Year |
Citation |
Score |
2019 |
Burnett K, Paul M, Ventre K, Samanez A, Jaswal S. Comparative Investigation of Native-State Dynamics in Trypsin Functional Variants by Hydrogen Exchange Mass Spectrometry Biophysical Journal. 116: 474a. DOI: 10.1016/J.Bpj.2018.11.2561 |
0.309 |
|
2019 |
Nagelj N, Kim M, Mathias K, Jaswal S. N-HXMS: A Method to Directly Measure Protein Folding and Stability under Native Conditions Biophysical Journal. 116: 192a. DOI: 10.1016/j.bpj.2018.11.1063 |
0.313 |
|
2015 |
Witten J, Ruschak A, Poterba T, Jaramillo A, Miranker AD, Jaswal SS. Mapping Protein Conformational Landscapes under Strongly Native Conditions with Hydrogen Exchange Mass Spectrometry. The Journal of Physical Chemistry. B. 119: 10016-24. PMID 26146955 DOI: 10.1021/Acs.Jpcb.5B04528 |
0.487 |
|
2014 |
Wagaman AS, Coburn A, Brand-Thomas I, Dash B, Jaswal SS. A comprehensive database of verified experimental data on protein folding kinetics. Protein Science : a Publication of the Protein Society. 23: 1808-12. PMID 25229122 DOI: 10.1002/Pro.2551 |
0.44 |
|
2014 |
Cohen P, Dill KA, Jaswal SS. Modeling the solvation of nonpolar amino acids in guanidinium chloride solutions. The Journal of Physical Chemistry. B. 118: 10618-23. PMID 25141127 DOI: 10.1021/Jp506379R |
0.31 |
|
2014 |
Wagaman AS, Jaswal SS. Capturing protein folding-relevant topology via absolute contact order variants Journal of Theoretical and Computational Chemistry. 13. DOI: 10.1142/S0219633614500059 |
0.452 |
|
2013 |
Jaswal SS. Biological insights from hydrogen exchange mass spectrometry. Biochimica Et Biophysica Acta. 1834: 1188-201. PMID 23117127 DOI: 10.1016/J.Bbapap.2012.10.011 |
0.385 |
|
2013 |
Jaswal SS, Fuhrmann CN, Ota N, Rader SD, Agard DA. α-Lytic Protease Handbook of Proteolytic Enzymes. 3: 2558-2565. DOI: 10.1016/B978-0-12-382219-2.00567-6 |
0.36 |
|
2007 |
Jaswal SS, Miranker AD. Scope and utility of hydrogen exchange as a tool for mapping landscapes. Protein Science : a Publication of the Protein Society. 16: 2378-90. PMID 17962401 DOI: 10.1110/Ps.072994207 |
0.431 |
|
2005 |
Jaswal SS, Truhlar SM, Dill KA, Agard DA. Comprehensive analysis of protein folding activation thermodynamics reveals a universal behavior violated by kinetically stable proteases. Journal of Molecular Biology. 347: 355-66. PMID 15740746 DOI: 10.1016/J.Jmb.2005.01.032 |
0.576 |
|
2002 |
Jaswal SS, Sohl JL, Davis JH, Agard DA. Energetic landscape of alpha-lytic protease optimizes longevity through kinetic stability. Nature. 415: 343-6. PMID 11797014 DOI: 10.1038/415343A |
0.673 |
|
1999 |
Cunningham EL, Jaswal SS, Sohl JL, Agard DA. Kinetic stability as a mechanism for protease longevity. Proceedings of the National Academy of Sciences of the United States of America. 96: 11008-14. PMID 10500115 DOI: 10.1073/Pnas.96.20.11008 |
0.643 |
|
1998 |
Sohl JL, Jaswal SS, Agard DA. Unfolded conformations of alpha-lytic protease are more stable than its native state. Nature. 395: 817-9. PMID 9796818 DOI: 10.1038/27470 |
0.659 |
|
1997 |
Jaswal SS, Sohl JI, Agard PA. Thermodynamic analysis of kinetic stability in alpha-lytic protease Faseb Journal. 11: A834. |
0.375 |
|
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