutrition, 51(Suppl. 4), S28–31.

By: E. Theil, J. Burton & J. Beard

Source: NC State University Libraries
Added: August 6, 2018

1997 journal article

The influence of conserved tyrosine 30 and tissue-dependent differences in sequence on ferritin function: use of blue and purple Fe(III) species as reporters of ferroxidation

Journal of Biological Inorganic Chemistry, 2(5), 652–661.

By: J. Fetter n, J. Cohen*, D. Danger n, L. Sanders* & E. Theil n

TL;DR: The impact of Y30F on rates of formation of Fe(III)-protein complexes in ferritin, combined with Mössbauer spectroscopic studies, indicate that at least one of the pathways for Fe oxidation/transfer in Ferritin is through the center of the four-helix bundle and is influenced by structural features dependent on tyrosine 30. (via Semantic Scholar)
UN Sustainable Development Goal Categories
Source: NC State University Libraries
Added: August 6, 2018

1997 chapter

Translational regulation of bioiron

In S. Silver & W. Walden (Eds.), Metal ions in gene regulation (pp. 131–156).

By: E. Theil*

Ed(s): . S. Silver & W. Walden

TL;DR: The problem of acquiring and concentrating iron is solved by the use of environmental iron to regulate expression of both iron-storage (ferritin) and iron-uptake (TfR) genes; changes in expression of ferritin and TfR are also regulated by growth factors and hormones and during cell differentiation. (via Semantic Scholar)
Source: NC State University Libraries
Added: August 6, 2018

1990 journal article

Regulation of ferritin and transferrin receptor messenger-rnas

Journal of Biological Chemistry, 265(9), 4771–4774.

By: E. Theil

Source: NC State University Libraries
Added: August 6, 2018

1987 review

FERRITIN - STRUCTURE, GENE-REGULATION, AND CELLULAR FUNCTION IN ANIMALS, PLANTS, AND MICROORGANISMS

[Review of ]. ANNUAL REVIEW OF BIOCHEMISTRY, 56, 289–315.

By: E. Theil*

UN Sustainable Development Goal Categories
Source: Web Of Science
Added: August 6, 2018

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