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David M. Jameson, Ph.D.

Professor of Cell and Molecular Biology

University of Hawai’i at Manoa

John A. Burns School of Medicine

651 Ilalo Street, BSB 222

Honolulu, HI 96813 USA

Tel:     808-956-8332
Fax:    808-692-1968

Email :


Pubmed Link 



Our laboratory utilizes fluorescence methodologies to elucidate dynamic aspects of biomolecules.  We are currently studying dynamin, a large (98kDa) GTPase which functions to “pinch-off” membrane vesicles in pathways such as receptor mediated endocytosis and synaptic vesicle recycling.  We carry out both in vitro and in vivo studies on the self-association modes of dynamin as well as its interaction with membranes and other proteins such as endophilin Arc/Arg3.1.  We also have a project on Botulinum Neurotoxin which involves biophysical studies on proteins forming the neurotoxin complex as well as development of in vitro and in vivo toxin assays based on Fluorescence Fluctuation Spectroscopy.


Steady-state and time-resolved fluorescence

Two-Photon Fluorescence Microscopy; FCS, FLIM


Jameson, D.M. and Ross, J.A. (2010) Chem. Rev. 110:2685-2708. Fluorescence Polarization/Anisotropy in Clinical Diagnostics and Imaging.

Wang, L., Barylko, B., Byers, C., Ross, A. J., Jameson, D. M. and Albanesi, J. P. (2010) Chem. 285:22753-22757. Dynamin 2 mutants linked to centronuclear myopathies form abnormally stable polymers.

Barylko, B., Wnag L., Binns, D.D.., Ross, J. A.., Tassin T., Collins, K., Jameson, D.M. and Albanesi, J. P. (2010) Biochemistry 49:10592-10594.  The Proline-Arginine Rich Domain (PRD) is a major Determinant of Dynamin Self-Activation.

Stefl, M., James, N. G., Ross, J. A. and Jameson, D.M. (2011) Anal. Biochem. 410:62-69. Application of Phasor to In Vitro Time-Resolved Fluorescence Measurements.

James, N.G., Ross, J.A., Stefl, M. and Jameson, D. M. (2011) Anal. Biochem. 410:70-76. Application of Phasor Plots to In Vitro Protein Studies.

Ross, J. A., Digman, M. A., Gratton, E., Albanesi, J. P. and Jameson, D. M. Biophysical J.(in Press) Oligomerization State of Dynamin 2 in Cell Membranes Using TIRF and Number and Brightness Analysis.

Ross, J. A., Chen, Y., Mueller, J.,Barylko, B., Wang, L., Banks, H. B., Albanesi, J. P. and Jameson, D.M. Biophysical J.  Dimeric Endophilin A2 Stimulates Assembly and GTPase Activity of Dynamin 2. Biophys J. 2011 Feb 2;100(3):729-37.

Ross, J.A., Gilmore, M.A., Williams, D., Aoki, K.R., Steward, L.E. and Jameson, D. M. (2011) Analy. Biochem. 433:36-42. Characterization of Forster resonance energy transfer in a botulinum neurotoxin protease assay.

Gilmore, M.A., Williams, D., Okawa, Y., Holguin, B., James, N.G., Ross, J.A., Aoki, R.K., Jameson, D. M. and Steward, L.E. (2011) Anal. Biochem. 433:43-49.  Depolarization after resonance energy transfer (DARET): A sensitive fluoresence-based assay for botulinum neurotoxin protease activity.

Buscaglia R, Jameson DM, Chaires JB. G-quadruplex structure and stability illuminated by 2-aminopurine phasor plots. Nucleric Acids Res. 2012 May;40(9):4203-15.

James NG, Digman MA, Gratton E, Barylko B, Ding X, Albanesi JP, Goldberg MS, Jameson DM. Number and brightness analysis of LRRK oligomerization in live cells. Biophys J. 2012 Jun 6;102(11):L41-3.

Montecinos-Franjola F, Ross JA, Sanchez SA, Brunet JE, Lagos R, Jameson DM, Monasterio O. Studies on the dissociation and urea-induced unfolding of FtsZ support the dimer nucleus polymerization mechanism. Biophys J. 2012 May 2;102(9):2176-85.

Jameson DM, James NG, Albanesi JP.  Fluorescence fluctuation spectroscopy approaches to the study of receptors in live cells.  Methods Enzymol. 2013;519-87-113.

Jameson DM, Vetromile CM, James NG. Investigations of protein-protein interactions using time-resolved fluorescence and phasors. Methods. 2013 Jan 22.