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1. Transferrin, biochemistry, physiology and clinical significance
by Morgan, E. H
1981, ISBN 9780080279923, Volume 4, no. 1, 123
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2. Full Text SUN-P251: Do Soluble Transferrin Receptor Levels Increase in Metabolic Syndrome?
by Kaner, G and Seremet Kürklü, N
Clinical Nutrition, ISSN 0261-5614, 09/2017, Volume 36, pp. S146 - S147
Transferrin
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3. Full Text Structural basis for iron piracy by pathogenic Neisseria
by Noinaj, Nicholas and Easley, Nicole C and Oke, Muse and Mizuno, Naoko and Gumbart, James and Boura, Evzen and Steere, Ashley N and Zak, Olga and Aisen, Philip and Tajkhorshid, Emad and Evans, Robert W and Gorringe, Andrew R and Mason, Anne B and Steven, Alasdair C and Buchanan, Susan K
Nature, ISSN 0028-0836, 03/2012, Volume 483, Issue 7387, pp. 53 - 61
Neisseria are obligate human pathogens causing bacterial meningitis, septicaemia and gonorrhoea. Neisseria require iron for survival and can extract it... 
ANTIBODIES | MOLECULAR-DYNAMICS | C-LOBE | MULTIDISCIPLINARY SCIENCES | BINDING PROTEIN-B | X-RAY | RECEPTOR | MENINGITIDIS | IDENTIFICATION | SCATTERING | HUMAN SERUM TRANSFERRIN | Apoproteins - chemistry | Transferrin-Binding Protein A - ultrastructure | Transferrin-Binding Protein B - metabolism | Species Specificity | Humans | Transferrin-Binding Protein A - metabolism | Bacterial Proteins - chemistry | Crystallography, X-Ray | Structure-Activity Relationship | Transferrin-Binding Protein B - ultrastructure | Biological Transport | Cattle | X-Ray Diffraction | Binding Sites | Apoproteins - metabolism | Models, Molecular | Scattering, Small Angle | Iron - metabolism | Molecular Dynamics Simulation | Animals | Neisseria - metabolism | Transferrin - ultrastructure | Neisseria - pathogenicity | Transferrin - chemistry | Transferrin-Binding Protein A - chemistry | Bacterial Proteins - metabolism | Protein Conformation | Bacterial Proteins - ultrastructure | Mice | Transferrin - metabolism | Transferrin-Binding Protein B - chemistry | Proteins | Transferrin | Neisseriaceae | Iron in the body | Research | Binding proteins | Properties | Structure | Health aspects | Bacteria | Vaccines | Mortality
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4. Full Text Determination of the diagnostic cut-off for fecal transferrin, and examination of its temperature stability in feces, and following sampling for fecal immunochemical testing (FIT) by the NS-Prime analyzer system
by Randell, Edward and Demian, Wael and Collins, Stacy and Fowler, Candace and McGrath, Jerry and Hollohan, Deborah and Lacey, Suzanne and Banoub, Joseph
Clinical Biochemistry, ISSN 0009-9120, 10/2015, Volume 48, Issue 15, pp. 1009 - 1009
Transferrin
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5. Full Text Transferrin/transferrin receptor‐mediated drug delivery
by Li, Hongyan and Qian, Zhong Ming
Medicinal Research Reviews, ISSN 0198-6325, 05/2002, Volume 22, Issue 3, pp. 225 - 250
Since transferrin was discovered more than half a century ago, a considerable effort has been made towards understanding tranferrin‐mediated iron uptake.... 
gene delivery | transferrin | transferrin receptor | drug delivery | Gene delivery | Transferrin | Drug delivery | Transferrin receptor | HUMAN-LEUKEMIC-CELLS | CHEMISTRY, MEDICINAL | HUMAN-SERUM TRANSFERRIN | DNA/TRANSFERRIN-PEI COMPLEXES | HEMOCHROMATOSIS PROTEIN HFE | BLOOD-BRAIN-BARRIER | MITOMYCIN-C CONJUGATE | NERVE GROWTH-FACTOR | TERMINAL HALF-MOLECULE | AMINO-ACID-SEQUENCE | PHARMACOLOGY & PHARMACY | IRON-RESPONSIVE ELEMENT | Humans | Transferrin - physiology | Iron - metabolism | Receptors, Transferrin - metabolism | Transferrin - genetics | Drug Delivery Systems | Endocytosis - physiology | Animals | Transferrin - chemistry | Receptors, Transferrin - physiology | Protein Conformation | Receptors, Transferrin - genetics | Transferrin - metabolism | Receptors, Transferrin - chemistry
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6. Full Text Corrigendum to "Serum soluble transferrin receptor concentrations are increased in central obesity. Results from a screening programme for hereditary hemochromatosis in men with hyperferritinemia" [Clin Chim Acta 400 111-116]
Clinica Chimica Acta, ISSN 0009-8981, 09/2014, Volume 436, p. 351
Transferrin
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7. Full Text Targeted Drug Delivery via the Transferrin Receptor-Mediated Endocytosis Pathway
by Zhong Ming Qian and Hongyan Li and Hongzhe Sun and Kwokping Ho
Pharmacological Reviews, ISSN 0031-6997, 12/2002, Volume 54, Issue 4, pp. 561 - 587
The membrane transferrin receptor-mediated endocytosis or internalization of the complex of transferrin bound iron and the transferrin receptor is the major... 
TERMINAL HALF-MOLECULE | DNA/TRANSFERRIN-PEI COMPLEXES | HEMOCHROMATOSIS PROTEIN HFE | PHARMACOLOGY & PHARMACY | IRON-RESPONSIVE ELEMENT | STRENUOUSLY EXERCISED RATS | BLOOD-BRAIN-BARRIER | MITOMYCIN-C CONJUGATE | POLYLYSINE DNA COMPLEXES | NONVIRAL GENE DELIVERY | HUMAN SERUM TRANSFERRIN | Brain - metabolism | Animals | Humans | Transferrin - chemistry | Receptors, Transferrin - physiology | Transferrin - physiology | Pharmaceutical Preparations - administration & dosage | Transferrin - metabolism | Receptors, Transferrin - metabolism | Drug Delivery Systems | Endocytosis - physiology | Receptors, Transferrin - chemistry
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8. Full Text Escape from bacterial iron piracy through rapid evolution of transferrin
by Barber, Matthew F and Elde, Nels C
Science, ISSN 0036-8075, 12/2014, Volume 346, Issue 6215, pp. 1362 - 1366
Can a single conversation change minds on divisive social issues, such as same-sex marriage? A randomized placebo-controlled trial assessed whether gay (n =... 
NUTRITIONAL IMMUNITY | PROTEIN | STRUCTURAL BASIS | LACTOFERRIN | MULTIDISCIPLINARY SCIENCES | NEISSERIA-MENINGITIDIS | DISEASE | INFECTION | RECEPTORS | BINDING | ASSOCIATION | Neisseria meningitidis - metabolism | Humans | Transferrin-Binding Protein A - metabolism | Molecular Sequence Data | Phylogeny | Transferrin - genetics | Haplorhini - immunology | Amino Acid Sequence | Haemophilus influenzae - metabolism | Selection, Genetic | Models, Molecular | Haplorhini - metabolism | Immunity, Innate | Polymorphism, Genetic | Transferrin-Binding Protein A - genetics | Animals | Neisseria - metabolism | Transferrin - chemistry | Protein Binding | Transferrin-Binding Protein A - chemistry | Neisseria gonorrhoeae - metabolism | Transferrin - metabolism | Haplorhini - genetics | Amino Acid Substitution | Evolution, Molecular | Host-bacteria relationships | Protein research | Transferrin | Immune response | Iron in the body | Research | Health aspects | Immunological research | Iron | Bacterial infections | Immune system | Binding | Pathogens | Evolutionary | Bacteria | Evolution | Piracy
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9. Iron in biochemistry and medicine, II
by Jacobs, A and Worwood, M
1980, ISBN 012378980X, xiii, 706
Iron -- Metabolism | Iron in the body
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10. Full Text How the binding of human transferrin primes the transferrin receptor potentiating iron release at endosomal pH
by Brian E. Eckenroth and Ashley N. Steere and N. Dennis Chasteen and Stephen J. Everse and Anne B. Mason and BROOKHAVEN NATIONAL LABORATORY (BNL)
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2011, Volume 108, Issue 32, pp. 13089 - 13094
Delivery of iron to cells requires binding of two iron-containing human transferrin (hTF) molecules to the specific homodimeric transferrin receptor (TFR) on... 
Transferrins | Receptors | Hydrogen bonds | Iron | Biochemistry | Dimers | Kinetics | Monomers | Transferrin receptors | Crystal structure | C-LOBE | N-LOBE | METABOLISM | MECHANISM | RECOGNITION | CRYSTAL-STRUCTURE | MOLECULAR CONTROL | MULTIDISCIPLINARY SCIENCES | PROVIDES INSIGHT | SOFTWARE | HUMAN SERUM TRANSFERRIN | Protein Structure, Tertiary | Humans | Models, Molecular | Iron - metabolism | Receptors, Transferrin - metabolism | Endosomes - metabolism | Amino Acid Motifs | Endocytosis | Transferrin - chemistry | Protein Binding | Transferrin - metabolism | Binding Sites | Hydrogen-Ion Concentration | Receptors, Transferrin - chemistry | Physiological aspects | Transferrin | Cell receptors | Research | Index Medicus | MUTAGENESIS | TRANSFERRIN | BASIC BIOLOGICAL SCIENCES | KINETICS | RESOLUTION | CRYSTAL STRUCTURE | TARGETS | IRON | DIMERS | 60 APPLIED LIFE SCIENCES | CONFORMATIONAL CHANGES | iron metabolism | iron release kinetics | protein–protein interactions | Biological Sciences
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11. Full Text Pooled analysis of iron-related genes in Parkinson's disease: Association with transferrin
by Rhodes, Shannon L and Buchanan, Daniel D and Ahmed, Ismaïl and Taylor, Kent D and Loriot, Marie-Anne and Sinsheimer, Janet S and Bronstein, Jeff M and Elbaz, Alexis and Mellick, George D and Rotter, Jerome I and Ritz, Beate
Neurobiology of Disease, ISSN 0969-9961, 2013, Volume 62, pp. 172 - 178
Abstract Pathologic features of Parkinson's disease (PD) include death of dopaminergic neurons in the substantia nigra, presence of α-synuclein containing Lewy... 
Neurology | Iron homeostasis | Pooled-analysis | Genetics | Transferrin | Epidemiology | Transferrin receptor 2 | OXIDATIVE STRESS | G277S MUTATION | HFE | NEURODEGENERATION | ALPHA-SYNUCLEIN | SUBSTANTIA-NIGRA | PARAQUAT | NEUROSCIENCES | ENVIRONMENTAL RISK-FACTORS | EXPOSURE | BRAIN IRON | Genetic Association Studies | Humans | Middle Aged | Male | Parkinson Disease - genetics | Iron - metabolism | Transferrin - genetics | Case-Control Studies | Young Adult | Adolescent | Adult | Female | Aged | Parkinson Disease - metabolism | Polymorphism, Single Nucleotide | Receptors, Transferrin - genetics | Genetic research | Iron | Analysis | Genes | Receptors, Transferrin | Parkinson Disease | Life Sciences | Santé publique et épidémiologie
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12. Full Text Kinetics of iron release from transferrin bound to the transferrin receptor at endosomal pH
by Steere, Ashley N and Byrne, Shaina L and Chasteen, N. Dennis and Mason, Anne B
BBA - General Subjects, ISSN 0304-4165, 03/2012, Volume 1820, Issue 3, pp. 326 - 333
Human serum transferrin (hTF) is a bilobal glycoprotein that reversibly binds Fe and delivers it to cells by the process of receptor-mediated endocytosis.... 
Fluorescence | Transferrin | Kinetics | Transferrin receptor | NITRILOTRIS(METHYLENEPHOSPHONIC ACID) | C-LOBE | HUMAN-SERUM TRANSFERRIN | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | N-LOBE | CONFORMATIONAL-CHANGE | BIOPHYSICS | TERMINAL MONOFERRIC TRANSFERRIN | BINDING-SITES | DIFERRIC TRANSFERRIN | ANION-BINDING | Endocytosis | Biological Transport | Humans | Protein Conformation | Transferrin - metabolism | Iron - metabolism | Receptors, Transferrin - metabolism | Endosomes - metabolism | Hydrogen-Ion Concentration | Receptors, Transferrin - chemistry | Iron
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13. Full Text Cryo-EM structure of an essential Plasmodium vivax invasion complex
by Gruszczyk, Jakub and Huang, Rick K and Chan, Li-Jin and Menant, Sébastien and Hong, Chuan and Murphy, James M and Mok, Yee-Foong and Griffin, Michael D. W and Pearson, Richard D and Wong, Wilson and Cowman, Alan F and Yu, Zhiheng and Tham, Wai-Hong
Nature, ISSN 0028-0836, 07/2018, Volume 559, Issue 7712, pp. 135 - 139
Plasmodium vivax is the most widely distributed malaria parasite that infects humans(1). P. vivax invades reticulocytes exclusively, and successful entry... 
RECEPTOR 1 | KNOWLESI | SUITE | RECOGNITION | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | VALIDATION | MALARIA | ERYTHROCYTE INVASION | Plasmodium vivax - ultrastructure | Protozoan Proteins - antagonists & inhibitors | Humans | Plasmodium vivax - genetics | Structure-Activity Relationship | Protozoan Proteins - genetics | Antigens, CD - genetics | Antigens, CD - metabolism | Malaria Vaccines - immunology | Protozoan Proteins - chemistry | Antigens, CD - chemistry | Receptors, Transferrin - genetics | Binding Sites | Antibodies, Monoclonal - immunology | Plasmodium vivax - chemistry | Antibodies, Monoclonal - pharmacology | Models, Molecular | Receptors, Transferrin - ultrastructure | Reticulocytes - metabolism | Receptors, Transferrin - metabolism | Cryoelectron Microscopy | Transferrin - ultrastructure | Transferrin - chemistry | Protozoan Proteins - ultrastructure | Mutation | Transferrin - metabolism | Antigens, CD - ultrastructure | Plasmodium vivax - cytology | Receptors, Transferrin - chemistry | Monoclonal antibodies | Physiological aspects | Plasmodium vivax | Models | Malaria | Protein binding | Plasmodium falciparum | Analysis | Vector-borne diseases | Antigens | Transferrin | Complex formation | Host specificity | Iron | Reticulocytes | Parasites | Epitopes | Electron microscopy | Erythroid cells | Molecular chains | Proteins | Microscopy | Reticulocyte-binding protein | Cellular structure | Crystal structure
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14. Full Text Inflammation-induced iron transport and metabolism by brain microglia
by McCarthy, Ryan C and Sosa, Jose Carlo and Gardeck, Andrew M and Baez, Andrew S and Lee, Chih-Hao and Wessling-Resnick, Marianne
Journal of Biological Chemistry, ISSN 0021-9258, 2018, Volume 293, Issue 20, pp. 7853 - 7863
Microglia are immune cells of the central nervous system and are implicated in brain inflammation. However, how brain microglia modulate transport and... 
CELLS | BIOCHEMISTRY & MOLECULAR BIOLOGY | HEPCIDIN | ACCUMULATION | CHAPERONE | RESPONSIVE ELEMENTS | EXPRESSION | Microglia - metabolism | Heme Oxygenase-1 - metabolism | Amyloid beta-Peptides - pharmacology | Glycolysis - drug effects | Transferrin - genetics | Brain - metabolism | Glycolysis - genetics | Oxidative Phosphorylation - drug effects | Heme Oxygenase-1 - genetics | Ferritins - metabolism |