Southworth, Daniel R.

Structural Analysis of E. coli hsp90 Reveals Dramatic Nucleotide-Dependent Conformational Rearrangements

Shiau, A. K., Harris, S. F., Southworth, D. R., & Agard, D. A. (2006) · Cell

Heat shock proteins researchProtein Structure and Dynamics

Cited by 455

Glucocorticoid Receptor Function Regulated by Coordinated Action of the Hsp90 and Hsp70 Chaperone Cycles

Kirschke, E., Goswami, D., Southworth, D., Griffin, P. R., & Agard, D. A. (2014) · Cell

Heat shock proteins researchProtein Structure and Dynamics

Cited by 399

Compromised function of the ESCRT pathway promotes endolysosomal escape of tau seeds and propagation of tau aggregation

Chen, J. J., Nathaniel, D. L., Raghavan, P., Nelson, M., Tian, R., Tse, E., Hong, J. Y., See, S. K., Mok, S.-A., Hein, M. Y., et al. (2019) · Journal of Biological Chemistry

Alzheimer's disease research and treatmentsCellular transport and secretion

Cited by 170

Client-loading conformation of the Hsp90 molecular chaperone revealed in the cryo-EM structure of the human Hsp90:Hop complex

Southworth, D. R., & Agard, D. A. (2011) · Molecular Cell

Heat shock proteins researchProtein Structure and Dynamics

Cited by 143

Specific Binding of Tetratricopeptide Repeat Proteins to Heat Shock Protein 70 (Hsp70) and Heat Shock Protein 90 (Hsp90) Is Regulated by Affinity and Phosphorylation

Assimon, V. A., Southworth, D. R., & Gestwicki, J. E. (2015) · Biochemistry

Heat shock proteins researchUbiquitin and proteasome pathways

Cited by 112

KRAS Protein Stability Is Regulated through SMURF2: UBCH5 Complex-Mediated β-TrCP1 Degradation

Shukla, S., Allam, U. S., Ahsan, A., Chen, G., Krishnamurthy, P. M., Marsh, K., Rumschlag, M., Shankar, S., Whitehead, C., Schipper, M., et al. (2014) · Neoplasia

Ubiquitin and proteasome pathwaysProtein Kinase Regulation and GTPase Signaling

Cited by 96

CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes

Gupta, M., Azumaya, C. M., Moritz, M., Pourmal, S., Diallo, A., Merz, G. E., Jang, G., Bouhaddou, M., Fossati, A., Brilot, A. F., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory)

SARS-CoV-2 and COVID-19 ResearchAdvanced Electron Microscopy Techniques and Applications

Cited by 89

The structure of an Hsp90-immunophilin complex reveals cochaperone recognition of the client maturation state

Lee, K., Thwin, A. C., Nadel, C. M., Tse, E., Gates, S. N., Gestwicki, J. E., & Southworth, D. R. (2021) · Molecular Cell

Heat shock proteins researchProtein Structure and Dynamics

Cited by 76

The molecular chaperone Hsp70 activates protein phosphatase 5 (PP5) by binding the tetratricopeptide repeat (TPR) domain

Connarn, J. N., Assimon, V. A., Reed, R. A., Tse, E., Southworth, D. R., Zuiderweg, E. R. P., Gestwicki, J. E., & Sun, D. (2014) · Journal of Biological Chemistry

Heat shock proteins researchProtein Tyrosine Phosphatases

Cited by 48

Unique structural features govern the activity of a human mitochondrial AAA+ disaggregase, Skd3

Cupo, R. R., Rizo, A. N., Braun, G. A., Tse, E., Chuang, E., Gupta, K., Southworth, D. R., & Shorter, J. (2022) · Cell Reports

Heat shock proteins researchMitochondrial Function and Pathology

Cited by 25

Unique structural features govern the activity of a human mitochondrial AAA+ disaggregase, Skd3

Cupo, R. R., Rizo, A. N., Braun, G. A., Tse, E., Chuang, E., Southworth, D. R., & Shorter, J. (2022) · Cell Reports

Heat shock proteins researchMitochondrial Function and Pathology

Cited by 25