Payne Lab: Publications

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[[Payne Lab | <font face="trebuchet ms" style="color:#ffffff"> '''Research''' </font>]] &nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;
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==Publications==
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==Publications==  
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8. "Humphries WH IV, Szymanski CJ, Payne CK, 2011 Endo-Lysosomal Vesicles Positive for Rab7 and LAMP1 Are Terminal Vesicles for the Transport of Dextran. PLoS ONE 6(10): e26626. doi:10.1371/journal.pone.0026626
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13. "Conditioned media downregulates nuclear expression of Nrf2," S. Sarkar, C.K. Payne, and M.L. Kemp, Cellular and Molecular Bioengineering, in press (2013).
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7. "Single particle tracking as a method to resolve differences in highly colocalized proteins," C.J. Szymanski, W.H. Humphries IV, C.K. Payne, Analyst,136, 3527-3533 (2011).
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12. "Nanoparticle surface charge mediates the cellular receptors used by protein-nanoparticle complexes," C.C. Fleischer and C.K. Payne, J. Phys. Chem. B, 116, 8901-8907 (2012).
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11. "Imaging lysosomal enzyme activity in live cells using self-quenched substrates," W.H. Humphries and C.K. Payne, Analytical Biochemistry, 424, 178-183 (2012).
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10. "Fluorescent coumarin thiols measure biological redox couples," K.G. Reddie, W.H. Humphries, C.P. Bain, C.K. Payne, M.L. Kemp, and N. Murthy, Organic Letters, 14, 680-683 (2012).
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9. "Nanoparticles act as protein carriers during cellular internalization," G.W. Doorley and C.K. Payne, Chem. Commun., 48, 2961-2963 (2012).
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8. "Endo-lysosomal vesicles positive for Rab7 and LAMP1 are terminal vesicles for the transport of dextran," W.H. Humphries IV, C.J. Szymanski, C.K. Payne, PLoS ONE 6, e26626 (2011). doi:10.1371/journal.pone.0026626.  [http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0026626 Link]
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7. "Single particle tracking as a method to resolve differences in highly colocalized proteins," C.J. Szymanski, W.H. Humphries IV, C.K. Payne, Analyst, 136, 3527-3533 (2011).
6. "Cellular binding of nanoparticles in the presence of serum proteins," G.W. Doorley and C.K. Payne, Chem. Commun., 47, 466-468 (2011). [http://openwetware.org/images/0/0b/6_Doorley_ChemComm.pdf PDF]
6. "Cellular binding of nanoparticles in the presence of serum proteins," G.W. Doorley and C.K. Payne, Chem. Commun., 47, 466-468 (2011). [http://openwetware.org/images/0/0b/6_Doorley_ChemComm.pdf PDF]
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1. "Cellular binding, motion, and internalization of synthetic gene delivery polymers," G.T. Hess, W.H. Humphries IV, N.C. Fay, and C.K. Payne, Biochim. Biophys. Acta, Mol. Cell Res., 1773, 1583-1588 (2007). pmid:17888530.  [http://openwetware.org/images/3/34/1_Hess_BBA.pdf PDF]
1. "Cellular binding, motion, and internalization of synthetic gene delivery polymers," G.T. Hess, W.H. Humphries IV, N.C. Fay, and C.K. Payne, Biochim. Biophys. Acta, Mol. Cell Res., 1773, 1583-1588 (2007). pmid:17888530.  [http://openwetware.org/images/3/34/1_Hess_BBA.pdf PDF]
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[http://openwetware.org/images/3/30/Payne_CV_2011.pdf '''C.K. Payne publications prior to Georgia Tech]''' <br>
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[http://openwetware.org/images/3/3e/Payne_CV_2012.pdf '''C.K. Payne publications prior to Georgia Tech]''' <br>

Revision as of 09:54, 12 March 2013

Research         People         Publications         Funding         News         Seminars         Positions Available         Outreach         Contact        



Publications

13. "Conditioned media downregulates nuclear expression of Nrf2," S. Sarkar, C.K. Payne, and M.L. Kemp, Cellular and Molecular Bioengineering, in press (2013).

12. "Nanoparticle surface charge mediates the cellular receptors used by protein-nanoparticle complexes," C.C. Fleischer and C.K. Payne, J. Phys. Chem. B, 116, 8901-8907 (2012).

11. "Imaging lysosomal enzyme activity in live cells using self-quenched substrates," W.H. Humphries and C.K. Payne, Analytical Biochemistry, 424, 178-183 (2012).

10. "Fluorescent coumarin thiols measure biological redox couples," K.G. Reddie, W.H. Humphries, C.P. Bain, C.K. Payne, M.L. Kemp, and N. Murthy, Organic Letters, 14, 680-683 (2012).

9. "Nanoparticles act as protein carriers during cellular internalization," G.W. Doorley and C.K. Payne, Chem. Commun., 48, 2961-2963 (2012).

8. "Endo-lysosomal vesicles positive for Rab7 and LAMP1 are terminal vesicles for the transport of dextran," W.H. Humphries IV, C.J. Szymanski, C.K. Payne, PLoS ONE 6, e26626 (2011). doi:10.1371/journal.pone.0026626. Link

7. "Single particle tracking as a method to resolve differences in highly colocalized proteins," C.J. Szymanski, W.H. Humphries IV, C.K. Payne, Analyst, 136, 3527-3533 (2011).

6. "Cellular binding of nanoparticles in the presence of serum proteins," G.W. Doorley and C.K. Payne, Chem. Commun., 47, 466-468 (2011). PDF

5. "Intracellular degradation of low-density lipoprotein probed with two-color fluorescence microscopy," W.H. Humphries IV, N.C. Fay, C.K. Payne, Integr. Biol., 2, 536 - 544 (2010). PDF

4. "Imaging intracellular quantum dots: Fluorescence microscopy and transmission electron microscopy," C.J. Szymanski, H. Yi, J.L. Liu, E.R. Wright, C.K. Payne, Nanobiotechnology Protocols, in press (2010).

3. "Pyrenebutyrate leads to cellular binding, not intracellular delivery, of polyarginine quantum dots," A.E. Jablonski, T. Kawakami, A.Y. Ting, C.K. Payne, J. Phys. Chem. Lett., 1, 1312–1315 (2010). PDF

x. "Pyrenebutyrate-Mediated Delivery of Quantum Dots across the Plasma Membrane of Living Cells," A.E. Jablonski, W.H. Humphries, C.K. Payne, J. Phys. Chem. B, 113 (2), 405-408 (2009), pmid:19099434, withdrawn. The conclusions drawn from the data in this manuscript were incorrect. A full discussion can be found in, "Pyrenebutyrate Leads to Cellular Binding, Not Intracellular Delivery, of Polyarginine Quantum Dots," A.E. Jablonski, T. Kawakami, A.Y. Ting, C.K. Payne, J. Phys. Chem. Lett., 1, 1312–1315 (2010).

2. "Imaging gene delivery with fluorescence microscopy," C.K. Payne, Nanomedicine, 2, 847-860 (2007). pmid:18095850.

1. "Cellular binding, motion, and internalization of synthetic gene delivery polymers," G.T. Hess, W.H. Humphries IV, N.C. Fay, and C.K. Payne, Biochim. Biophys. Acta, Mol. Cell Res., 1773, 1583-1588 (2007). pmid:17888530. PDF

C.K. Payne publications prior to Georgia Tech

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