Category: Frieden Publications

Dr. Frieden’s Publications

Peptide-Level Interactions between Proteins and Small-Molecule Drug Candidates by Two Hydrogen-Deuterium Exchange MS-Based Methods: The Example of Apolipoprotein E3.

Wang H., Rempel D.L., Giblin D., Frieden C., & Gross M.L. (2017). “Peptide-Level Interactions between Proteins and Small-Molecule Drug Candidates by Two Hydrogen-Deuterium Exchange MS-Based Methods: The Example of Apolipoprotein E3.” Anal Chem. 2017 Oct 17;89(20):10687-10695. doi: 10.1021/acs.analchem.7b01121. Epub 2017 Sep 25. (Abstract)

Understanding Curli Amyloid-Protein Aggregation by Hydrogen-Deuterium Exchange and Mass Spectrometry.

Wang H., Shu Q., Rempel D.L., Frieden C., & Gross M.L. (2017). “Understanding Curli Amyloid-Protein Aggregation by Hydrogen-Deuterium Exchange and Mass Spectrometry.” Int J Mass Spectrom. 2017 Sep;420:16-23. doi: 10.1016/j.ijms.2016.10.006. Epub 2016 Oct 11. (Abstract)

A mechanism for lipid binding to apoE and the role of intrinsically disordered regions coupled to domain-domain interactions.

Frieden C., Wang H., & Ho C.M.W. (2017). “A mechanism for lipid binding to apoE and the role of intrinsically disordered regions coupled to domain-domain interactions.” Proc Natl Acad Sci U S A. 2017 Jun 13;114(24):6292-6297. doi: 10.1073/pnas.1705080114. Epub 2017 May 30. (Abstract)

Solution NMR structure of CsgE: Structural insights into a chaperone and regulator protein important for functional amyloid formation.

Shu Q., Krezel A.M., Cusumano Z.T., Pinkner J.S., Klein R., Hultgren S.J., & Frieden C. (2016). “Solution NMR structure of CsgE: Structural insights into a chaperone and regulator protein important for functional amyloid formation.” Proc Natl Acad Sci U S A. 2016 Jun 28;113(26):7130-5. doi: 10.1073/pnas.1607222113. Epub 2016 Jun 13. (Abstract)

Continuous and pulsed hydrogen-deuterium exchange and mass spectrometry characterize CsgE oligomerization.

Wang H., Shu Q., Rempel D.L., Frieden C., & Gross M.L. (2015). “Continuous and pulsed hydrogen-deuterium exchange and mass spectrometry characterize CsgE oligomerization.” Biochemistry. 2015 Oct 27;54(42):6475-81. doi: 10.1021/acs.biochem.5b00871. Epub 2015 Oct 14. (Abstract)

The binding of apolipoprotein E to oligomers and fibrils of amyloid-β alters the kinetics of amyloid aggregation.

Garai K., Verghese P.B., Baban B., Holtzman D.M., & Frieden C. (2014). “The binding of apolipoprotein E to oligomers and fibrils of amyloid-β alters the kinetics of amyloid aggregation.” Biochemistry. 2014 Oct 14;53(40):6323-31. doi: 10.1021/bi5008172. Epub 2014 Sep 25. (Abstract)