Crystal Structure of the Ectodomain of Human Transferrin Receptor

[20] Processing of X-ray diffraction data collected in oscillation mode

Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475

The CCP4 suite: programs for protein crystallography

Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,317

NMRPipe: A multidimensional spectral processing system based on UNIX pipes

Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., & Bax, A. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00197809 · Cited by 15,961

Improved methods for building protein models in electron density maps and the location of errors in these models

Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,616

Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons

Nicholls, A. O., Sharp, K. A., & Honig, B. H. (1991) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340110407 · Cited by 5,230

Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme

Andersson, S., Davis, D. L., Dahlbäck, H., Jörnvall, H., & Russell, D. W. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83172-6 · Cited by 1,229

The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells

Richardson, D. R., & Ponka, P. (1997) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/s0304-4157(96)00014-7 · Cited by 714

Crystal Structure of the Hemochromatosis Protein HFE and Characterization of Its Interaction with Transferrin Receptor

Lebrón, J. A., Bennett, M. J., Vaughn, D. E., Chirino, A. J., Snow, P. M., Mintier, G. A., Feder, J. N., & Björkman, P. J. (1998) · Cell · doi:10.1016/s0092-8674(00)81151-4 · Cited by 639

Structure of human lactoferrin: Crystallographic structure analysis and refinement at 2·8 Å resolution

Anderson, B. F., Baker, H. M., Norris, G. E., Rice, D. W., & Baker, E. N. (1989) · Journal of Molecular Biology · doi:10.1016/0022-2836(89)90602-5 · Cited by 597

Prostate-specific membrane antigen is a hydrolase with substrate and pharmacologic characteristics of a neuropeptidase.

Carter, R., Feldman, A., & Coyle, J. T. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.2.749 · Cited by 374

Molecular structure of serum transferrin at 3.3-.ANG. resolution

Bailey, S., Evans, R. W., Garratt, R. C., Gorinsky, B. A., Hasnain, S. S., Horsburgh, C., Jhoti, H., Lindley, P. F., & Mydin, A. (1988) · Biochemistry · doi:10.1021/bi00415a061 · Cited by 365

Apolactoferrin structure demonstrates ligand-induced conformational change in transferrins

Andersen, B. F., Baker, H. M., Morris, G. E., Rumball, S. V., & Baker, E. N. (1990) · Nature · doi:10.1038/344784a0 · Cited by 363

Primary structure of human transferrin receptor deduced from the mRNA sequence

Schneider, C., Owen, M. J., Banville, D. L., & Williams, J. G. (1984) · Nature · doi:10.1038/311675b0 · Cited by 347

The human transferrin receptor gene: genomic organization, and the complete primary structure of the receptor deduced from a cDNA sequence

McClelland, A., Kühn, L. C., & Ruddle, F. H. (1984) · Cell · doi:10.1016/0092-8674(84)90004-7 · Cited by 342

Association of the transferrin receptor in human placenta with HFE, the protein defective in hereditary hemochromatosis

Parkkila, S., Waheed, A., Britton, R. S., Bacon, B. R., Zhou, X. Y., Tomatsu, S., Fleming, R. E., & Sly, W. S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.24.13198 · Cited by 336

Identification of the intermolecular disulfide bonds of the human transferrin receptor and its lipid‐attachment site.

Jing, S. Q., & Trowbridge, I. S. (1987) · The EMBO Journal · doi:10.1002/j.1460-2075.1987.tb04758.x · Cited by 207

The Hereditary Hemochromatosis Protein, HFE, Specifically Regulates Transferrin-mediated Iron Uptake in HeLa Cells

Roy, C. N., Penny, D. M., Feder, J. N., & Enns, C. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.13.9022 · Cited by 203

The structure of aconitase

Robbins, A. H., & Stout, C. D. (1989) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340050406 · Cited by 189

A new role for the transferrin receptor in the release of iron from transferrin

Bali, P. K., Zak, O., & Aisen, P. (1991) · Biochemistry · doi:10.1021/bi00216a003 · Cited by 182

Ligand-Induced Conformational Change in Transferrins: Crystal Structure of the Open Form of the N-Terminal Half-Molecule of Human Transferrin,

Jeffrey, P. D., Bewley, M. C., MacGillivray, R. T. A., Mason, A. B., Woodworth, R. C., & Baker, E. N. (1998) · Biochemistry · doi:10.1021/bi9812064 · Cited by 166

Algorithm for ribbon models of proteins

Carson, M., & Bugg, C. E. (1986) · Journal of Molecular Graphics · doi:10.1016/0263-7855(86)80010-8 · Cited by 143

The Structure of the Aeromonas proteolytica Aminopeptidase Complexed with a Hydroxamate Inhibitor

Chevrier, B., d'Orchymont, H., Schalk, C., Tarnus, C., & Moras, D. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0393k.x · Cited by 139

Binding to cellular receptors results in increased iron release from transferrin at mildly acidic pH

Sipe, D. M., & Murphy, R. F. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)92931-5 · Cited by 122

A high yield purification of the human transferrin receptor and properties of its major extracellular fragment.

Turkewitz, A. P., Amatruda, J. F., Borhani, D. W., Harrison, S. C., & Schwartz, A. L. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68479-0 · Cited by 111

Structure of membrane glutamate carboxypeptidase

Rawlings, N. D., & Barrett, A. J. (1997) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(97)00008-3 · Cited by 93

Expression of glycosylated and nonglycosylated human transferrin in mammalian cells. Characterization of the recombinant proteins with comparison to three commercially available transferrins

Mason, A. B., Miller, M. K., Funk, W. D., Banfield, D. K., Savage, K. J. J., Oliver, R. W. A., Green, B. N., MacGillivray, R. T. A., & Woodworth, R. C. (1993) · Biochemistry · doi:10.1021/bi00071a025 · Cited by 91

Molecular Cloning of a Peptidase Against N‐Acetylaspartylglutamate from a Rat Hippocampal cDNA Library

Bzdega, T., Turi, T. G., Wróblewska, B., She, D., Chung, H. S., Kim, H., & Neale, J. H. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69062270.x · Cited by 84

Isolation and expression of a rat brain cDNA encoding glutamate carboxypeptidase II

Luthi‐Carter, R., Berger, U. V., Barczak, A. K., Enna, M., & Coyle, J. T. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.6.3215 · Cited by 73

Primary receptor-recognition site of human transferrin is in the C-terminal lobe.

Zak, O., Trinder, D., & Aisen, P. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37254-x · Cited by 64

Elimination of the O-linked glycosylation site at Thr 104 results in the generation of a soluble human-transferrin receptor

Rutledge, E. A., Root, B., Lucas, J., & Enns, C. (1994) · Blood · doi:10.1182/blood.v83.2.580.bloodjournal832580 · Cited by 62

Transferrin uptake and release by reticulocytes treated with proteolytic enzymes and neuraminidase

Hemmaplardh, D., & Morgan, E. H. (1976) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(76)90384-9 · Cited by 61

Structural model of phospholipid-reconstituted human transferrin receptor derived by electron microscopy

Fuchs, H., Lücken, U., Tauber, R., Engel, A. H., & Gessner, R. V. (1998) · Structure · doi:10.1016/s0969-2126(98)00124-5 · Cited by 57

Effects of structural modifications on the biologic activity of human transferrin

Kornfeld, S. (1968) · Biochemistry · doi:10.1021/bi00843a010 · Cited by 56

A region of the C-terminal portion of the human transferrin receptor contains an asparagine-linked glycosylation site critical for receptor structure and function

Williams, A. M., & Enns, C. A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31456-x · Cited by 41

Intermolecular disulfide bonds are not required for the expression of the dimeric state and functional activity of the transferrin receptor.

Alvarez, E., Gironès, N., & Davis, R. J. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb08347.x · Cited by 38

Functional Analysis of Human/Chicken Transferrin Receptor Chimeras Indicates that the Carboxy‐Terminal Region is Important for Ligand Binding

Buchegger, F., Trowbridge, I. S., Liu, L. S., White, S., & Collawn, J. F. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0009u.x · Cited by 37

Crystallization and X-ray diffraction studies of a soluble form of the human transferrin receptor

Borhani, D. W., & Harrison, S. C. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90255-5 · Cited by 27

Expression of gratitude

Mason, D. T. (1996) · The American Journal of Cardiology · doi:10.1016/s0002-9149(97)89410-6 · Cited by 3

Targeted Drug Delivery via the Transferrin Receptor-Mediated Endocytosis Pathway

Qian, Z., Li, H., Sun, H., & Ho, K. (2002) · Pharmacological Reviews · doi:10.1124/pr.54.4.561 · Cited by 1,035

The roles of iron in health and disease

Lieu, P. T., Heiskala, M. K., Peterson, P. A., & Yang, Y. M. (2001) · Molecular Aspects of Medicine · doi:10.1016/s0098-2997(00)00006-6 · Cited by 829

Chemistry and biology of eukaryotic iron metabolism

Aisen, P. (2001) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(01)00063-2 · Cited by 804

Transferrin and transferrin receptors update

Kawabata, H. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.06.037 · Cited by 719

The transferrin receptor part I: Biology and targeting with cytotoxic antibodies for the treatment of cancer

Daniels‐Wells, T. R., Delgado, T., Rodríguez, J. A., Helguera, G. F., & Penichet, M. L. (2006) · Clinical Immunology · doi:10.1016/j.clim.2006.06.010 · Cited by 646

Structural model of phospholipid-reconstituted human transferrin receptor derived by electron microscopy

Fuchs, H., Lücken, U., Tauber, R., Engel, A. H., & Gessner, R. V. (1998) · Structure · doi:10.1016/s0969-2126(98)00124-5 · Cited by 57

Structure of the human transferrin receptor-transferrin complex

Cheng, Y., Zak, O., Aisen, P., Harrison, S. C., & Walz, T. (2004) · Cell · doi:10.1016/s0092-8674(04)00130-8 · Cited by 571

How the binding of human transferrin primes the transferrin receptor potentiating iron release at endosomal pH

Eckenroth, B. E., Steere, A. N., Chasteen, N. D., Everse, S. J., & Mason, A. B. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1105786108 · Cited by 160

Structure Watch

(2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1379

Mysteries of the Transferrin-Transferrin Receptor 1 Interaction Uncovered

Richardson, D. R. (2004) · Cell · doi:10.1016/s0092-8674(04)00165-5 · Cited by 37