Daniel R. Southworth, Ph.D.

Affiliations: 
2004 Johns Hopkins University, Baltimore, MD 
Area:
translation of the genetic code
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"Daniel Southworth"

Parents

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Rachel Green grad student 2004 Johns Hopkins
 (The ribosomal components involved in translocation of the tRNA:mRNA complex.)

Children

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Kanghyun Lee post-doc 2018- UCSF (Chemistry Tree)
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Publications

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Felker D, Lee K, Pospiech TH, et al. (2023) Mapping interactions of calmodulin and neuronal NO synthase by crosslinking and mass spectrometry. The Journal of Biological Chemistry. 105464
Nadel CM, Thwin AC, Callahan M, et al. (2023) The E3 Ubiquitin Ligase, CHIP/STUB1, Inhibits Aggregation of Phosphorylated Proteoforms of Microtubule-associated Protein Tau (MAPT). Journal of Molecular Biology. 168026
Braxton JR, Shao H, Tse E, et al. (2023) Asymmetric apical domain states of mitochondrial Hsp60 coordinate substrate engagement and chaperonin assembly. Biorxiv : the Preprint Server For Biology
Cupo RR, Rizo AN, Braun GA, et al. (2022) Unique structural features govern the activity of a human mitochondrial AAA+ disaggregase, Skd3. Cell Reports. 40: 111408
Seraphim TV, Nano N, Cheung YWS, et al. (2021) Assembly principles of the human R2TP chaperone complex reveal the presence of R2T and R2P complexes. Structure (London, England : 1993)
Lee K, Thwin AC, Nadel CM, et al. (2021) The structure of an Hsp90-immunophilin complex reveals cochaperone recognition of the client maturation state. Molecular Cell
Verba K, Gupta M, Azumaya C, et al. (2021) CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes. Research Square
Gupta M, Azumaya CM, Moritz M, et al. (2021) CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes. Biorxiv : the Preprint Server For Biology
Lopez KE, Rizo AN, Tse E, et al. (2020) Conformational plasticity of the ClpAP AAA+ protease couples protein unfolding and proteolysis. Nature Structural & Molecular Biology
Chen JJ, Nathaniel DL, Raghavan P, et al. (2019) Compromised function of the ESCRT pathway promotes endolysosomal escape of tau seeds and propagation of tau aggregation. The Journal of Biological Chemistry
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