Category: Frieden Publications

Dr. Frieden’s Publications

Structure-Function Analysis of the Curli Accessory Protein CsgE Defines Surfaces Essential for Coordinating Amyloid Fiber Formation.

Klein R.D., Shu Q., Cusumano Z.T., Nagamatsu K., Gualberto N.C., Lynch A.J.L., Wu C., Wang W., Jain N., Pinkner J.S., Amarasinghe G.K., Hultgren S.J., Frieden C., & Chapman M.R. (2018). “Structure-Function Analysis of the Curli Accessory Protein CsgE Defines Surfaces Essential for Coordinating Amyloid Fiber Formation.” MBio. 2018 Jul 17;9(4). pii: e01349-18. doi: 10.1128/mBio.01349-18. (Abstract)

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)