ReviewBiometals : an international journal on the role of metal ions in biology, biochemistry, and medicine2007
A structural comparison of human serum transferrin and human lactoferrin.
Review in Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
43 citing papers in PubMed, 117 citations in OpenAlex.
- FeBioactive materials · 2026Article
- First implementation of a polymer-polymer aqueous two-phase system to improve lateral-flow immunoassay sensitivity via dextranase integration on paper.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2026Article
- Unraveling the Serum Protein Landscape in Celiac Disease: Current Evidence and Future Directions.Immunity, inflammation and disease · 2025Review
- Article
- MAD-microbial (origin of) Alzheimer's disease hypothesis: from infection and the antimicrobial response to disruption of key copper-based systems.Frontiers in neuroscience · 2024Review
- A Proteomics Investigation of Salivary Profiles as Potential Biomarkers for Autism Spectrum Disorder (ASD).The protein journal · 2023Article
- Recent Advances of Proteomics in Management of Acute Kidney Injury.Diagnostics (Basel, Switzerland) · 2023Review
- Biomedical Applications of Lactoferrin on the Ocular Surface.Pharmaceutics · 2023Review
- The Influence of Lactoferrin in Plasma and Peritoneal Fluid on Iron Metabolism in Women with Endometriosis.International journal of molecular sciences · 2023Article
- Extraintestinal pathogenicVirulence · 2022Article
- Mechanistic Insight into the Binding of Huperzine a with Human Transferrin: Computational, Spectroscopic and Calorimetric Approaches.ACS omega · 2022Article
- High-Level Expression of Cell-Surface Signaling System Hxu Enhances Pseudomonas aeruginosa Bloodstream Infection.Infection and immunity · 2022Article
- Evaluation of the collagen-binding properties and virulence of killed Streptococcus mutans in a silkworm model.Scientific reports · 2022Article
- An Overview of Nanotechnologies for Drug Delivery to the Brain.Pharmaceutics · 2022Review
- Essentiality of Trace Elements in Pregnancy, Fertility, and Gynecologic Cancers-A State-of-the-Art Review.Nutrients · 2021Review
- Nanoparticles for Targeted Brain Drug Delivery: What Do We Know?International journal of molecular sciences · 2021Review
- Lactoferrin and Its Detection Methods: A Review.Nutrients · 2021Review
- Structural insight into the novel iron-coordination and domain interactions of transferrin-1 from a model insect, Manduca sexta.Protein science : a publication of the Protein Society · 2021Article
- Discovery of a Highly Conserved Peptide in the Iron Transporter Melanotransferrin that Traverses an Intact Blood Brain Barrier and Localizes in Neural Cells.Frontiers in neuroscience · 2021Article
- Comparison of protein profiles of the pellicle, gingival crevicular fluid, and saliva: possible origin of pellicle proteins.Biological research · 2020Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
The transferrins are a family of proteins that bind free iron in the blood and bodily fluids. Serum transferrins function to deliver iron to cells via a receptor-mediated endocytotic process as well as to remove toxic free iron from the blood and to provide an anti-bacterial, low-iron environment. Lactoferrins (found in bodily secretions such as milk) are only known to have an anti-bacterial function, via their ability to tightly bind free iron even at low pH, and have no known transport function. Though these proteins keep the level of free iron low, pathogenic bacteria are able to thrive by obtaining iron from their host via expression of outer membrane proteins that can bind to and remove iron from host proteins, including both serum transferrin and lactoferrin. Furthermore, even though human serum transferrin and lactoferrin are quite similar in sequence and structure, and coordinate iron in the same manner, they differ in their affinities for iron as well as their receptor binding properties: the human transferrin receptor only binds serum transferrin, and two distinct bacterial transport systems are used to capture iron from serum transferrin and lactoferrin. Comparison of the recently solved crystal structure of iron-free human serum transferrin to that of human lactoferrin provides insight into these differences.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.