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Paul Schimmel, Ph.D.

Affiliations: 
The Skaggs Institute Scripps Research Institute, La Jolla, La Jolla, CA, United States 
Area:
Biophysical Chemistry & Translational Medicine
Website:
http://www.scripps.edu/schimmel/
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"Paul Schimmel"
Bio:

http://www.nasonline.org/member-directory/members/50806.html

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Parents

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Gordon G. Hammes grad student 1966 MIT
 (Kinetic and thermodynamic studies of reactions of biological interest)
Paul J. Flory post-doc 1966-1967 Stanford

Children

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Maria Jasin grad student MIT (Cell Biology Tree)
Lynne Joy Regan grad student 1987 MIT
Brian E. Nordin grad student 2002 Scripps Institute
Martha A. Lovato grad student 2003 Scripps Institute
W. Todd Miller post-doc MIT
Litao Sun post-doc 2012-
Jonathan J. Burbaum post-doc 1988-1991 MIT
Karin M. Musier-Forsyth post-doc 1989-1992 MIT
Rebecca W. Alexander post-doc 1996-1999 MIT
Joseph Walter Chihade post-doc 1996-1999 MIT
Lluís Ribas de Pouplana post-doc 1993-2001 Scripps Institute
Min Guo post-doc 2005-2010 The Scripps Research Institute, La Jolla, CA
Valerie A. de Crecy-Lagard research scientist 1999-2004 Scripps Institute (ID Tree)

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Publications

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Kuhle B, Chen Q, Schimmel P. (2023) tRNA renovatio: Rebirth through fragmentation. Molecular Cell
de Potter B, Vallee I, Camacho N, et al. (2023) Domain collapse and active site ablation generate a widespread animal mitochondrial seryl-tRNA synthetase. Nucleic Acids Research
Han L, Luo Z, Ju Y, et al. (2023) The binding mode of orphan glycyl-tRNA synthetase with tRNA supports the synthetase classification and reveals large domain movements. Science Advances. 9: eadf1027
Ju Y, Han L, Chen B, et al. (2021) X-shaped structure of bacterial heterotetrameric tRNA synthetase suggests cryptic prokaryote functions and a rationale for synthetase classifications. Nucleic Acids Research
Sun L, Wei N, Kuhle B, et al. (2021) CMT2N-causing aminoacylation domain mutants enable Nrp1 interaction with AlaRS. Proceedings of the National Academy of Sciences of the United States of America. 118
Kuhle B, Chihade J, Schimmel P. (2020) Relaxed sequence constraints favor mutational freedom in idiosyncratic metazoan mitochondrial tRNAs. Nature Communications. 11: 969
Blocquel D, Sun L, Matuszek Z, et al. (2019) CMT disease severity correlates with mutation-induced open conformation of histidyl-tRNA synthetase, not aminoacylation loss, in patient cells. Proceedings of the National Academy of Sciences of the United States of America
Naganuma M, Sekine SI, Chong YE, et al. (2018) Author Correction: The selective tRNA aminoacylation mechanism based on a single G•U pair. Nature
Xu Z, Lo WS, Beck DB, et al. (2018) Bi-allelic Mutations in Phe-tRNA Synthetase Associated with a Multi-system Pulmonary Disease Support Non-translational Function. American Journal of Human Genetics. 103: 100-114
Chong YE, Guo M, Yang XL, et al. (2018) Distinct ways of G:U recognition by conserved tRNA binding motifs. Proceedings of the National Academy of Sciences of the United States of America
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