Carl Frieden, Ph.D.

Carl Frieden

Biochemistry and Molecular Biophysics

Lab Website
Graduate Programs (DBBS)
Publications (PubMed / NIH)

Office: 215 McDonnell Science Building
Phone: 314-362-3344


Protein folding, aggregation, intrinsically disordered proteins, fluorescence methods, ApoE lipoproteins and Alzheimer’s disease

Carl Frieden lab research

Select Publications

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)

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)

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)

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)

Wang H., Shu Q., Frieden C., & Gross M.L. (2017). “Deamidation slows Curli Amyloid-Protein Aggregation.” Biochemistry. 2017 Jun 13;56(23):2865-2872. doi: 10.1021/acs.biochem.7b00241. Epub 2017 May 26. (Abstract)

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)

Mondal T., Wang H., DeKoster G.T., Baban B., Gross M.L., & Frieden C. (2016). “ApoE: In Vitro Studies of a Small Molecule Effector.” Biochemistry. 2016 May 10;55(18):2613-21. doi: 10.1021/acs.biochem.6b00324. Epub 2016 Apr 27. (Abstract)

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)

Frieden C. (2015). “ApoE: the role of conserved residues in defining function.” Protein Sci. 2015 Jan;24(1):138-44. doi: 10.1002/pro.2597. Epub 2014 Dec 9. (Abstract)

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)

Hammes G. & Frieden C. (2014). “Robert A. Alberty” National Academy of Sciences. Biographical Memoirs. (Article)

Frieden, C. and Garai, K.
Concerning the structure of apoE.
Protein Sci. 22:1820-1825 (2013). (Abstract)

Crick, S.L., Ruff, K.M., Garai, K., Frieden, C. and Pappu, R.V.
Unmasking the roles of N- and C-terminal flanking sequences from exon 1 of huntingtin as modulators of polyglutamine aggregation.
PNAS 110:20075-20080 (2013). (Abstract)

Verghese, P.B., Castellano, J.M., Garai, K., Wang, Y., Jiang, H., Shah, A., Bu, G., Frieden, C. and Holtzmann, D.M.
ApoE influences amyloid-β (Aβ) clearance despite minimal apoE/Aβ association in physiological conditions.
PNAS 110:E1807-1816 (2013). (Abstract)

Garai, K. and Frieden, C.
Quantitative analysis of the time course of Aβ oligomerization and subsequent growth steps using tetramethylrhodamine-labeled Aβ.
PNAS 110:3321-3326 (2013). (Abstract)