Hecht, Michael H.

Rationally designed mutations convert de novo amyloid-like fibrils into monomeric β-sheet proteins

Wang, W., & Hecht, M. H. (2002) · Proceedings of the National Academy of Sciences

Alzheimer's disease research and treatmentsProtein Structure and Dynamics

Cited by 159

Mutations in lambda repressor's amino-terminal domain: implications for protein stability and DNA binding.

Hecht, M. H., Nelson, H. C., & Sauer, R. T. (1983) · Proceedings of the National Academy of Sciences

Bacterial Genetics and BiotechnologyProtein Structure and Dynamics

Cited by 137

Mutations Defining the Operator-binding Sites of Bacteriophage Repressor

Nelson, H. C. M., Hecht, M. H., & Sauer, R. T. (1983) · Cold Spring Harbor Symposia on Quantitative Biology

Bacterial Genetics and BiotechnologyProtein Structure and Dynamics

Cited by 49

Selection of a promiscuous minimalist cAMP phosphodiesterase from a library of de novo designed proteins

Schnettler, J. D., Wang, M. S., Gantz, M., Bunzel, H. A., Karas, C., Hollfelder, F., & Hecht, M. H. (2024) · Nature Chemistry

Enzyme Catalysis and ImmobilizationProtein Structure and Dynamics

Cited by 18

Selection of a Promiscuous Minimalist cAMP Phosphodiesterase from a Library of De Novo Designed Proteins

Schnettler, J. D., Wang, M. S., Gantz, M., Karas, C., Hollfelder, F., & Hecht, M. H. (2023) · Nature Chemistry

Enzyme Catalysis and ImmobilizationProtein Structure and Dynamics

Cited by 18