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Publications using kDalton

Below is a  list of publications in which kDalton has been used (24 known), in reverse order by publication year. If you publish data analyzed with kDalton  please send the citation to John Philo.

  1. Casey, J. S., Walker, A. R., Zhai, X., Garno, J. C., Russo, P. S., and Maverick, A. W. (2024). Structural Information on Supramolecular Copper(II) beta-Diketonate Complexes from Atomic Force Microscopy and Analytical Ultracentrifugation. ACS omega. 9, 2629-2638.[free full text]
  2. Philo JS, Sydor W, Arakawa T (2020). The Glucagon-Like Peptide 2 Analog Teduglutide Reversibly Associates to Form Pentamers. J. Pharm. Sci. 109, 775-84 [free PDF]
  3. Zhou, X. X., Fan, L. Z., Li, P., Shen, K., and Lin, M. Z. (2017). Optical control of cell signaling by single-chain photoswitchable kinases. Science 355, 836-842. [free full text]
  4. Ogawa, H., Qiu, Y., Philo, J. S., Arakawa, T., Ogata, C. M., and Misono, K. S. (2010). Reversibly bound chloride in the atrial natriuretic peptide receptor hormone-binding domain: Possible allosteric regulation and a conserved structural motif for the chloride-binding site. Protein Sci. 19, 544-557. [free PDF]
  5. Dey, S., Hu, Z., Xu, X. L., Sacchettini, J. C., and Grant, G. A. (2007). The effect of hinge mutations on effector binding and domain rotation in Escherichia coli D-3-phosphoglycerate dehydrogenase. J. Biol. Chem. 282, 18418-18426.
  6. Gao, X. and Harris, T. K. (2006). Role of the PH domain in regulating in vitro autophosphorylation events required for reconstitution of PDK1 catalytic activity. Bioorg. Chem. 34, 200-223.
  7. Carulla, N., Woodward, C., and Barany, G. (2002). BetaCore, a designed water soluble four-stranded antiparallel b-sheet protein. Protein Sci. 11, 1539-1551.
  8. Li, T. S., Yamane, H., Arakawa, T., Narhi, L. O., and Philo, J. S. (2002). Effect of the intermolecular disulfide bond on the conformation and stability of glial cell line-derived neurotrophic factor. Proteins 15, 59-64.[free PDF]

  9. Philo, J. S. (2000). Sedimentation equilibrium analysis of mixed associations using numerical constraints to impose mass or signal conservation. Methods Enzymol. 321, 100-120.

  10. Hsu, Y. R., Nybo, R., Sullivan, J. K., Costigan, V., Spahr, C. S., Wong, C., Jones, M., Pentzer, A. G., Crouse, J. A., Pacifici, R. E., Lu, H. S., Morris, C. F., and Philo, J. S. (1999). Heparin is essential for a single keratinocyte growth factor molecule to bind and form a complex with two molecules of the extracellular domain of its receptor. Biochemistry 38, 2523-2534.[abstract]

  11. Horan, T. P., Martin, F., Simonet, L., Arakawa, T., and Philo, J. S. (1997). Dimerization of granulocyte-colony stimulating factor receptor: the Ig plus CRH construct of granulocyte-colony stimulating factor receptor forms a 2:2 complex with a ligand. J. Biochem. (Tokyo) 121, 370-375.[free PDF]

  12. Hsu, Y. R., Wu, G. M., Mendiaz, E. A., Syed, R., Wypych, J., Toso, R., Mann, M. B., Boone, T. C., Narhi, L. O., Lu, H. S., and Langley, K. E. (1997). The majority of stem cell factor exists as monomer under physiological conditions. J. Biol. Chem. 272, 6406-6415. [free full text}
  13. Narhi, L. O., Rosenfeld, R., Shimamoto, G., Lee, R., Hawkins, N., Li, T. S., Philo, J. S., Wen, J., and Arakawa, T. (1997). Comparison of solution properties of human and rat ciliary neurotrophic factor. J. Peptide Res. 50, 300-309.[abstract]

  14. Philo, J. S., Aoki, K. H., Arakawa, T., Narhi, L. O., and Wen, J. (1996). Dimerization of the extracellular domain of the erythropoietin (EPO) receptor by EPO: One high-affinity and one low-affinity interaction. Biochemistry 35, 1681-1691. [abstract]

  15. Horan, T. P., Wen, J., Narhi, L. O., Parker, V., Garcia, A., Arakawa, T., and Philo, J. S. (1996). Dimerization of the extracellular domain of granulocyte-colony stimulating factor receptor by ligand binding: A monovalent ligand induces 2:2 complexes. Biochemistry 35, 4886-4896.[abstract]

  16. Philo, J. S., Wen, J., Wypych, J., Schwartz, M. G., Mendiaz, E. A., and Langley, K. E. (1996). Human stem cell factor dimer forms a complex with two molecules of the extracellular domain of its receptor, Kit. J. Biol. Chem. 271, 6895-6902.[free PDF}

  17. Arakawa, T., Li, T. S., Philo, J. S., Narhi, L. O., Horan, T. P., and Osslund, T. D. (1996). Characterization of granulocyte-colony stimulating factor: structure and interactions with its receptor. EOS J. Immunol. Immunopharmacol. 16, 35-40.
  18. Hill, J. S., Davis, R. C., Yang, D., Wen, J., Philo, J. S., Poon, P. H., Phillips, M. L., Kempner, E. S., and Wong, H. (1996). Human hepatic lipase subunit structure determination. J. Biol. Chem. 271, 22931-22936.[free PDF]
  19. Narhi, L. O., Philo, J. S., Li, T. S., Zhang, M., Samal, B., and Arakawa, T. (1996). Induction of a-helix in the b-sheet protein tumor necrosis factor-a: Acid-induced denaturation. Biochemistry 35, 11454-11460.[abstract]

  20. Horan, T. P., Wen, J., Arakawa, T., Liu, N., Brankow, D., Hu, S., Ratzkin, B., and Philo, J. S. (1995). Binding of Neu differentiation factor with the extracellular domain of Her2 and Her3. J. Biol. Chem. 270, 24604-24608.[free PDF]

  21. Lu, H. S., Chang, D., Philo, J. S., Zhang, K., Narhi, L. O., Liu, N. L., Zhang, M., Sun, J. L., Wen, J., Yanagihara, D., Karunagaran, D., Yarden, Y., and Ratzkin, B. (1995). Studies on the structure and function of glycosylated and nonglycosylated neu differentiation factors - similarities and differences of the alpha-isoform and beta-isoform. J. Biol. Chem. 270, 4784-4791.[free PDF]

  22. Philo, J. S., Talvenheimo, J., Wen, J., Rosenfeld, R., Welcher, A. A., and Arakawa, T. (1994). Interactions of neurotrophin-3 (NT-3), brain-derived neurotrophic factor (BDNF), and the NT-3/BDNF heterodimer with the extracellular domains of the TrkB and TrkC receptors. J. Biol. Chem. 269, 27840-27846.[free PDF]

  23. Arakawa, T., Haniu, M., Narhi, L. O., Miller, J. A., Talvenheimo, J., Philo, J. S., Chute, H. T., Matheson, C., Carnahan, J., Louis, J.-C., Yan, Q., Welcher, A. A., and Rosenfeld, R. (1994). Formation of heterodimers from 3 neurotrophins, nerve growth- factor, neurotrophin-3, and brain-derived neurotrophic factor. J. Biol. Chem. 269, 27833-27839.[free PDF]
  24. Rosenfeld, R., Philo, J. S., Haniu, M., Stoney, K., Rohde, M. F., Wu, G.-M., Narhi, L. O., Wong, C., Boone, T., Hawkins, N. N., Miller, J. M., and Arakawa, T. (1993). Sites of iodination in recombinant human brain-derived neurotrophic factor and its effect on neurotrophic activity. Protein Sci. 2, 1664-1674. [free PDF]