# Publications Search Within Results Search Within Results search ## 20 results Show filters filter\_alt Sort by Year of PublicationAlphabetical A-Z sort ## 20 results Download 20 citations download- [BibTeX](/node/1915601/export?format=bibtex) - [EndNote X3 XML](/node/1915601/export?format=endnote8) - [EndNote 7 XML](/node/1915601/export?format=endnote7) - [Endnote tagged](/node/1915601/export?format=tagged) - [Marc](/node/1915601/export?format=marc) - [PubMedId](/node/1915601/export?format=pubmed_id) - [RIS](/node/1915601/export?format=ris) ### 2026 Jeremy B. Conway, Sohaib Abdul Rehman, and Maxim B. Prigozhin. 2026. “[DNA-Functionalized Nanoparticles for Multicolor Cathodoluminescence Imaging](/publication/dna-functionalized-nanoparticles-multicolor-cathodoluminescence-imaging)”. BioRxiv. doi:https://doi.org/10.64898/2026.04.07.716901 Jeremy B. Conway, Sohaib Abdul Rehman, and Maxim B. Prigozhin. 2026. “[DNA-Functionalized Nanoparticles for Multicolor Cathodoluminescence Imaging](/publication/dna-functionalized-nanoparticles-multicolor-cathodoluminescence-imaging)”. BioRxiv. doi:https://doi.org/10.64898/2026.04.07.716901 - [ descriptionPublisher's Version](https://www.biorxiv.org/content/10.64898/2026.04.07.716901v1) - [ picture\_as\_pdfPreprint](/sites/g/files/omnuum7281/files/2026-04/Main_text.pdf) - [ picture\_as\_pdfSupplementary Information](/sites/g/files/omnuum7281/files/2026-04/SI.pdf) - [ descriptionPublisher's Version](https://www.biorxiv.org/content/10.64898/2026.04.07.716901v1) - [ picture\_as\_pdfPreprint](/sites/g/files/omnuum7281/files/2026-04/Main_text.pdf) - [ picture\_as\_pdfSupplementary Information](/sites/g/files/omnuum7281/files/2026-04/SI.pdf) ### 2025 Xingchi Yan, Polly Y. Yu, A. Srinivasan, S. K. Sreenivas, Jeremy B. Conway, and Maxim B. Prigozhin. 2025. “[Identifying Intermolecular Interactions in Single-Molecule Localization Microscopy](/publication/identifying-intermolecular-interactions-single-molecule-localization-microscopy)”. Proc. Natl. Acad. Sci. USA, 122, 20 Xingchi Yan, Polly Y. Yu, A. Srinivasan, S. K. Sreenivas, Jeremy B. Conway, and Maxim B. Prigozhin. 2025. “[Identifying Intermolecular Interactions in Single-Molecule Localization Microscopy](/publication/identifying-intermolecular-interactions-single-molecule-localization-microscopy)”. Proc. Natl. Acad. Sci. USA, 122, 20 - [ descriptionPublisher's Version](https://www.pnas.org/doi/10.1073/pnas.2409426122) - [ picture\_as\_pdfPaper](/sites/g/files/omnuum7281/files/2026-04/yan-et-al-2025-identifying-intermolecular-interactions-in-single-molecule-localization-microscopy.pdf) - [ picture\_as\_pdfSupplementary Information](/sites/g/files/omnuum7281/files/2026-04/pnas.2409426122.sapp_.pdf) - [ descriptionPublisher's Version](https://www.pnas.org/doi/10.1073/pnas.2409426122) - [ picture\_as\_pdfPaper](/sites/g/files/omnuum7281/files/2026-04/yan-et-al-2025-identifying-intermolecular-interactions-in-single-molecule-localization-microscopy.pdf) - [ picture\_as\_pdfSupplementary Information](/sites/g/files/omnuum7281/files/2026-04/pnas.2409426122.sapp_.pdf) Sohaib Abdul Rehman, Jeremy B. Conway, Amy Nichols, Edward R. Soucy, Amanda Dee, Kristal Stevens, Simon Merminod, Isabella MacNaughton, Abigail Curtis, and Maxim B. Prigozhin. 2025. “[Multicolor Cathodoluminescence Imaging of Single Lanthanide Nanoparticles](/publication/multicolor-cathodoluminescence-imaging-single-lanthanide-nanoparticles)”. Nature Communications, 16, 1 Sohaib Abdul Rehman, Jeremy B. Conway, Amy Nichols, Edward R. Soucy, Amanda Dee, Kristal Stevens, Simon Merminod, Isabella MacNaughton, Abigail Curtis, and Maxim B. Prigozhin. 2025. “[Multicolor Cathodoluminescence Imaging of Single Lanthanide Nanoparticles](/publication/multicolor-cathodoluminescence-imaging-single-lanthanide-nanoparticles)”. Nature Communications, 16, 1 - [ descriptionPublisher's Version](https://www.nature.com/articles/s41467-025-64409-8) - [ picture\_as\_pdfPaper](/sites/g/files/omnuum7281/files/2026-04/s41467-025-64409-8.pdf) - [ picture\_as\_pdfSupplementary Information](/sites/g/files/omnuum7281/files/2026-04/41467_2025_64409_MOESM1_ESM-compressed.pdf) - [ descriptionMCB news story](https://www.mcb.harvard.edu/department/news/a-new-colorful-method-for-nanoscale-imaging-harnesses-electron-induced-light/) - [ descriptionPublisher's Version](https://www.nature.com/articles/s41467-025-64409-8) - [ picture\_as\_pdfPaper](/sites/g/files/omnuum7281/files/2026-04/s41467-025-64409-8.pdf) - [ picture\_as\_pdfSupplementary Information](/sites/g/files/omnuum7281/files/2026-04/41467_2025_64409_MOESM1_ESM-compressed.pdf) - [ descriptionMCB news story](https://www.mcb.harvard.edu/department/news/a-new-colorful-method-for-nanoscale-imaging-harnesses-electron-induced-light/) ### 2023 S. Dagdeviren, M. F. Hoang, M. Sarikhani, V. Meier, J. C. Benoit, M. C. Okawa, V. Y. Melnik, E. M. Ricci-Blair, N. Foot, R. H. Friedline, X. Hu, L. A. Tauer, A. Srinivasan, M. B. Prigozhin, S. K. Shenoy, S. Kumar, J. K. Kim, and R. T. Lee. 2023. “[An Insulin-Regulated Arrestin Domain Protein Controls Hepatic Glucagon Action ](/publications/insulin-regulated-arrestin-domain-protein-controls-hepatic-glucagon-action)”. Journal of Biological Chemistry, 299, 8, Pp. 105045 S. Dagdeviren, M. F. Hoang, M. Sarikhani, V. Meier, J. C. Benoit, M. C. Okawa, V. Y. Melnik, E. M. Ricci-Blair, N. Foot, R. H. Friedline, X. Hu, L. A. Tauer, A. Srinivasan, M. B. Prigozhin, S. K. Shenoy, S. Kumar, J. K. Kim, and R. T. Lee. 2023. “[An Insulin-Regulated Arrestin Domain Protein Controls Hepatic Glucagon Action ](/publications/insulin-regulated-arrestin-domain-protein-controls-hepatic-glucagon-action)”. Journal of Biological Chemistry, 299, 8, Pp. 105045 - [ descriptionPublisher's Version](https://www.jbc.org/article/S0021-9258(23)02073-2/fulltext) - [ picture\_as\_pdfSI](/sites/g/files/omnuum7281/files/prigozhin/files/mmc1.pdf) - [ picture\_as\_pdfPaper](/sites/g/files/omnuum7281/files/prigozhin/files/piis0021925823020732.pdf) - [ descriptionPublisher's Version](https://www.jbc.org/article/S0021-9258(23)02073-2/fulltext) - [ picture\_as\_pdfSI](/sites/g/files/omnuum7281/files/prigozhin/files/mmc1.pdf) - [ picture\_as\_pdfPaper](/sites/g/files/omnuum7281/files/prigozhin/files/piis0021925823020732.pdf) ### 2019 M. B. Prigozhin*, P. C. Maurer*, A. M. Courtis, M. D. Wisser N. Liu, C. Siefe, B. Tian, E. Chan, G. Song, S. Fischer, S. Aloni, D. F. Ogletree, E. S. Barnard, L.-M. Joubert, J. Rao, A. P. Alivisatos, R. M. Macfarlane, B. E. Cohen, Y. Cui, J. A. Dionne, and S. Chu. 2019. “[Bright Sub-20-Nm Cathodoluminescent Nanoprobes for Electron Microscopy](https://www.nature.com/articles/s41565-019-0395-0)”. Nature Nanotechnology, 14, Pp. 420-25 M. B. Prigozhin*, P. C. Maurer*, A. M. Courtis, M. D. Wisser N. Liu, C. Siefe, B. Tian, E. Chan, G. Song, S. Fischer, S. Aloni, D. F. Ogletree, E. S. Barnard, L.-M. Joubert, J. Rao, A. P. Alivisatos, R. M. Macfarlane, B. E. Cohen, Y. Cui, J. A. Dionne, and S. Chu. 2019. “[Bright Sub-20-Nm Cathodoluminescent Nanoprobes for Electron Microscopy](https://www.nature.com/articles/s41565-019-0395-0)”. Nature Nanotechnology, 14, Pp. 420-25 - add\_circle\_outline do\_not\_disturb\_on Abstract - [ descriptionPublisher's Version](https://www.nature.com/articles/s41565-019-0395-0) - [ picture\_as\_pdfprigozhin\_naturenano\_2019...](/sites/g/files/omnuum7281/files/prigozhin/files/prigozhin_naturenano_main.pdf) - [ picture\_as\_pdfprigozhin\_naturenano\_2019...](/sites/g/files/omnuum7281/files/prigozhin/files/prigozhin_naturenano_si.pdf) Electron microscopy has been instrumental in our understanding of complex biological systems. Although electron microscopy reveals cellular morphology with nanoscale resolution, it does not provide information on the location of different types of... - [ descriptionPublisher's Version](https://www.nature.com/articles/s41565-019-0395-0) - [ picture\_as\_pdfprigozhin\_naturenano\_2019...](/sites/g/files/omnuum7281/files/prigozhin/files/prigozhin_naturenano_main.pdf) - [ picture\_as\_pdfprigozhin\_naturenano\_2019...](/sites/g/files/omnuum7281/files/prigozhin/files/prigozhin_naturenano_si.pdf) M. B. Prigozhin*, Y. Zhang*, K. Schulten, M. Gruebele, and T. V. Pogorelov. 2019. “[Fast Pressure-Jump All-Atom Simulations and Experiments Reveal Site-Specific Protein Dehydration-Folding Dynamics](https://www.pnas.org/content/116/12/5356)”. Proc. Natl. Acad. Sci. USA, 116, 12, Pp. 5356-61 M. B. Prigozhin*, Y. Zhang*, K. Schulten, M. Gruebele, and T. V. Pogorelov. 2019. “[Fast Pressure-Jump All-Atom Simulations and Experiments Reveal Site-Specific Protein Dehydration-Folding Dynamics](https://www.pnas.org/content/116/12/5356)”. Proc. Natl. Acad. Sci. USA, 116, 12, Pp. 5356-61 - add\_circle\_outline do\_not\_disturb\_on Abstract - [ descriptionPublisher's Version](https://www.pnas.org/content/116/12/5356) - [ picture\_as\_pdfprigozhin\_pnas\_2019.pdf](/sites/g/files/omnuum7281/files/prigozhin/files/prigozhin_pnas_2019.pdf) As theory and experiment have shown, protein dehydration is a major contributor to protein folding. Dehydration upon folding can be characterized directly by all-atom simulations of fast pressure drops, which create desolvated pockets inside the nascent... - [ descriptionPublisher's Version](https://www.pnas.org/content/116/12/5356) - [ picture\_as\_pdfprigozhin\_pnas\_2019.pdf](/sites/g/files/omnuum7281/files/prigozhin/files/prigozhin_pnas_2019.pdf) Andrei G. Gasic, Mayank M. Boob, Maxim B. Prigozhin, Dirar Homouz, Caleb M. Daugherty, Martin Gruebele, and Margaret S. Cheung. 2019. “[Critical Phenomena in the Temperature-Pressure-Crowding Phase Diagram of a Protein](/publications/critical-phenomena-temperature-pressure-crowding-phase-diagram-protein)”. Physical Review X, 9, 4, Pp. 041035 Andrei G. Gasic, Mayank M. Boob, Maxim B. Prigozhin, Dirar Homouz, Caleb M. Daugherty, Martin Gruebele, and Margaret S. Cheung. 2019. “[Critical Phenomena in the Temperature-Pressure-Crowding Phase Diagram of a Protein](/publications/critical-phenomena-temperature-pressure-crowding-phase-diagram-protein)”. Physical Review X, 9, 4, Pp. 041035 - [ descriptionPublisher's Version](https://journals.aps.org/prx/abstract/10.1103/PhysRevX.9.041035) - [ picture\_as\_pdfphysrevx.9.041035.pdf](/sites/g/files/omnuum7281/files/prigozhin/files/physrevx.9.041035.pdf) - [ descriptionPublisher's Version](https://journals.aps.org/prx/abstract/10.1103/PhysRevX.9.041035) - [ picture\_as\_pdfphysrevx.9.041035.pdf](/sites/g/files/omnuum7281/files/prigozhin/files/physrevx.9.041035.pdf) ### 2015 M. B. Prigozhin*, S.-H. Chao*, S. Sukenik, T. V. Pogorelov, and M. Gruebele. 2015. “[Mapping Fast Protein Folding With Multiple-Site Fluorescent Probes](https://www.pnas.org/content/early/2015/06/11/1422683112.abstract)”. Proc. Natl. Acad. Sci. USA, 112, 26, Pp. 7966-71 M. B. Prigozhin*, S.-H. Chao*, S. Sukenik, T. V. Pogorelov, and M. Gruebele. 2015. “[Mapping Fast Protein Folding With Multiple-Site Fluorescent Probes](https://www.pnas.org/content/early/2015/06/11/1422683112.abstract)”. Proc. Natl. Acad. Sci. USA, 112, 26, Pp. 7966-71 - [ descriptionPublisher's Version](https://www.pnas.org/content/early/2015/06/11/1422683112.abstract) - [ picture\_as\_pdfprigozhin\_pnas\_2015.pdf](/sites/g/files/omnuum7281/files/prigozhin/files/prigozhin_pnas_2015.pdf) - [ descriptionPublisher's Version](https://www.pnas.org/content/early/2015/06/11/1422683112.abstract) - [ picture\_as\_pdfprigozhin\_pnas\_2015.pdf](/sites/g/files/omnuum7281/files/prigozhin/files/prigozhin_pnas_2015.pdf) A. J. Wirth*, Y. Liu*, M. B. Prigozhin, K. Schulten, and M. Gruebele. 2015. “[Comparing Fast Pressure Jump and Temperature Jump Protein Folding Experiments and Simulations](https://pubs.acs.org/doi/abs/10.1021/jacs.5b02474)”. J. Am. Chem. Soc., 137, 22, Pp. 7152-59 A. J. Wirth*, Y. Liu*, M. B. Prigozhin, K. Schulten, and M. Gruebele. 2015. “[Comparing Fast Pressure Jump and Temperature Jump Protein Folding Experiments and Simulations](https://pubs.acs.org/doi/abs/10.1021/jacs.5b02474)”. J. Am. Chem. Soc., 137, 22, Pp. 7152-59 - add\_circle\_outline do\_not\_disturb\_on Abstract - [ descriptionPublisher's Version](https://pubs.acs.org/doi/abs/10.1021/jacs.5b02474) - [ picture\_as\_pdfwirth\_jacs\_2015.pdf](/sites/g/files/omnuum7281/files/prigozhin/files/wirth_jacs_2015.pdf) The unimolecular folding reaction of small proteins is now amenable to a very direct mechanistic comparison between experiment and simulation. We present such a comparison of microsecond pressure and temperature jump refolding kinetics of the engineered... - [ descriptionPublisher's Version](https://pubs.acs.org/doi/abs/10.1021/jacs.5b02474) - [ picture\_as\_pdfwirth\_jacs\_2015.pdf](/sites/g/files/omnuum7281/files/prigozhin/files/wirth_jacs_2015.pdf) ### 2014 P. B. Lawrence*, Y. Gavrilov*, S. S. Matthews, M. I. Langlois, D. Shental-Bechor, H. M. Greenblatt, B. K. Pandey, M. S. Smith, R. Paxman, C. B. Torgerson, J. P. Merrell, C. Ritz, M. B. Prigozhin, Y. Levy, and J. L. Price. 2014. “[Criteria for Selecting PEGylation Sites on Proteins for Higher Thermodynamic and Proteolytic Stability](https://pubs.acs.org/doi/abs/10.1021/ja5095183)”. J. Am. Chem. Soc., 136, 50, Pp. 17547-60 P. B. Lawrence*, Y. Gavrilov*, S. S. Matthews, M. I. Langlois, D. Shental-Bechor, H. M. Greenblatt, B. K. Pandey, M. S. Smith, R. Paxman, C. B. Torgerson, J. P. Merrell, C. Ritz, M. B. Prigozhin, Y. Levy, and J. L. Price. 2014. “[Criteria for Selecting PEGylation Sites on Proteins for Higher Thermodynamic and Proteolytic Stability](https://pubs.acs.org/doi/abs/10.1021/ja5095183)”. J. Am. Chem. Soc., 136, 50, Pp. 17547-60 - add\_circle\_outline do\_not\_disturb\_on Abstract - [ descriptionPublisher's Version](https://pubs.acs.org/doi/abs/10.1021/ja5095183) - [ picture\_as\_pdflawrence\_jacs\_2014.pdf](/sites/g/files/omnuum7281/files/prigozhin/files/lawrence_jacs_2014.pdf) PEGylation of protein side chains has been used for more than 30 years to enhance the pharmacokinetic properties of protein drugs. However, there are no structure- or sequence-based guidelines for selecting sites that provide optimal PEG-based... - [ descriptionPublisher's Version](https://pubs.acs.org/doi/abs/10.1021/ja5095183) - [ picture\_as\_pdflawrence\_jacs\_2014.pdf](/sites/g/files/omnuum7281/files/prigozhin/files/lawrence_jacs_2014.pdf) M. B. Prigozhin, G. E. Scott, and S. Denos. 2014. “[Mechanical Modeling and Computer Simulation of Protein Folding](https://pubs.acs.org/doi/abs/10.1021/ed400719c)”. J. Chem. Ed., 91, 11, Pp. 1939-42 M. B. Prigozhin, G. E. Scott, and S. Denos. 2014. “[Mechanical Modeling and Computer Simulation of Protein Folding](https://pubs.acs.org/doi/abs/10.1021/ed400719c)”. J. Chem. Ed., 91, 11, Pp. 1939-42 - add\_circle\_outline do\_not\_disturb\_on Abstract - [ descriptionPublisher's Version](https://pubs.acs.org/doi/abs/10.1021/ed400719c) - [ picture\_as\_pdfprigozhin\_jchemed\_2014.pd...](/sites/g/files/omnuum7281/files/prigozhin/files/prigozhin_jchemed_2014.pdf) In this activity, science education and modern technology are bridged to teach students at the high school and undergraduate levels about protein folding and to strengthen their model building skills. Students are guided from a textbook picture of a... - [ descriptionPublisher's Version](https://pubs.acs.org/doi/abs/10.1021/ed400719c) - [ picture\_as\_pdfprigozhin\_jchemed\_2014.pd...](/sites/g/files/omnuum7281/files/prigozhin/files/prigozhin_jchemed_2014.pdf) Y. Liu, M. B. Prigozhin, K. Schulten, and M. Gruebele. 2014. “[Observation of Complete Pressure-Jump Protein Refolding in Molecular Dynamics Simulation and Experiment](https://pubs.acs.org/doi/abs/10.1021/ja412639u)”. J. Am. Chem. Soc., 136, 11, Pp. 4265-72 Y. Liu, M. B. Prigozhin, K. Schulten, and M. Gruebele. 2014. “[Observation of Complete Pressure-Jump Protein Refolding in Molecular Dynamics Simulation and Experiment](https://pubs.acs.org/doi/abs/10.1021/ja412639u)”. J. Am. Chem. Soc., 136, 11, Pp. 4265-72 - add\_circle\_outline do\_not\_disturb\_on Abstract - [ descriptionPublisher's Version](https://pubs.acs.org/doi/abs/10.1021/ja412639u) - [ picture\_as\_pdfliu\_jacs\_2014.pdf](/sites/g/files/omnuum7281/files/prigozhin/files/liu_jacs_2014.pdf) Density is an easily adjusted variable in molecular dynamics (MD) simulations. Thus, pressure-jump (P-jump)-induced protein refolding, if it could be made fast enough, would be ideally suited for comparison with MD. Although pressure denaturation perturbs... - [ descriptionPublisher's Version](https://pubs.acs.org/doi/abs/10.1021/ja412639u) - [ picture\_as\_pdfliu\_jacs\_2014.pdf](/sites/g/files/omnuum7281/files/prigozhin/files/liu_jacs_2014.pdf) - Previous page chevron\_left - [1](?page=0 "Current page") - [2](?page=1 "Go to page 2") - [ Next page chevron\_right ](?page=1 "Go to next page")