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Dealing with iron: Common structural principles in proteins that transport iron and heme
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/prot.340200208openalex-snapshot
Conformational analysis of hemopexin by fourier‐transform infrared and circular dichroism spectroscopy
inferredcites →https://doi.org/10.1006/jmbi.1995.0611openalex-snapshot
Crystal Structure of Diferric Hen Ovotransferrin at 2.4 Å Resolution
inferredcites →https://doi.org/10.1006/jmbi.1996.0091openalex-snapshot
Altered Domain Closure and Iron Binding in Transferrins: The Crystal Structure of the Asp60Ser Mutant of the Amino-terminal Half-molecule of Human Lactoferrin
inferredcites →https://doi.org/10.1007/978-1-4612-3956-7_12openalex-snapshot
Structural and Functional Flexibility of Lactoferrin
inferredcites →https://doi.org/10.1016/0005-2795(72)90283-8openalex-snapshot
Lactoferrin and transferrin: A comparative study
inferredcites →https://doi.org/10.1016/0014-5793(92)80060-topenalex-snapshot
Human melanotransferrin (p97) has only one functional iron‐binding site
inferredcites →https://doi.org/10.1016/0022-2836(89)90602-5openalex-snapshot
Structure of human lactoferrin: Crystallographic structure analysis and refinement at 2·8 Å resolution
inferredcites →https://doi.org/10.1016/0162-0134(86)80107-6openalex-snapshot
Estimation of the ferrous—transferrin binding constants based on thermodynamic studies of nickel(II)—transferrin
inferredcites →https://doi.org/10.1016/0162-0134(92)84061-qopenalex-snapshot
New perspectives on the structure and function of transferrins
inferredcites →https://doi.org/10.1016/0968-0004(82)90183-9openalex-snapshot
The evolution of transferrin
inferredcites →https://doi.org/10.1016/0968-0004(83)90217-7openalex-snapshot
Iron uptake and utilization by mammalian cells. I: Cellular uptake of transferrin and iron
inferredcites →https://doi.org/10.1016/0968-0004(86)90196-9openalex-snapshot
She walked in the very best circles…
inferredcites →https://doi.org/10.1016/0968-0004(87)90163-0openalex-snapshot
Transferrins: insights into structure and function from studies on lactoferrin
inferredcites →https://doi.org/10.1016/s0014-5793(02)02248-2openalex-snapshot
A second melanotransferrin gene (MTf2) and a novel protein isoform: explanation for the membrane‐bound and soluble forms of melanotransferrin?
inferredcites →https://doi.org/10.1016/s0021-9258(17)37057-6openalex-snapshot
The 1.9 A x-ray structure of a closed unliganded form of the periplasmic glucose/galactose receptor from Salmonella typhimurium.
inferredcites →https://doi.org/10.1016/s0021-9258(18)43229-2openalex-snapshot
The formation of Fe3+-transferrin-CO3(2-) via the binding and oxidation of Fe2+.
inferredcites →https://doi.org/10.1016/s0021-9258(18)53247-6openalex-snapshot
Identification of the histidine residues of hemopexin that coordinate with heme-iron and of a receptor-binding region.
inferredcites →https://doi.org/10.1016/s0021-9258(20)71310-4openalex-snapshot
Domain structure of rabbit hemopexin. Isolation and characterization of a heme-binding glycopeptide.
inferredcites →https://doi.org/10.1016/s0076-6879(97)77028-9openalex-snapshot
[26] Raster3D: Photorealistic molecular graphics
inferredcites →https://doi.org/10.1016/s0898-8838(08)60176-2openalex-snapshot
Structure and Reactivity of Transferrins
inferredcites →https://doi.org/10.1016/s0959-440x(99)00035-4openalex-snapshot
β Propellers: structural rigidity and functional diversity
inferredcites →https://doi.org/10.1016/s0968-0004(99)01384-5openalex-snapshot
The WD repeat: a common architecture for diverse functions
inferredcites →https://doi.org/10.1016/s0969-2126(01)00189-7openalex-snapshot
1.8 å crystal structure of the C-terminal domain of rabbit serum haemopexin
inferredcites →https://doi.org/10.1021/bi00079a018openalex-snapshot
Characterization of hemopexin and its interaction with heme by differential scanning calorimetry and circular dichroism
inferredcites →https://doi.org/10.1021/bi00096a004openalex-snapshot
Structural evidence for a pH-sensitive dilysine trigger in the hen ovotransferrin N-lobe: Implications for transferrin iron release
inferredcites →https://doi.org/10.1021/bi00105a019openalex-snapshot
Receptor-modulated iron release from transferrin: differential effects on N- and C-terminal sites
inferredcites →https://doi.org/10.1021/bi00415a061openalex-snapshot
Molecular structure of serum transferrin at 3.3-.ANG. resolution
inferredcites →https://doi.org/10.1021/bi00515a031openalex-snapshot
Studies of anion binding by transferrin using carbon-13 nuclear magnetic resonance spectroscopy
inferredcites →https://doi.org/10.1021/bi010907popenalex-snapshot
Ligand Variation in the Transferrin Family: The Crystal Structure of the H249Q Mutant of the Human Transferrin N-lobe As a Model for Iron Binding in Insect Transferrins,
inferredcites →https://doi.org/10.1021/bi980355jopenalex-snapshot
Two High-Resolution Crystal Structures of the Recombinant N-Lobe of Human Transferrin Reveal a Structural Change Implicated in Iron Release,
inferredcites →https://doi.org/10.1021/bi9812064openalex-snapshot
Ligand-Induced Conformational Change in Transferrins: Crystal Structure of the Open Form of the N-Terminal Half-Molecule of Human Transferrin,
inferredcites →https://doi.org/10.1021/bi990134topenalex-snapshot
Dual Role of Lys206−Lys296 Interaction in Human Transferrin N-Lobe: Iron-Release Trigger and Anion-Binding Site
inferredcites →https://doi.org/10.1023/a:1009252919854openalex-snapshot
Iron and activated oxygen species in biology: The basic chemistry
inferredcites →https://doi.org/10.1038/13294openalex-snapshot
Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two beta-propeller domains.
inferredcites →https://doi.org/10.1038/344784a0openalex-snapshot
Apolactoferrin structure demonstrates ligand-induced conformational change in transferrins
inferredcites →https://doi.org/10.1038/nsb1197-919openalex-snapshot
Structure of Haemophilus influenzae Fe+3-binding protein reveals convergent evolution within a superfamily
inferredcites →https://doi.org/10.1073/pnas.80.8.2263openalex-snapshot
Binding of apotransferrin to K562 cells: explanation of the transferrin cycle.
inferredcites →https://doi.org/10.1073/pnas.82.1.73openalex-snapshot
Complete amino acid sequence of human hemopexin, the heme-binding protein of serum.
inferredcites →https://doi.org/10.1073/pnas.84.7.1769openalex-snapshot
Structure of human lactoferrin at 3.2-A resolution.
inferredcites →https://doi.org/10.1074/jbc.271.22.12790openalex-snapshot
Cooperative Interactions between the Amino- and Carboxyl-terminal Lobes Contribute to the Unique Iron-binding Stability of Lactoferrin
inferredcites →https://doi.org/10.1074/jbc.274.15.10190openalex-snapshot
Alternative Structural State of Transferrin
inferredcites →https://doi.org/10.1074/jbc.274.40.28445openalex-snapshot
Crystal Structure of Hen Apo-ovotransferrin
inferredcites →https://doi.org/10.1107/s0021889891004399openalex-snapshot
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
inferredcites →https://doi.org/10.1107/s0907444901017309openalex-snapshot
The crystal and molecular structures of diferric porcine and rabbit serum transferrins at resolutions of 2.15 and 2.60 Å, respectively
inferredcites →https://doi.org/10.1107/s0907444992012101openalex-snapshot
The mechanism of iron uptake by transferrins: the structure of an 18 kDa NII-domain fragment from duck ovotransferrin at 2.3 Å resolution
inferredcites →https://doi.org/10.1107/s0907444998004417openalex-snapshot
Structure of Human Apolactoferrin at 2.0 Å Resolution. Refinement and Analysis of Ligand-Induced Conformational Change
inferredcites →https://doi.org/10.1107/s0907444999003807openalex-snapshot
Structure of mare apolactoferrin: the N and C lobes are in the closed form
inferredcites →https://doi.org/10.1107/s0907444999094317openalex-snapshot
Structure of human apolactoferrin at 2.0 Å resolution. Refinement and analysis of ligand-induced conformational change. Addendum
inferredcites →https://doi.org/10.1111/j.1365-2958.1995.mmi_18030383.xopenalex-snapshot
Quelling the red menace: haem capture by bacteria
inferredcites →https://doi.org/10.1111/j.1365-2958.1996.tb02484.xopenalex-snapshot
Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes
inferredcites →https://doi.org/10.1111/j.1432-1033.1974.tb03386.xopenalex-snapshot
Transfer of Heme from Ferrihemoglobin and Ferrihemoglobin Isolated Chains to Hemopexin
inferredcites →https://doi.org/10.1111/j.1432-1033.1995.1102g.xopenalex-snapshot
Transferrin, a Mechanism for Iron Release
inferredcites →https://doi.org/10.1128/mr.57.2.320-346.1993openalex-snapshot
Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria
inferredcites →https://doi.org/10.1139/o01-153openalex-snapshot
Lactoferrin and transferrin: Functional variations on a common structural framework
inferredcites →https://doi.org/10.1201/9780824744175.fmatt1openalex-snapshot
Molecular and Cellular Iron Transport
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inferred← citeshttps://doi.org/10.1016/j.pep.2010.04.019openalex-snapshot
Expression, purification, and characterization of recombinant human transferrin from rice (Oryza sativa L.)
inferred← citeshttps://doi.org/10.1016/s0006-3495(03)74769-9openalex-snapshot
A Computational Study of the Open and Closed Forms of the N-Lobe Human Serum Transferrin Apoprotein
inferred← citeshttps://doi.org/10.1016/s0091-679x(06)79018-5openalex-snapshot
Reconstructing the Endocytotic Machinery
inferred← citeshttps://doi.org/10.1016/s0092-8674(04)00130-8openalex-snapshot
Structure of the Human Transferrin Receptor-Transferrin Complex
inferred← citeshttps://doi.org/10.1016/s0092-8674(04)00165-5openalex-snapshot
Mysteries of the Transferrin-Transferrin Receptor 1 Interaction Uncovered
inferred← citeshttps://doi.org/10.1016/s1773-2247(12)50006-7openalex-snapshot
Targeted lipid-based systems for siRNA delivery
inferred← citeshttps://doi.org/10.1017/s003358350500404xopenalex-snapshot
Role of cofactors in metalloprotein folding
inferred← citeshttps://doi.org/10.1021/acs.analchem.6b04631openalex-snapshot
Analytical Methods for Imaging Metals in Biology: From Transition Metal Metabolism to Transition Metal Signaling
inferred← citeshttps://doi.org/10.1021/acs.cgd.9b00169openalex-snapshot
Lysine as Size-Control Additive in a Bioinspired Synthesis of Pure Superparamagnetic Magnetite Nanoparticles
inferred← citeshttps://doi.org/10.1021/acs.jcim.8b00525openalex-snapshot
Insights into the Mechanisms of the Pyrazinamide Resistance of Three Pyrazinamidase Mutants N11K, P69T, and D126N
inferred← citeshttps://doi.org/10.1021/acsaenm.6c00253openalex-snapshot
Investigation of Cytotoxic Factors Affecting Cell Viability in Response to Iron Nitride Particles
inferred← citeshttps://doi.org/10.1021/acsbiomaterials.8b00791openalex-snapshot
Polydopamine-Assisted Hydroxyapatite and Lactoferrin Multilayer on Titanium for Regulating Bone Balance and Enhancing Antibacterial Property
inferred← citeshttps://doi.org/10.1021/cr900052gopenalex-snapshot
Living with Iron (and Oxygen): Questions and Answers about Iron Homeostasis
inferred← citeshttps://doi.org/10.1021/jp310719gopenalex-snapshot
Aqueous Guanidinium–Carbonate Interactions by Molecular Dynamics and Neutron Scattering: Relevance to Ion–Protein Interactions
inferred← citeshttps://doi.org/10.1021/la047162jopenalex-snapshot
Surface-Induced Unfolding of Human Lactoferrin
inferred← citeshttps://doi.org/10.1023/b:biom.0000027693.60932.26openalex-snapshot
Lactoferrin: Role in iron homeostasis and host defense against microbial infection
inferred← citeshttps://doi.org/10.1038/nature25982openalex-snapshot
Carbonate-sensitive phytotransferrin controls high-affinity iron uptake in diatoms
inferred← citeshttps://doi.org/10.1038/s42004-022-00703-6openalex-snapshot
β-Hydroxylation of α-amino-β-hydroxylbutanoyl-glycyluridine catalyzed by a nonheme hydroxylase ensures the maturation of caprazamycin
inferred← citeshttps://doi.org/10.1038/srep00999openalex-snapshot
Iron and bismuth bound human serum transferrin reveals a partially-opened conformation in the N-lobe
inferred← citeshttps://doi.org/10.1038/srep04806openalex-snapshot
Alternative splicing contributes to the coordinated regulation of ferritin subunit levels in Bactrocera dorsalis (Hendel)
inferred← citeshttps://doi.org/10.1039/b604184copenalex-snapshot
Structural modelling of metal ion binding to human haemopexin
inferred← citeshttps://doi.org/10.1039/b604193kopenalex-snapshot
Heme and virulence: how bacterial pathogens regulate, transport and utilize heme
inferred← citeshttps://doi.org/10.1039/b705136kopenalex-snapshot
Iron-binding properties of plant phenolics and cranberry's bio-effects
inferred← citeshttps://doi.org/10.1039/c2nj40201gopenalex-snapshot
Ytterbium-substituted transferrin and lactoferrin for near-infrared luminescent pH indication
inferred← citeshttps://doi.org/10.1039/c7ra04272hopenalex-snapshot
Specific identification of human transferrin conformations using a cyanine dye supramolecular assembly
inferred← citeshttps://doi.org/10.1039/d0ra09326bopenalex-snapshot
A computational perspective on the dynamic behaviour of recurrent drug resistance mutations in the pncA gene from Mycobacterium tuberculosis
inferred← citeshttps://doi.org/10.1039/d2nj01696fopenalex-snapshot
Turn-on silicon-based fluorescent probe for visualizing endogenous CO during hypoxia
inferred← citeshttps://doi.org/10.1039/d4ta05988copenalex-snapshot
Mode of electroactive species evolution from Fe 3 X 4 (X = Se, S, O): guidelines from the redox chemistry of chalcogen anions
inferred← citeshttps://doi.org/10.1042/bj20031283openalex-snapshot
Oxo-iron clusters in a bacterial iron-trafficking protein: new roles for a conserved motif
inferred← citeshttps://doi.org/10.1046/j.1365-2958.2003.03686.xopenalex-snapshot
Ligand delivery by haem carrier proteins: the binding of Serratia marcescens haemophore to its outer membrane receptor is mediated by two distinct peptide regions
inferred← citeshttps://doi.org/10.1073/pnas.0730378100openalex-snapshot
Biological inorganic chemistry at the beginning of the 21st century
inferred← citeshttps://doi.org/10.1073/pnas.0904793106openalex-snapshot
Characterization of a Bacillus subtilis transporter for petrobactin, an anthrax stealth siderophore
inferred← citeshttps://doi.org/10.1073/pnas.0914898107openalex-snapshot
Noncanonical interactions between serum transferrin and transferrin receptor evaluated with electrospray ionization mass spectrometry
inferred← citeshttps://doi.org/10.1073/pnas.1121549109openalex-snapshot
Induced fit on heme binding to the Pseudomonas aeruginosa cytoplasmic protein (PhuS) drives interaction with heme oxygenase (HemO)
inferred← citeshttps://doi.org/10.1073/pnas.2305495120openalex-snapshot
Pumping iron: A multi-omics analysis of two extremophilic algae reveals iron economy management
inferred← citeshttps://doi.org/10.1074/jbc.c700081200openalex-snapshot
Acetylated Histone Tail Peptides Induce Structural Rearrangements in the RSC Chromatin Remodeling Complex
inferred← citeshttps://doi.org/10.1074/jbc.m110.127506openalex-snapshot
Iron-mediated Oxidation Induces Conformational Changes within the Redox-sensing Protein HbpS
inferred← citeshttps://doi.org/10.1074/jbc.m408963200openalex-snapshot
The Interaction of Covalently Bound Heme with the Cytochrome c Maturation Protein CcmE
inferred← citeshttps://doi.org/10.1074/jbc.m414650200openalex-snapshot
Calorimetric Studies of Melanotransferrin (p97) and Its Interaction with Iron
inferred← citeshttps://doi.org/10.1074/jbc.m508355200openalex-snapshot
Functional Characterization of the C-terminal Domain of the Cytochrome c Maturation Protein CcmE
inferred← citeshttps://doi.org/10.1074/jbc.m508903200openalex-snapshot
RPE65 Is an Iron(II)-dependent Isomerohydrolase in the Retinoid Visual Cycle
inferred← citeshttps://doi.org/10.1074/jbc.m604592200openalex-snapshot
The Crystal Structure of Iron-free Human Serum Transferrin Provides Insight into Inter-lobe Communication and Receptor Binding
inferred← citeshttps://doi.org/10.1074/jbc.m607684200openalex-snapshot
Structure of the Escherichia coli O157:H7 Heme Oxygenase ChuS in Complex with Heme and Enzymatic Inactivation by Mutation of the Heme Coordinating Residue His-193
inferred← citeshttps://doi.org/10.1074/jbc.m700664200openalex-snapshot
Evidence That the Heme Regulatory Motifs in Heme Oxygenase-2 Serve as a Thiol/Disulfide Redox Switch Regulating Heme Binding
inferred← citeshttps://doi.org/10.1074/jbc.m709907200openalex-snapshot
FutA2 Is a Ferric Binding Protein from Synechocystis PCC 6803
inferred← citeshttps://doi.org/10.1074/mcp.m500095-mcp200openalex-snapshot
Structural Allostery and Binding of the Transferrin·Receptor Complex
inferred← citeshttps://doi.org/10.1080/07391102.2020.1761879openalex-snapshot
Structural insights of catalytic mechanism in mutant pyrazinamidase of Mycobacterium tuberculosis
inferred← citeshttps://doi.org/10.1080/10425170701461854openalex-snapshot
Molecular cloning and characterization of a transferrin cDNA from the white-spotted flower chafer,Protaetia brevitarsis
inferred← citeshttps://doi.org/10.1080/15216540500380871openalex-snapshot
Hemoglobin and heme scavenging
inferred← citeshttps://doi.org/10.1080/15216540701689666openalex-snapshot
Heme‐hemopexin: A ‘Chronosteric’ heme‐protein
inferred← citeshttps://doi.org/10.1080/19420862.2022.2122957openalex-snapshot
Physicochemical and biological impact of metal-catalyzed oxidation of IgG1 monoclonal antibodies and antibody-drug conjugates via reactive oxygen species
inferred← citeshttps://doi.org/10.1089/ars.2009.2787openalex-snapshot
Heme Scavenging and the Other Facets of Hemopexin
inferred← citeshttps://doi.org/10.1089/ars.2011.4282openalex-snapshot
Pathological Conditions Involving Extracellular Hemoglobin: Molecular Mechanisms, Clinical Significance, and Novel Therapeutic Opportunities for α 1 -Microglobulin
inferred← citeshttps://doi.org/10.1089/ars.2012.4878openalex-snapshot
Trapping of Human Hemoglobin by Haptoglobin: Molecular Mechanisms and Clinical Applications
inferred← citeshttps://doi.org/10.1093/chromsci/45.10.710openalex-snapshot
Thiophilic Interaction Chromatography of Mammalian and Avian Transferrins
inferred← citeshttps://doi.org/10.1093/jee/tox321openalex-snapshot
Transferrin Family Genes in the Brown Planthopper, Nilaparvata lugens (Hemiptera: Delphacidae) in Response to Three Insecticides
inferred← citeshttps://doi.org/10.1093/ndt/gfr711openalex-snapshot
Effects of intravenous iron on mononuclear cells during the haemodialysis session
inferred← citeshttps://doi.org/10.1099/mic.0.27091-0openalex-snapshot
The novel extracellular Streptomyces reticuli haem-binding protein HbpS influences the production of the catalase-peroxidase CpeB
inferred← citeshttps://doi.org/10.1107/s1744309108008348openalex-snapshot
Crystallization and preliminary characterization of a novel haem-binding protein ofStreptomyces reticuli
inferred← citeshttps://doi.org/10.1111/1574-6968.12093openalex-snapshot
Elucidation of haem-binding sites in the actinobacterial protein HbpS
inferred← citeshttps://doi.org/10.1111/dgd.12148openalex-snapshot
Comparative biochemical analysis of the major yolk protein in the sea urchin egg and coelomic fluid
inferred← citeshttps://doi.org/10.1111/febs.12825openalex-snapshot
A structural model of human ferroportin and of its iron binding site
inferred← citeshttps://doi.org/10.1111/j.1574-6976.2012.00324.xopenalex-snapshot
Persistence ofBartonellaspp. stealth pathogens: from subclinical infections to vasoproliferative tumor formation
inferred← citeshttps://doi.org/10.1111/j.1742-4658.2006.05381.xopenalex-snapshot
Three mammalian cytochromes b561 are ascorbate‐dependent ferrireductases
inferred← citeshttps://doi.org/10.1111/j.1742-4658.2006.05609.xopenalex-snapshot
Reductive nitrosylation and peroxynitrite‐mediated oxidation of heme–hemopexin
inferred← citeshttps://doi.org/10.1111/j.1751-1097.2004.tb00081.xopenalex-snapshot
Comparison of Nonmetal and Metal Hydrophilic Photosensitizer, ATX‐S10 (Na) and ATN‐2, Binding with Human Serum Proteins Using Spectrophotometry¶
inferred← citeshttps://doi.org/10.1111/mmi.12189openalex-snapshot
The C andida glabrata sterol scavenging mechanism, mediated by the ATP ‐binding cassette transporter A us1p, is regulated by iron limitation
inferred← citeshttps://doi.org/10.1116/1.2965135openalex-snapshot
Interfacial adsorption and denaturization of human milk and recombinant rice lactoferrin
inferred← citeshttps://doi.org/10.1124/pr.57.4.3openalex-snapshot
Carbon Monoxide: Endogenous Production, Physiological Functions, and Pharmacological Applications
inferred← citeshttps://doi.org/10.1128/iai.00210-10openalex-snapshot
Antibody Targeting the Ferritin-Like Protein ControlsListeriaInfection
inferred← citeshttps://doi.org/10.1128/iai.00245-06openalex-snapshot
Environmental Signals Generate a Differential and Coordinated Expression of the Heme Receptor Gene Family of Bartonella quintana
inferred← citeshttps://doi.org/10.1128/iai.00497-07openalex-snapshot
Transcriptional Regulation of the Heme Binding Protein Gene Family of Bartonella quintana Is Accomplished by a Novel Promoter Element and Iron Response Regulator
inferred← citeshttps://doi.org/10.1128/iai.73.9.5482-5492.2005openalex-snapshot
Iron Acquisition from Transferrin by Candida albicans Depends on the Reductive Pathway
inferred← citeshttps://doi.org/10.1128/jb.01195-12openalex-snapshot
Iron-Regulated Surface Determinant (Isd) Proteins of Staphylococcus lugdunensis
inferred← citeshttps://doi.org/10.1128/jb.186.12.3903-3910.2004openalex-snapshot
Structural Basis for Iron Binding and Release by a Novel Class of Periplasmic Iron-Binding Proteins Found in Gram-Negative Pathogens
inferred← citeshttps://doi.org/10.1128/mbio.01211-25openalex-snapshot
Iron acquisition strategies in pathogenic fungi
inferred← citeshttps://doi.org/10.1128/msphere.00165-26openalex-snapshot
Iron and its import systems enhance copper accumulation in Streptococcus pneumoniae
inferred← citeshttps://doi.org/10.1134/s0006297916100059openalex-snapshot
Iron-sulfur clusters in mitochondrial metabolism: Multifaceted roles of a simple cofactor
inferred← citeshttps://doi.org/10.1139/o01-153openalex-snapshot
Lactoferrin and transferrin: Functional variations on a common structural framework
inferred← citeshttps://doi.org/10.1139/v11-019openalex-snapshot
Quadrupolar central transition (QCT) and 13C NMR competition studies of metal ion binding to ovotransferrin
inferred← citeshttps://doi.org/10.1146/annurev-micro-041222-023252openalex-snapshot
Molecular Mechanisms for Iron Uptake and Homeostasis in Marine Eukaryotic Phytoplankton
inferred← citeshttps://doi.org/10.1146/annurev.pharmtox.010909.105600openalex-snapshot
Mechanisms of Cell Protection by Heme Oxygenase-1
inferred← citeshttps://doi.org/10.1152/ajprenal.00426.2012openalex-snapshot
Renal cortical hemopexin accumulation in response to acute kidney injury
inferred← citeshttps://doi.org/10.1155/2021/6987454openalex-snapshot
Rapid Screening and Estimation of Binding Constants for Interactions of Fe3+ with Two Metalloproteins, Apotransferrin and Transferrin, Using Affinity Mode of Capillary Electrophoresis
inferred← citeshttps://doi.org/10.11606/d.46.2017.tde-21062017-091716openalex-snapshot
Conjugados de ovalbumina e albumina bovina com desferrioxamina e suas interações com íons metálicos
inferred← citeshttps://doi.org/10.11613/bm.2012.034openalex-snapshot
Iron metabolism: current facts and future decisions
inferred← citeshttps://doi.org/10.1186/1472-6750-12-92openalex-snapshot
Characterization of transferrin receptor-mediated endocytosis and cellular iron delivery of recombinant human serum transferrin from rice (Oryza sativaL.)
inferred← citeshttps://doi.org/10.1186/s12935-024-03393-3openalex-snapshot
The sensitivity of acute myeloid leukemia cells to cytarabine is increased by suppressing the expression of Heme oxygenase-1 and hypoxia-inducible factor 1-alpha
inferred← citeshttps://doi.org/10.1186/s12936-021-03827-7openalex-snapshot
Characterization of the substrate binding site of an iron detoxifying membrane transporter from Plasmodium falciparum
inferred← citeshttps://doi.org/10.1186/s12964-023-01074-8openalex-snapshot
The prognostic and therapeutic potential of HO-1 in leukemia and MDS
inferred← citeshttps://doi.org/10.1186/s40824-021-00212-yopenalex-snapshot
Bio-nano interactions: binding proteins, polysaccharides, lipids and nucleic acids onto magnetic nanoparticles
inferred← citeshttps://doi.org/10.12691/jfnr-5-1-7openalex-snapshot
Advantages of the Supplementation with both a Protein and Heme Hydrolyzate and Ionic Iron during Iron Deficiency Anemia
inferred← citeshttps://doi.org/10.13172/2052-0069-2-2-580openalex-snapshot
Plant seed-derived human transferrin: expression, characterisation and applications
inferred← citeshttps://doi.org/10.1371/journal.pbio.0000079openalex-snapshot
How Mammals Acquire and Distribute Iron Needed for Oxygen-Based Metabolism
inferred← citeshttps://doi.org/10.1371/journal.pone.0028151openalex-snapshot
Conserved and Divergent Roles of Bcr1 and CFEM Proteins in Candida parapsilosis and Candida albicans
inferred← citeshttps://doi.org/10.1371/journal.pone.0109900openalex-snapshot
Involvement of the Iron Regulatory Protein from Eisenia andrei Earthworms in the Regulation of Cellular Iron Homeostasis
inferred← citeshttps://doi.org/10.14720/aas.2018.112.1.4openalex-snapshot
Transferrin gene expression in Salmo sp.
inferred← citeshttps://doi.org/10.1515/revic-2022-0031openalex-snapshot
Iron metabolism: pathways and proteins in homeostasis
inferred← citeshttps://doi.org/10.1529/biophysj.107.114637openalex-snapshot
Exploring Transferrin-Receptor Interactions at the Single-Molecule Level
inferred← citeshttps://doi.org/10.1562/2004-03-17-ra-117openalex-snapshot
Comparison of Non-metal and Metal Hydrophilic Photosensitizer (ATX-S10 (Na) and ATN-2) Binding with Human Serum Proteins using Spectrophotometry
inferred← citeshttps://doi.org/10.1579/0044-7447(2007)36[107:mbaobe]2.0.co;2openalex-snapshot
Metal Biology: Aspects of Beneficial Effects
inferred← citeshttps://doi.org/10.1590/s2175-97902022e20942openalex-snapshot
Neuroprotective effects of sinapic acid involve the iron regulatory role on the rotenone-induced Parkinson’s disease model
inferred← citeshttps://doi.org/10.17116/repro201521625-30openalex-snapshot
The structure and functions of lactoferrin and its role in human reproduction (a review)
inferred← citeshttps://doi.org/10.18388/abp.2007_3284openalex-snapshot
Isolation and characterisation of crocodile and python ovotransferrins.
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