Frieden, Carl

ApoE influences amyloid-β (Aβ) clearance despite minimal apoE/Aβ association in physiological conditions

Verghese, P. B., Castellano, J. M., Garai, K., Wang, Y., Jiang, H., Shah, A., Bu, G., Frieden, C., & Holtzman, D. M. (2013) · Proceedings of the National Academy of Sciences

Alzheimer's disease research and treatmentsNeuroinflammation and Neurodegeneration Mechanisms

Cited by 556

Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide

Hu, X., Crick, S. L., Bu, G., Frieden, C., Pappu, R. V., & Lee, J.-M. (2009) · Proceedings of the National Academy of Sciences

Alzheimer's disease research and treatmentsNeuroinflammation and Neurodegeneration Mechanisms

Cited by 426

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) · Biochemistry

Alzheimer's disease research and treatmentsDementia and Cognitive Impairment Research

Cited by 145

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) · Proceedings of the National Academy of Sciences

Protein Structure and DynamicsAlzheimer's disease research and treatments

Cited by 134

Structural differences between apoE3 and apoE4 may be useful in developing therapeutic agents for Alzheimer’s disease

Frieden, C., & Garai, K. (2012) · Proceedings of the National Academy of Sciences

Alzheimer's disease research and treatmentsProtein Structure and Dynamics

Cited by 133

APOE3 -Jacksonville (V236E) variant reduces self-aggregation and risk of dementia

Liu, C.-C., Murray, M. E., Li, X., Zhao, N., Wang, N., Heckman, M. G., Shue, F., Martens, Y., Li, Y., Raulin, A.-C., et al. (2021) · Science Translational Medicine

Alzheimer's disease research and treatmentsDementia and Cognitive Impairment Research

Cited by 108

Hydrogen/deuterium exchange and electron-transfer dissociation mass spectrometry determine the interface and dynamics of apolipoprotein E oligomerization

Huang, R. Y.-C., Garai, K., Frieden, C., & Gross, M. L. (2011) · Biochemistry

Mass Spectrometry Techniques and ApplicationsAlzheimer's disease research and treatments

Cited by 97

Mass spectrometry-based protein footprinting characterizes the structures of oligomeric apolipoprotein E2, E3, and E4

Gau, B., Garai, K., Frieden, C., & Gross, M. L. (2011) · Biochemistry

Mass Spectrometry Techniques and ApplicationsAlzheimer's disease research and treatments

Cited by 74

The Association−Dissociation Behavior of the ApoE Proteins: Kinetic and Equilibrium Studies

Garai, K., & Frieden, C. (2010) · Biochemistry

Alzheimer's disease research and treatmentsProtein Structure and Dynamics

Cited by 67

Dissociation of Apolipoprotein E Oligomers to Monomer Is Required for High-Affinity Binding to Phospholipid Vesicles

Garai, K., Baban, B., & Frieden, C. (2011) · Biochemistry

Alzheimer's disease research and treatmentsLipid Membrane Structure and Behavior

Cited by 57

Apolipoprotein E4 has extensive conformational heterogeneity in lipid-free and lipid-bound forms

Stuchell-Brereton, M. D., Zimmerman, M. I., Miller, J. J., Mallimadugula, U. L., Incicco, J. J., Roy, D., Smith, L. G., Cubuk, J., Baban, B., DeKoster, G. T., et al. (2023) · Proceedings of the National Academy of Sciences

Alzheimer's disease research and treatmentsProtein Structure and Dynamics

Cited by 48

An NADH-induced conformational change that mediates the sequential 3β-hydroxysteroid dehydrogenase/isomerase activities is supported by affinity labeling and the time-dependent activation of isomerase

Thomas, J. L., Frieden, C., Nash, W. E., & Strickler, R. C. (1995) · Journal of Biological Chemistry

Steroid Chemistry and BiochemistryBiochemical and Molecular Research

Cited by 48

Effect of temperature on the mechanism of actin polymerization

Zimmerle, C. T., & Frieden, C. (1986) · Biochemistry

Cellular Mechanics and InteractionsMicrotubule and mitosis dynamics

Cited by 45

Apo E: The role of conserved residues in defining function

Frieden, C. (2015) · Protein Science

Alzheimer's disease research and treatmentsProtein Structure and Dynamics

Cited by 29