SARS-CoV-2 Fusion Peptide has a Greater Membrane Perturbating Effect than SARS-CoV with Highly Specific Dependence on Ca²⁺
A. L. Lai and J. H. Freed.
J. Mol. Biol. 433, 166946 (2021)
<doi:10.1016/j.jmb.2021.166946>
PMID: 33744314      PMCID: PMC7969826
 

Microsecond dynamics in proteins by two-dimensional ESR. II. Addressing computational challenges
P. Gupta, K. Chaudhari, and J. H. Freed.
J. Chem. Phys. 154, 084115 (2021)
Supporting Information
<doi:10.1063/5.0042441>
PMID: 33639766      PMCID: PMC7928224
 

Microsecond Exchange Processes Studied by Two-Dimensional ESR at 95 GHz
B. Dzikovski, V. V. Khramtsov, S. Chandrasekaran, C. Dunnam, M. Shah, and J. H. Freed.
J. Am. Chem. Soc. 142, 21368-21381 (2020)
Supporting Information
<doi:10.1021/jacs.0c09469>
PMID: 33305945      PMCID: PMC7810061
 

Engineered chemotaxis core signaling units indicate a constrained kinase-off state
A. R. Muok, T. K. Chua, M. Srivastava, W. Yang, Z. Maschmann, P. P. Borbat, J. Chong, S. Zhang, J. H. Freed, A. Briegel, B. R. Crane.
Sci. Signal. 13, eabc1328 (2020)
Supporting Information
<doi:10.1126/scisignal.abc1328>
PMID: 33172954      PMCID: PMC7790435
 

Structural Dynamics by NMR in the Solid State: The Unified MOMD Perspective Applied to Organic Frameworks with Interlocked Molecules
E. Meirovitch, Z. Liang, and J. H. Freed.
J. Phys. Chem. B 124, 6225-6235 (2020)
Supporting Information
<doi:10.1021/acs.jpcb.0c03687>
PMID: 32584038      PMCID: PMC7666760
 

Conformational Dynamics in Extended RGD-Containing Peptides
W. R. Lindemann, A. J. Mijalis, J. L. Alonso, P. P. Borbat, J. H. Freed, M. A. Arnaout, B. L. Pentelute, and J. H. Ortony.
Biomacromolecules 21, 2786-2794 (2020)
Supporting Information
<doi:10.1021/acs.biomac.0c00506>
PMID: 32469507      PMCID: PMC7388056
 

Microsecond dynamics in proteins by two-dimensional ESR: Predictions
P. Gupta, Z. Liang, and J. H. Freed.
J. Chem. Phys. 152, 214112 (2020)
Supporting Information
<doi:10.1063/5.0008094>
PMID: 32505151      PMCID: PMC7863697
 

George K. Fraenkel, Electron Spin Resonance Pioneer
J.H. Freed.
In Pioneers of Magnetic Resonance. Strom, E. T., Mainz, V. V., Eds.   American Chemical Society: Washington, DC, ACS Symposium Series, 2020; Volume 1349, Chapter 8, pp. 137-154.
<doi:10.1021/bk-2020-1349.ch008>
PMID: None-book      PMCID: None-book
 

High-yield production in E. coli and characterization of full-length functional p13^II protein from human T-cell leukemia virus type 1
E. R. Georgieva, P. P. Borbat, C. Fanouraki, J. H. Freed.
Protein Expr. Purif. 173, 105659 (2020)
Supporting Information
<doi:10.1016/j.pep.2020.105659>
PMID: 32360379      PMCID: PMC7266171
 

Ca²⁺ Ions Promote Fusion of Middle East Respiratory Syndrome Coronavirus with Host Cells and Increase Infectivity
M. R. Straus, T. Tang, A. L. Lai, A. Flegel, M. Bidon, J. H. Freed, S. Daniel, G. R. Whittaker.
J. Virol. 94, e00426-20 (2020)
Supporting Information
<doi:10.1128/JVI.00426-20>
PMID: 32295925      PMCID: PMC7307142
 

Calcium Ions Directly Interact with the Ebola Virus Fusion Peptide To Promote Structure-Function Changes That Enhance Infection
L. Nathan, A. L. Lai, J. K. Millet, M. R. Straus, J. H. Freed, G. R. Whittaker, and S. Daniel.
ACS Infect. Dis. 6, 250-260 (2020)
Supporting Information
<doi:10.1021/acsinfecdis.9b00296>
PMID: 31746195      PMCID: PMC7040957
 

Local ordering and dynamics in anisotropic media by magnetic resonance: from liquid crystals to proteins
E. Meirovitch & J. H. Freed.
Liq. Cryst. 47, 1926-1954 (2020)
<doi:10.1080/02678292.2019.1622158>
PMID: 32435078      PMCID: PMC7239324
 

The asymmetric function of Dph1–Dph2 heterodimer in diphthamide biosynthesis
M. Dong, E. E. Dando, I. Kotliar, X. Su, B. Dzikovski, J. H. Freed, and H. Lin.
J. Biol. Inorg. Chem. 24, 777-782 (2019)
<doi:10.1007/s00775-019-01702-0>
PMID: 31463593      PMCID: PMC6893874
 

Insights into histidine kinase activation mechanisms from the monomeric blue light sensor EL346
I. Dikiy, U. R. Edupuganti, R. R. Abzalimov, P. P. Borbat, M. Srivastava, J. H. Freed, and K. H. Gardner.
Proc. Natl. Acad. Sci. 116, 4963-4972 (2019)
Supporting Information
<doi:10.1073/pnas.1813586116>
PMID: 30808807      PMCID: PMC6421462
 

Comment on "Distinct Populations in Spin-Label EPR Spectra from Nitroxides."
E. Meirovitch, B. Dzikovski, and J. H. Freed.
J. Phys. Chem. B 123, 2454-2456 (2019)
Supporting Information
<doi:10.1021/acs.jpcb.8b07730>
PMID: 30768266      PMCID: PMC6497408
 

Singular Value Decomposition Method To Determine Distance Distributions in Pulsed Dipolar Electron Spin Resonance: II. Estimating Uncertainty
M. Srivastava and J. H. Freed.
J. Phys. Chem. A 123, 359-370 (2019)
Supporting Information
<doi:10.1021/acs.jpca.8b07673>
PMID: 30525624      PMCID: PMC6372347
 

Cofactors are essential constituents of stable and seeding-active tau fibrils
Y. Fichou, Y. Lin, J. N. Rauch, M. Vigers, Z. Zeng, M. Srivastava, T. J. Keller, J. H. Freed, K. S. Kosik, and S. Han.
Proc. Natl. Acad. Sci. 115, 13234-13239 (2018)
Supporting Information
<doi:10.1073/pnas.1810058115>
PMID: 30538196      PMCID: PMC6310788
 

Phenyl-Ring Dynamics in Amyloid Fibrils and Proteins: The Microscopic-Order-Macroscopic-Disorder Perspective
E. Meirovitch, Z. Liang, and J. H. Freed.
J. Phys. Chem. B 122, 8675-8684 (2018)
Supporting Information
<doi:10.1021/acs.jpcb.8b06330>
PMID: 30141954      PMCID: PMC6174686
 

A facile approach for the in vitro assembly of multimeric membrane transport proteins
E. A. Riederer, P. J. Focke, E. R. Georgieva, N. Akyuz, K. Matulef, P. P. Borbat, J. H. Freed, S. C. Blanchard, O. Boudker, and F. I. Valiyaveetil.
eLife 7, e36478 (2018)
Supporting Information
<doi:10.7554/eLife.36478>
PMID: 29889023      PMCID: PMC6025958
 

Open and Closed Form of Maltose Binding Protein in Its Native and Molten Globule State As Studied by Electron Paramagnetic Resonance Spectroscopy
B. Selmke, P. P. Borbat, C. Nickolaus, R. Varadarajan, J. H. Freed, and W. E. Trommer.
Biochemistry 57, 5507-5512 (2018)
Supporting Information
<doi:10.1021/acs.biochem.8b00322>
PMID: 30004675      PMCID: PMC6211580
 

Site-Specific Incorporation of a Cu²⁺ Spin Label into Proteins for Measuring Distances by Pulsed Dipolar Electron Spin Resonance Spectroscopy
G. E. Merz, P. P. Borbat, A. R. Muok, M. Srivastava, D. N. Bunck, J. H. Freed, and B. R. Crane.
J. Phys. Chem. B 122, 9443-9451 (2018)
Supporting Information
<doi:10.1021/acs.jpcb.8b05619>
PMID: 30222354      PMCID: PMC6215709
 

MOMD Analysis of NMR Line Shapes from AΒ-Amyloid Fibrils: A New Tool for Characterizing Molecular Environments in Protein Aggregates
E. Meirovitch, Z. Liang, and J. H. Freed.
J. Phys. Chem. B 122, 4793-4801 (2018)
Supporting Information
<doi:10.1021/acs.jpcb.8b02181>
PMID: 29624402      PMCID: PMC5945340
 

Structural basis for membrane anchoring and fusion regulation of the herpes simplex virus fusogen gB
R. S. Cooper, E. R. Georgieva, P. P. Borbat, J. H. Freed, and E. E. Heldwein.
Nat. Struct. Mol. Biol. 25, 416-424 (2018)
Supporting Information
<doi:10.1038/s41594-018-0060-6>
PMID: 29728654      PMCID: PMC5942590
 

Organometallic and radical intermediates reveal mechanism of diphthamide biosynthesis
M. Dong, V. Kathiresan, M. K. Fenwick, A. T. Torelli, Y. Zhang, J. D. Caranto, B. Dzikovski, A. Sharma, K. M. Lancaster, J. H. Freed, S. E. Ealick, B. M. Hoffman, and H. Lin.
Science 359, 1247-1250 (2018)
Supporting Information
<doi:10.1126/science.aao6595>
PMID: 29590073      PMCID: PMC6066404
 

Protein dynamics in the solid-state from ²H NMR lineshape analysis. III. MOMD in the presence of Magic Angle Spinning
E. Meirovitch, Z. Liang, J. H. Freed.
Solid State Nucl. Magn. Reson. 89, 35-44 (2018)
<doi:10.1016/j.ssnmr.2017.11.001>
PMID: 29208317      PMCID: PMC5772661