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Neupane, K., Foster, D. A. N., Dee, D. R., Yu, H., Wang, F., Woodside, M. T. (2016) Direct observation of transition paths during the folding of proteins and nucleic acids. Science, 352 (6282). 239-242 doi:10.1126/science.aad0637

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Reference TypeJournal (article/letter/editorial)
TitleDirect observation of transition paths during the folding of proteins and nucleic acids
JournalScience
AuthorsNeupane, K.Author
Foster, D. A. N.Author
Dee, D. R.Author
Yu, H.Author
Wang, F.Author
Woodside, M. T.Author
Year2016 (April 8)Volume352
Issue6282
PublisherAmerican Association for the Advancement of Science (AAAS)
DOIdoi:10.1126/science.aad0637Search in ResearchGate
Generate Citation Formats
Mindat Ref. ID2803650Long-form Identifiermindat:1:5:2803650:8
GUID0
Full ReferenceNeupane, K., Foster, D. A. N., Dee, D. R., Yu, H., Wang, F., Woodside, M. T. (2016) Direct observation of transition paths during the folding of proteins and nucleic acids. Science, 352 (6282). 239-242 doi:10.1126/science.aad0637
Plain TextNeupane, K., Foster, D. A. N., Dee, D. R., Yu, H., Wang, F., Woodside, M. T. (2016) Direct observation of transition paths during the folding of proteins and nucleic acids. Science, 352 (6282). 239-242 doi:10.1126/science.aad0637
In(2016, April) Science Vol. 352 (6282) American Association for the Advancement of Science (AAAS)

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Greenleaf, W. J., Frieda, K. L., Foster, D. A. N., Woodside, M. T., Block, S. M. (2008) Direct Observation of Hierarchical Folding in Single Riboswitch Aptamers. Science, 319 (5863). 630-633 doi:10.1126/science.1151298
Neupane, Krishna, Ritchie, Dustin B., Yu, Hao, Foster, Daniel A. N., Wang, Feng, Woodside, Michael T. (2012) Transition Path Times for Nucleic Acid Folding Determined from Energy-Landscape Analysis of Single-Molecule Trajectories. Physical Review Letters, 109 (6). doi:10.1103/physrevlett.109.068102
Neupane, Krishna, Hoffer, Noel Q., Woodside, M. T. (2018) Measuring the Local Velocity along Transition Paths during the Folding of Single Biological Molecules. Physical Review Letters, 121 (1). doi:10.1103/physrevlett.121.018102
Hoffer, Noel Q., Neupane, Krishna, Woodside, Michael T. (2021) Observing the base-by-base search for native structure along transition paths during the folding of single nucleic acid hairpins. Proceedings of the National Academy of Sciences, 118 (49) doi:10.1073/pnas.2101006118
Woodside, M. T., Anthony, P. C., Behnke-Parks, W. M., Larizadeh, K., Herschlag, D., Block, S. M. (2006) Direct Measurement of the Full, Sequence-Dependent Folding Landscape of a Nucleic Acid. Science, 314 (5801). 1001-1004 doi:10.1126/science.1133601
Comstock, M. J., Whitley, K. D., Jia, H., Sokoloski, J., Lohman, T. M., Ha, T., Chemla, Y. R. (2015) Direct observation of structure-function relationship in a nucleic acid-processing enzyme. Science, 348 (6232). 352-354 doi:10.1126/science.aaa0130
Hoffer, Noel Q., Neupane, Krishna, Pyo, Andrew G. T., Woodside, Michael T. (2019) Measuring the average shape of transition paths during the folding of a single biological molecule. Proceedings of the National Academy of Sciences, 116 (17) 8125-8130 doi:10.1073/pnas.1816602116
Yu, H., Liu, X., Neupane, K., Gupta, A. N., Brigley, A. M., Solanki, A., Sosova, I., Woodside, M. T. (2012) Direct observation of multiple misfolding pathways in a single prion protein molecule. Proceedings of the National Academy of Sciences, 109 (14) 5283-5288 doi:10.1073/pnas.1107736109
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Yu, H., Gupta, A. N., Liu, X., Neupane, K., Brigley, A. M., Sosova, I., Woodside, M. T. (2012) Energy landscape analysis of native folding of the prion protein yields the diffusion constant, transition path time, and rates. Proceedings of the National Academy of Sciences, 109 (36) 14452-14457 doi:10.1073/pnas.1206190109
Pucci, F., Garris, C., Lai, C. P., Newton, A., Pfirschke, C., Engblom, C., Alvarez, D., Sprachman, M., Evavold, C., Magnuson, A., von Andrian, U. H., Glatz, K., Breakefield, X. O., Mempel, T. R., Weissleder, R., Pittet, M. J. (2016) SCS macrophages suppress melanoma by restricting tumor-derived vesicle-B cell interactions. Science, 352 (6282). 242-246 doi:10.1126/science.aaf1328
 
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