Topp:Publications: Difference between revisions

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Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders. Moorthy, BS. Iyer, LK, and Topp, EM, Journal of Visualized Experiments (JoVE) (98), e52503, doi:10.3791/52503 (2015). Published 04/14/2015. NIHMS ID: NIHMS653055. 4/21/2015 10 110.
<li>[http://www.jove.com/video/52503/mass-spectrometric-approaches-to-study-protein-structure-interactions Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders.] BS Moorthy, LK Iyer, and <strong>EM Topp,</strong> Journal of Visualized Experiments (JoVE) (98), e52503, doi:10.3791/52503 (2015). Published 04/14/2015. NIHMS ID: NIHMS653055. 4/21/2015 10 110.


Structural transitions and interactions in the early stages of human glucagon amyloid fibrillation. Moorthy, Balakrishnan S., Ghomi, Hamed T., Lill, Markus A., and Topp. Elizabeth M., Biophysical Journal, 108/4: 937-948, 2015. PMCID: PMC4336368 112.
<li>[http://www.ncbi.nlm.nih.gov/pubmed/?term=Structural+transitions+and+interactions+in+the+early+stages+of+human+glucagon+amyloid+fibrillation Structural transitions and interactions in the early stages of human glucagon amyloid fibrillation.] BA Moorthy, HT Ghomi, MA Lill, and <strong>EM Topp,</strong>. <em>Biophysical Journal</em>, 108/4: 937-948, 2015. PMCID: PMC4336368 112.</li>


Thiol-disulfide exchange in peptides derived from human growth hormone during lyophilization and storage in the solid-state. Chandrasekhar, Saradha and Topp, Elizabeth M., Journal of Pharmaceutical Sciences, 104/4: 1291-1302, 2015. PMID: 25631887 111.
<li>[http://www.ncbi.nlm.nih.gov/pubmed/25631887 Thiol-disulfide exchange in peptides derived from human growth hormone during lyophilization and storage in the solid-state.] S Chandrasekhar, and <strong>EM Topp,</strong>, <em>Journal of Pharmaceutical Sciences</em>, 104/4: 1291-1302, 2015. PMID: 25631887 111.</li>


Photolytic crosslinking to probe protein-protein and protein-matrix interactions in lyophilized powders. Iyer, Lavanya K., Moorthy, Balakrishnan S., and Topp, Elizabeth M., submitted to Molecular Pharmaceutics, March 5, 2015.
<li>Photolytic crosslinking to probe protein-protein and protein-matrix interactions in lyophilized powders. LK Iyer, BS Moorthy, and <strong>EM Topp,</strong>, <em>submitted to Molecular Pharmaceutics, March 5, 2015.</em></li>
Cocrystalline solids of telaprevir with enhanced oral absorption. Stavropoulos, K, Johnston, S., Zhang, Y, Bhisetti, G, Hurrey, M., Hurter, P., Topp, E., and Kadiyala, I, Journal of Pharmaceutical Sciences, submitted January 14, 2015. 113.


<li>Cocrystalline solids of telaprevir with enhanced oral absorption. K Stavropoulos, S Johnston, Y Zhang, G Bhisetti, M Hurrey, P Hurter, <strong>E Topp</strong>, and I Kadiyala, <em>Journal of Pharmaceutical Sciences, submitted January 14, 2015. 113.</em></li>


<li>[http://www.ncbi.nlm.nih.gov/pubmed/24816133 Predicting Protein Aggregation during Storage in Lyophilized Solids Using Solid State Amide Hydrogen/Deuterium Exchange with Mass Spectrometric Analysis (ssHDX-MS).] BS Moorthy, SG  Schultz, SG Kim, <strong>E.M. Topp</strong>. <em>Molecular Pharmaceutics</em>, Jun 2;11(6):1869-79, 2014.</li>


 
<li>[http://www.ncbi.nlm.nih.gov/pubmed/?term=Commentary%3A+Current+perspectives+on+the+aggregation+of+protein+drugs Commentary: Current perspectives on the aggregation of protein drugs.] <strong>EM Topp</strong>. <em>AAPS Journal</em>, <em>AAPS Journal</em>, May;16(3):413-4, 2014.</li>
<li>[http://www.ncbi.nlm.nih.gov/pubmed/24816133 Predicting Protein Aggregation during Storage in Lyophilized Solids Using Solid State Amide Hydrogen/Deuterium Exchange with Mass Spectrometric Analysis (ssHDX-MS).] B.S. Moorthy, S.G. Schultz, S.G. Kim, <strong>E.M. Topp</strong>. <em>Molecular Pharmaceutics</em>, Jun 2;11(6):1869-79, 2014.</li>
 
<li>[http://www.ncbi.nlm.nih.gov/pubmed/?term=Commentary%3A+Current+perspectives+on+the+aggregation+of+protein+drugs Commentary: Current perspectives on the aggregation of protein drugs.] <strong>E. M. Topp</strong>. <em>AAPS Journal</em>, <em>AAPS Journal</em>, May;16(3):413-4, 2014.</li>


<li>[http://www.ncbi.nlm.nih.gov/pubmed/?term=Thiol%E2%80%93Disulfide+Exchange+in+Peptides+Derived+from+Human+Growth+Hormone Thiol–Disulfide Exchange in Peptides Derived from Human Growth Hormone.] S. Chandrasekhar, D.E. Epling, A.M. Sophocleous and <strong>E.M. Topp</strong>. <em>Journal of Pharmaceutical Sciences</em>, 103/4: 1032–1042, April 2014.</li>
<li>[http://www.ncbi.nlm.nih.gov/pubmed/?term=Thiol%E2%80%93Disulfide+Exchange+in+Peptides+Derived+from+Human+Growth+Hormone Thiol–Disulfide Exchange in Peptides Derived from Human Growth Hormone.] S. Chandrasekhar, D.E. Epling, A.M. Sophocleous and <strong>E.M. Topp</strong>. <em>Journal of Pharmaceutical Sciences</em>, 103/4: 1032–1042, April 2014.</li>


<li>[Analyzing subvisible particles in protein drug products: A comparison of dynamic light scattering (DLS) and resonant mass measurement (RMM). J. Panchal, J. Kotarek, E. Marszal,and <strong>E.M. Topp</strong>. <em>AAPS Journal<em>, 16/3: 440-451, 2014. DOI: 10.1208/s12248-014-9579-6.
<li>[Analyzing subvisible particles in protein drug products: A comparison of dynamic light scattering (DLS) and resonant mass measurement (RMM). J Panchal, J Kotarek, E Marszal,and <strong>EM Topp</strong>. <em>AAPS Journal</em>, 16/3: 440-451, 2014. DOI: 10.1208/s12248-014-9579-6.


<li>[http://www.ncbi.nlm.nih.gov/pubmed/23662940 Microarrays and microneedle arrays for delivery of peptides, proteins, vaccines and other applications.] S. Chandrasekhar, L.K. Iyer, J.P. Panchal, <strong>E.M. Topp</strong>. J.B. Cannon and V.V. Ranade, <em>Expert Opinion in Drug Delivery</em>, 10/8: 1155-1170, 2013.</li>
<li>[http://www.ncbi.nlm.nih.gov/pubmed/23662940 Microarrays and microneedle arrays for delivery of peptides, proteins, vaccines and other applications.] S Chandrasekhar, LK Iyer, JP Panchal, <strong>EM Topp</strong>, JB Cannon and VV Ranade, <em>Expert Opinion in Drug Delivery</em>, 10/8: 1155-1170, 2013.</li>


<li>[http://pubs.acs.org/doi/abs/10.1021/mp4004332?prevSearch=Photolytic%2Blabeling%2Bto%2Bprobe%2Bprotein-protein%2Band%2Bprotein-matrix%2Binteractions%2Bin%2Blyophilized%2Bpowders&searchHistoryKey= Photolytic labeling to probe protein-protein and protein-matrix interactions in lyophilized powders.] L.K. Iyer, B.S. Moorthy, and <strong>E.M. Topp</strong>. <em>Molecular Pharmaceutics</em>, 10: 4629-4639, 2013.</li>
<li>[http://pubs.acs.org/doi/abs/10.1021/mp4004332?prevSearch=Photolytic%2Blabeling%2Bto%2Bprobe%2Bprotein-protein%2Band%2Bprotein-matrix%2Binteractions%2Bin%2Blyophilized%2Bpowders&searchHistoryKey= Photolytic labeling to probe protein-protein and protein-matrix interactions in lyophilized powders.] LK Iyer, BS Moorthy, and <strong>EM Topp</strong>. <em>Molecular Pharmaceutics</em>, 10: 4629-4639, 2013.</li>


<li>[http://www.sciencedirect.com/science/article/pii/S0098135413002287 Protein aggregation and lyophilization: Protein structural descriptors as predictors of aggregation propensity.] B.C. Roughton, L.K. Iyer, E. Bertelsen, <strong>E.M. Topp</strong>, EM and K.V. Camarda. <em>Journal of Computers and Chemical Engineering</em>, 58/11: 369-377, 2013.</li>
<li>[http://www.sciencedirect.com/science/article/pii/S0098135413002287 Protein aggregation and lyophilization: Protein structural descriptors as predictors of aggregation propensity.] BC Roughton, LK Iyer, E Bertelsen, <strong>EM Topp</strong>, and KV Camarda. <em>Journal of Computers and Chemical Engineering</em>, 58/11: 369-377, 2013.</li>


<li>Effect of deamidation on the in vivo fate of monoclonal antibodies. S. Chandrasekhar, B.S. Moorthy, B. Xie and <strong>E.M. Topp</strong>, in Biobetters: Protein Engineering to Approach the Curative, A. Rosenberg and B. Demeule (eds.), <em>Advances in Pharmaceutical Sciences</em> series, Academic Press, New York, invited.</li>
<li>Effect of deamidation on the in vivo fate of monoclonal antibodies. S Chandrasekhar, BS Moorthy, B Xie and <strong>EM Topp</strong>, in <em>Biobetters: Protein Engineering to Approach the Curative</em>, A Rosenberg and B Demeule (eds.), <em>Advances in Pharmaceutical Sciences</em> series, Academic Press, New York, invited.</li>


<li>[http://onlinelibrary.wiley.com/doi/10.1002/14356007.o22_o08/abstract Approaches to pharmaceutical product design.] B.C. Roughton, K.V. Camarada and <strong>E.M. Topp</strong>, in <em>Ullman’s Encyclopedia of Industrial Chemistry</em>, Wiley-VCH Verlag GmbH & Co., Mannheim, Germany, 2012. DOI: 10.1002/14356007.o22_o08; published online 15 JAN 2013.</li>
<li>[http://onlinelibrary.wiley.com/doi/10.1002/14356007.o22_o08/abstract Approaches to pharmaceutical product design.] BC Roughton, KV Camarada and <strong>EM Topp</strong>, in <em>Ullman’s Encyclopedia of Industrial Chemistry</em>, Wiley-VCH Verlag GmbH & Co., Mannheim, Germany, 2012. DOI: 10.1002/14356007.o22_o08; published online 15 JAN 2013.</li>


<li>[http://books.google.com/books?id=GBciDxg-TfgC&pg=PA1351&lpg=PA1351&dq=Optimizing+protein-excipient+interactions+for+the+development+of+aggregation-reducing+lyophilized+formulations&source=bl&ots=MxS08Q6Ha5&sig=pmFheAns2tvu2gzBzKFYV2CHdpw&hl=en&sa=X&ei=Kq6yU_fnNKe8ygOznoDgAg&ved=0CC4Q6AEwAg#v=onepage&q=Optimizing%20protein-excipient%20interactions%20for%20the%20development%20of%20aggregation-reducing%20lyophilized%20formulations&f=false Optimizing protein-excipient interactions for the development of aggregation-reducing lyophilized formulations.] B.C. Roughton, A.I. Pokphanh, <strong>E.M. Topp</strong> and K.V. Camarda. <em>Proceedings of the 11th International Symposium on Process Systems Engineering</em>, I. a Karimi and R. Srinivasan (eds.), Elsevier, Oxford, UK, 2012. pp. 1351-1355.</li>
<li>[http://books.google.com/books?id=GBciDxg-TfgC&pg=PA1351&lpg=PA1351&dq=Optimizing+protein-excipient+interactions+for+the+development+of+aggregation-reducing+lyophilized+formulations&source=bl&ots=MxS08Q6Ha5&sig=pmFheAns2tvu2gzBzKFYV2CHdpw&hl=en&sa=X&ei=Kq6yU_fnNKe8ygOznoDgAg&ved=0CC4Q6AEwAg#v=onepage&q=Optimizing%20protein-excipient%20interactions%20for%20the%20development%20of%20aggregation-reducing%20lyophilized%20formulations&f=false Optimizing protein-excipient interactions for the development of aggregation-reducing lyophilized formulations.] BC Roughton, AI Pokphanh, <strong>EM Topp</strong> and KV Camarda. <em>Proceedings of the 11th International Symposium on Process Systems Engineering</em>, I a Karimi and R Srinivasan (eds.), Elsevier, Oxford, UK, 2012. pp. 1351-1355.</li>


<li>[http://www.ncbi.nlm.nih.gov/pubmed/22304418 Protein G, Protein A and Protein-A-derived peptides inhibit the agitation induced aggregation of IgG.] J. Zhang and <strong>E.M. Topp</strong>. <em>Molecular Pharmaceutics</em>, 9(3): 622-628, 2012.  DOI: 10.1021/mp200548x.</li>
<li>[http://www.ncbi.nlm.nih.gov/pubmed/22304418 Protein G, Protein A and Protein-A-derived peptides inhibit the agitation induced aggregation of IgG.] J Zhang and <strong>EM Topp</strong>. <em>Molecular Pharmaceutics</em>, 9(3): 622-628, 2012.  DOI: 10.1021/mp200548x.</li>


<li>[http://www.ncbi.nlm.nih.gov/pubmed/22352990 Localized hydration in lyophilized myoglobin by hydrogen-deuterium exchange mass spectrometry. 2. Exchange kinetics.] A.M. Sophocleous, <strong>E.M. Topp</strong>. <em>Mol Pharm.</em> 2012 Apr 2;9(4):727-33. doi: 10.1021/mp2004093. Epub 2012 Feb 29.</li>
<li>[http://www.ncbi.nlm.nih.gov/pubmed/22352990 Localized hydration in lyophilized myoglobin by hydrogen-deuterium exchange mass spectrometry. 2. Exchange kinetics.] AM Sophocleous, <strong>EM Topp</strong>. <em>Mol Pharm.</em> 2012 Apr 2;9(4):727-33. doi: 10.1021/mp2004093. Epub 2012 Feb 29.</li>


<li>[http://www.ncbi.nlm.nih.gov/pubmed/22352965 Localized hydration in lyophilized myoglobin by hydrogen-deuterium exchange mass spectrometry. 1. Exchange mapping.] A.M. Sophocleous, J. Zhang, <strong>E.M. Topp</strong>. <em>Mol Pharm.</em> 2012 Apr 2;9(4):718-26. doi: 10.1021/mp3000088. Epub 2012 Feb 29.</li>
<li>[http://www.ncbi.nlm.nih.gov/pubmed/22352965 Localized hydration in lyophilized myoglobin by hydrogen-deuterium exchange mass spectrometry. 1. Exchange mapping.] AM Sophocleous, J Zhang, <strong>EM Topp</strong>. <em>Mol Pharm.</em> 2012 Apr 2;9(4):718-26. doi: 10.1021/mp3000088. Epub 2012 Feb 29.</li>


<li>[http://www.ncbi.nlm.nih.gov/pubmed/22304418 Protein G, protein A and protein A-derived peptides inhibit the agitation induced aggregation of IgG.] J. Zhang, <strong>E.M. Topp</strong>. <em>Mol Pharm.</em> 2012 Mar 5;9(3):622-8. doi: 10.1021/mp200548x. Epub 2012 Feb 9.</li>
<li>[http://www.ncbi.nlm.nih.gov/pubmed/22304418 Protein G, protein A and protein A-derived peptides inhibit the agitation induced aggregation of IgG.] J Zhang, <strong>EM Topp</strong>. <em>Mol Pharm.</em> 2012 Mar 5;9(3):622-8. doi: 10.1021/mp200548x. Epub 2012 Feb 9.</li>


<li>Probing protein conformation in lyophilized powders by hydrogen/deuterium exchange: Deuterium uptake kinetics in lyophilized myoglobin powders. A. Sophocleous and <strong>E.M. Topp</strong>. <em>Molecular Pharmaceutics.</em> Invited manuscript for special issue, “Advances in Biophysical and Bioanalytical Protein Characterization”. <em>Submitted August 17, 2011. Reviewers’ comments received November 16, 2011.</em></li>
<li>Probing protein conformation in lyophilized powders by hydrogen/deuterium exchange: Deuterium uptake kinetics in lyophilized myoglobin powders. A Sophocleous and <strong>EM Topp</strong>. <em>Molecular Pharmaceutics.</em> Invited manuscript for special issue, “Advances in Biophysical and Bioanalytical Protein Characterization”. <em>Submitted August 17, 2011. Reviewers’ comments received November 16, 2011.</em></li>


<li>[http://www.sciencedirect.com/science/article/pii/S0098135411002456 Use of glass transitions in carbohydrate excipient design for lyophilized protein formulations]. B.C. Roughton, <strong>E.M. Topp</strong>, and K.V. Camarda. <em>Computers and Chemical Engineering</em>, in press. DOI:10.1016/j.compchemeng.2011.07.018.</li>
<li>[http://www.sciencedirect.com/science/article/pii/S0098135411002456 Use of glass transitions in carbohydrate excipient design for lyophilized protein formulations]. BC Roughton, <strong>EM Topp</strong>, and KV Camarda. <em>Computers and Chemical Engineering</em>, in press. DOI:10.1016/j.compchemeng.2011.07.018.</li>


<li>Localized effects of hydration on lyophilized myoglobin by hydrogen/deuterium exchange mass spectrometry. A.M. Sophocleous, J. Zhang and <strong>E.M. Topp</strong>, <em>submitted to Biophysical Journal, June 24, 2011. Reviewers’ comments received August 15, 2011. Revised version submitted October 29, 2011.</em></li>
<li>Localized effects of hydration on lyophilized myoglobin by hydrogen/deuterium exchange mass spectrometry. A.M. Sophocleous, J Zhang and <strong>EM Topp</strong>, <em>submitted to <em>Biophysical Journal</em>, June 24, 2011. Reviewers’ comments received August 15, 2011. Revised version submitted October 29, 2011.</em></li>


<li>Proteins and peptides: Physical and chemical stability. Andreas Sophocleous, Jun Zhang, Lavanya Iyer, Saradha Chandra Sekhar and <strong>Elizabeth M. Topp</strong>, Encyclopedia of Pharmaceutical Science and Technology, 4th ed., James Swarbrick, D.Sc., Ph.D., Editor. Informa Healthcare, New York, NY. <em>Submitted April 26, 2011.</em></li>
<li>Proteins and peptides: Physical and chemical stability. A Sophocleous, J Zhang, L Iyer, S Chandrasekhar and <strong>EM Topp</strong>, <em>Encyclopedia of Pharmaceutical Science and Technology</em>, 4th ed., James Swarbrick, D.Sc., Ph.D., Editor. Informa Healthcare, New York, NY. <em>Submitted April 26, 2011.</em></li>


<li>[http://www.ncbi.nlm.nih.gov/pubmed/20195761 Adhesive/dentin interface: the weak link in the composite restoration.] P. Spencer, Q. Ye, J. Park, <strong>E.M Topp</strong>, A. Misra, O. Marangos, Y. Wang, B.S. Bohaty, V. Singh, F. Sene, J. Eslick, K.V. Camarda, J.L. Katz. <em>Ann Biomed Eng</em>. 38(6): 1989-2003, 2010.</li>
<li>[http://www.ncbi.nlm.nih.gov/pubmed/20195761 Adhesive/dentin interface: the weak link in the composite restoration.] P Spencer, Q Ye, J Park, <strong>EM Topp</strong>, A Misra, O Marangos, Y Wang, BS Bohaty, V Singh, F Sene, J Eslick, KV Camarda, JL Katz. <em>Ann Biomed Eng</em>. 38(6): 1989-2003, 2010.</li>


<li>[http://onlinelibrary.wiley.com/doi/10.1002/jps.22206/full Thiol-disulfide interchange in the tocinoic acid/glutathione system during freezing and drying.] M. Thing, J. Zhang, J. Laurence and <strong>E.M. Topp</strong>. <em>J Pharm Sci</em>, 99/12: 4849-4856, 2010. DOI 10.1002/jps.22206.</li>  
<li>[http://onlinelibrary.wiley.com/doi/10.1002/jps.22206/full Thiol-disulfide interchange in the tocinoic acid/glutathione system during freezing and drying.] M Thing, J Zhang, J Laurence and <strong>EM Topp</strong>. <em>J Pharm Sci</em>, 99/12: 4849-4856, 2010. DOI 10.1002/jps.22206.</li>  


<li>[http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2860647/ Effect of photoinitiator system and water content on dynamic mechanical properties of a light-cured bisGMA/HEMA dental resin.[]  J. Park, Q. Ye, <strong>E.M. Topp</strong>, S.L. Kieweg and P. Spencer. <em>J Biomed Mater Res A</em>. 93A/4: 1245-1251, 2010. DOI: 10.1002/jbm.a.32617.</li>
<li>[http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2860647/ Effect of photoinitiator system and water content on dynamic mechanical properties of a light-cured bisGMA/HEMA dental resin.[]  J Park, Q Ye, <strong>EM Topp</strong>, SL Kieweg and P Spencer. <em>J Biomed Mater Res A</em>. 93A/4: 1245-1251, 2010. DOI: 10.1002/jbm.a.32617.</li>
   
   
<li>[http://www.ncbi.nlm.nih.gov/pubmed/19748537 Immune response to controlled release of immunomodulating peptides in an experimental autoimmune encephalomyelitis (EAE) mouse model.] Hong Zhao, Paul Kiptoo, Todd D. Williams, Teruna J. Siahaan and <strong>Elizabeth M. Topp</strong>. <em>J Control Release</em>. 141: 145-152, 2010. DOI: 10.1016/j.jconrel.2009.09.002.</li>
<li>[http://www.ncbi.nlm.nih.gov/pubmed/19748537 Immune response to controlled release of immunomodulating peptides in an experimental autoimmune encephalomyelitis (EAE) mouse model.] H Zhao, P Kiptoo, TD Williams, TJ Siahaan and <strong>EM Topp</strong>. <em>J Control Release</em>. 141: 145-152, 2010. DOI: 10.1016/j.jconrel.2009.09.002.</li>  
 
<li>[http://onlinelibrary.wiley.com/doi/10.1002/9780470595886.ch19/summary Protein conformation and reactivity in amorphous solids.] S. Sinha, S. Xie and <strong>E.M. Topp</strong>, in [http://www.researchandmarkets.com/reports/1403442/formulation_and_process_development_strategies Formulation and Process Development Strategies for Manufacturing of Biopharmaceuticals], F. Jameel and S. Hershenson, eds., John Wiley and Sons, Hoboken, NJ, 2010. ISBN: 978-0-470-11812-2. pp. 493-506.</li>
 
<li>[http://onlinelibrary.wiley.com/doi/10.1002/9780470595886.ch2/summary Chemical instability in peptide and protein pharmaceuticals.] <strong>Elizabeth M. Topp</strong>, Lei Zhang, Hong Zhao, Robert W. Payne, Gabriel J. Evans and Mark C. Manning.  [http://www.researchandmarkets.com/reports/1403442/formulation_and_process_development_strategies Formulation and Process Development Strategies for Manufacturing  Biopharmaceuticals], F. Jameel and S. Hershenson, eds., John Wiley and Sons, Hoboken, NJ, 2010. ISBN: 978-0-470-11812-2. pp. 41-68.</li>
 
<li>[http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2783757/ Water sorption and dynamic mechanical properties characteristics of dentin adhesives with a urethane-based multifunctional methacrylate monomer.] Jong-Gu Park, Qiang Ye, <strong>Elizabeth M. Topp</strong>, Anil Misra and Paulette Spencer. <em>Dent Mater.</em> 25: 1569-1575, 2009.</li>  


<li>[http://www.ncbi.nlm.nih.gov/pubmed/19358261 Dynamic mechanical analysis and esterase degradation of dentin adhesives containing a branched methacrylate.] Jong-Gu Park, Qiang Ye, <strong>Elizabeth M. Topp</strong>, Chi H. Lee, Elisabet L. Kostoryz, Anil Misra and Paulette Spencer. <em>J Biomed Mater Res B Applied Biomat.</em> 91B(1): 61-70, 2009. DOI: 10.1002/jbm.b.31374.</li>
<li>[http://onlinelibrary.wiley.com/doi/10.1002/9780470595886.ch19/summary Protein conformation and reactivity in amorphous solids.] S Sinha, S Xie and <strong>EM Topp</strong>, in [http://www.researchandmarkets.com/reports/1403442/formulation_and_process_development_strategies <em>Formulation and Process Development Strategies for Manufacturing of Biopharmaceuticals</em>], F Jameel and S Hershenson, eds., John Wiley and Sons, Hoboken, NJ, 2010. ISBN: 978-0-470-11812-2. pp. 493-506.</li>


<li>[http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2758931/ Enzyme-catalyzed hydrolysis of dentin adhesives containing a new urethane-based trimethacrylate monomer.] Jong-Gu Park, Qiang Ye, <strong>Elizabeth M. Topp</strong> and Paulette Spencer. <em>J Biomed Mater Res B Applied Biomater.</em> 91B: 562–571, 2009.</li>
<li>[http://onlinelibrary.wiley.com/doi/10.1002/9780470595886.ch2/summary Chemical instability in peptide and protein pharmaceuticals.] <strong>EM Topp</strong>, L Zhang, H Zhao, RW Payne, GJ Evans and MC Manning. [http://www.researchandmarkets.com/reports/1403442/formulation_and_process_development_strategies <em>Formulation and Process Development Strategies for Manufacturing  Biopharmaceuticals</em>], F Jameel and S Hershenson, eds., John Wiley and Sons, Hoboken, NJ, 2010. ISBN: 978-0-470-11812-2. pp. 41-68.</li></ol>
<li>[http://onlinelibrary.wiley.com/doi/10.1002/jps.21516/full Reversibility and regioselectivity of thiol/disulfide exchange in lyophilized solids.] L. Zhang, T.D. Williams and <strong>E.M. Topp</strong>. <em>J Pharm Sci.</em> 98/9: 3312-3318, 2009.</li></ol>
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Latest revision as of 05:47, 22 April 2015

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Recent research and review papers published, accepted for publication, under review or in preparation.

http://www.ncbi.nlm.nih.gov/pubmed/?term=topp%2C+elizabeth+m

  1. Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders. BS Moorthy, LK Iyer, and EM Topp, Journal of Visualized Experiments (JoVE) (98), e52503, doi:10.3791/52503 (2015). Published 04/14/2015. NIHMS ID: NIHMS653055. 4/21/2015 10 110.
  2. Structural transitions and interactions in the early stages of human glucagon amyloid fibrillation. BA Moorthy, HT Ghomi, MA Lill, and EM Topp,. Biophysical Journal, 108/4: 937-948, 2015. PMCID: PMC4336368 112.
  3. Thiol-disulfide exchange in peptides derived from human growth hormone during lyophilization and storage in the solid-state. S Chandrasekhar, and EM Topp,, Journal of Pharmaceutical Sciences, 104/4: 1291-1302, 2015. PMID: 25631887 111.
  4. Photolytic crosslinking to probe protein-protein and protein-matrix interactions in lyophilized powders. LK Iyer, BS Moorthy, and EM Topp,, submitted to Molecular Pharmaceutics, March 5, 2015.
  5. Cocrystalline solids of telaprevir with enhanced oral absorption. K Stavropoulos, S Johnston, Y Zhang, G Bhisetti, M Hurrey, P Hurter, E Topp, and I Kadiyala, Journal of Pharmaceutical Sciences, submitted January 14, 2015. 113.
  6. Predicting Protein Aggregation during Storage in Lyophilized Solids Using Solid State Amide Hydrogen/Deuterium Exchange with Mass Spectrometric Analysis (ssHDX-MS). BS Moorthy, SG Schultz, SG Kim, E.M. Topp. Molecular Pharmaceutics, Jun 2;11(6):1869-79, 2014.
  7. Commentary: Current perspectives on the aggregation of protein drugs. EM Topp. AAPS Journal, AAPS Journal, May;16(3):413-4, 2014.
  8. Thiol–Disulfide Exchange in Peptides Derived from Human Growth Hormone. S. Chandrasekhar, D.E. Epling, A.M. Sophocleous and E.M. Topp. Journal of Pharmaceutical Sciences, 103/4: 1032–1042, April 2014.
  9. [Analyzing subvisible particles in protein drug products: A comparison of dynamic light scattering (DLS) and resonant mass measurement (RMM). J Panchal, J Kotarek, E Marszal,and EM Topp. AAPS Journal, 16/3: 440-451, 2014. DOI: 10.1208/s12248-014-9579-6.
  10. Microarrays and microneedle arrays for delivery of peptides, proteins, vaccines and other applications. S Chandrasekhar, LK Iyer, JP Panchal, EM Topp, JB Cannon and VV Ranade, Expert Opinion in Drug Delivery, 10/8: 1155-1170, 2013.
  11. Photolytic labeling to probe protein-protein and protein-matrix interactions in lyophilized powders. LK Iyer, BS Moorthy, and EM Topp. Molecular Pharmaceutics, 10: 4629-4639, 2013.
  12. Protein aggregation and lyophilization: Protein structural descriptors as predictors of aggregation propensity. BC Roughton, LK Iyer, E Bertelsen, EM Topp, and KV Camarda. Journal of Computers and Chemical Engineering, 58/11: 369-377, 2013.
  13. Effect of deamidation on the in vivo fate of monoclonal antibodies. S Chandrasekhar, BS Moorthy, B Xie and EM Topp, in Biobetters: Protein Engineering to Approach the Curative, A Rosenberg and B Demeule (eds.), Advances in Pharmaceutical Sciences series, Academic Press, New York, invited.
  14. Approaches to pharmaceutical product design. BC Roughton, KV Camarada and EM Topp, in Ullman’s Encyclopedia of Industrial Chemistry, Wiley-VCH Verlag GmbH & Co., Mannheim, Germany, 2012. DOI: 10.1002/14356007.o22_o08; published online 15 JAN 2013.
  15. Optimizing protein-excipient interactions for the development of aggregation-reducing lyophilized formulations. BC Roughton, AI Pokphanh, EM Topp and KV Camarda. Proceedings of the 11th International Symposium on Process Systems Engineering, I a Karimi and R Srinivasan (eds.), Elsevier, Oxford, UK, 2012. pp. 1351-1355.
  16. Protein G, Protein A and Protein-A-derived peptides inhibit the agitation induced aggregation of IgG. J Zhang and EM Topp. Molecular Pharmaceutics, 9(3): 622-628, 2012. DOI: 10.1021/mp200548x.
  17. Localized hydration in lyophilized myoglobin by hydrogen-deuterium exchange mass spectrometry. 2. Exchange kinetics. AM Sophocleous, EM Topp. Mol Pharm. 2012 Apr 2;9(4):727-33. doi: 10.1021/mp2004093. Epub 2012 Feb 29.
  18. Localized hydration in lyophilized myoglobin by hydrogen-deuterium exchange mass spectrometry. 1. Exchange mapping. AM Sophocleous, J Zhang, EM Topp. Mol Pharm. 2012 Apr 2;9(4):718-26. doi: 10.1021/mp3000088. Epub 2012 Feb 29.
  19. Protein G, protein A and protein A-derived peptides inhibit the agitation induced aggregation of IgG. J Zhang, EM Topp. Mol Pharm. 2012 Mar 5;9(3):622-8. doi: 10.1021/mp200548x. Epub 2012 Feb 9.
  20. Probing protein conformation in lyophilized powders by hydrogen/deuterium exchange: Deuterium uptake kinetics in lyophilized myoglobin powders. A Sophocleous and EM Topp. Molecular Pharmaceutics. Invited manuscript for special issue, “Advances in Biophysical and Bioanalytical Protein Characterization”. Submitted August 17, 2011. Reviewers’ comments received November 16, 2011.
  21. Use of glass transitions in carbohydrate excipient design for lyophilized protein formulations. BC Roughton, EM Topp, and KV Camarda. Computers and Chemical Engineering, in press. DOI:10.1016/j.compchemeng.2011.07.018.
  22. Localized effects of hydration on lyophilized myoglobin by hydrogen/deuterium exchange mass spectrometry. A.M. Sophocleous, J Zhang and EM Topp, submitted to Biophysical Journal, June 24, 2011. Reviewers’ comments received August 15, 2011. Revised version submitted October 29, 2011.
  23. Proteins and peptides: Physical and chemical stability. A Sophocleous, J Zhang, L Iyer, S Chandrasekhar and EM Topp, Encyclopedia of Pharmaceutical Science and Technology, 4th ed., James Swarbrick, D.Sc., Ph.D., Editor. Informa Healthcare, New York, NY. Submitted April 26, 2011.
  24. Adhesive/dentin interface: the weak link in the composite restoration. P Spencer, Q Ye, J Park, EM Topp, A Misra, O Marangos, Y Wang, BS Bohaty, V Singh, F Sene, J Eslick, KV Camarda, JL Katz. Ann Biomed Eng. 38(6): 1989-2003, 2010.
  25. Thiol-disulfide interchange in the tocinoic acid/glutathione system during freezing and drying. M Thing, J Zhang, J Laurence and EM Topp. J Pharm Sci, 99/12: 4849-4856, 2010. DOI 10.1002/jps.22206.
  26. Effect of photoinitiator system and water content on dynamic mechanical properties of a light-cured bisGMA/HEMA dental resin.[ J Park, Q Ye, EM Topp, SL Kieweg and P Spencer. J Biomed Mater Res A. 93A/4: 1245-1251, 2010. DOI: 10.1002/jbm.a.32617.
  27. Immune response to controlled release of immunomodulating peptides in an experimental autoimmune encephalomyelitis (EAE) mouse model. H Zhao, P Kiptoo, TD Williams, TJ Siahaan and EM Topp. J Control Release. 141: 145-152, 2010. DOI: 10.1016/j.jconrel.2009.09.002.
  28. Protein conformation and reactivity in amorphous solids. S Sinha, S Xie and EM Topp, in Formulation and Process Development Strategies for Manufacturing of Biopharmaceuticals, F Jameel and S Hershenson, eds., John Wiley and Sons, Hoboken, NJ, 2010. ISBN: 978-0-470-11812-2. pp. 493-506.
  29. Chemical instability in peptide and protein pharmaceuticals. EM Topp, L Zhang, H Zhao, RW Payne, GJ Evans and MC Manning. Formulation and Process Development Strategies for Manufacturing Biopharmaceuticals, F Jameel and S Hershenson, eds., John Wiley and Sons, Hoboken, NJ, 2010. ISBN: 978-0-470-11812-2. pp. 41-68.

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