John M. Pascal, Ph.D.

Affiliations: 
2000 University of Texas at Austin, Austin, Texas, U.S.A. 
Area:
Biochemistry: Structural Biology, Protein Engineering, And Drug Design
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"John Pascal"
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Jon D. Robertus grad student 2000 UT Austin
 (Crystal structures of ebulin, a non-toxic ribosome -inactivating protein.)
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Publications

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Rouleau-Turcotte É, Krastev DB, Pettitt SJ, et al. (2022) Captured snapshots of PARP1 in the active state reveal the mechanics of PARP1 allostery. Molecular Cell
Sverzhinsky A, Tomkinson AE, Pascal JM. (2021) Cryo-EM structures and biochemical insights into heterotrimeric PCNA regulation of DNA ligase. Structure (London, England : 1993)
Maluchenko NV, Nilov DK, Pushkarev SV, et al. (2021) Mechanisms of Nucleosome Reorganization by PARP1. International Journal of Molecular Sciences. 22
Langelier MF, Billur R, Sverzhinsky A, et al. (2021) HPF1 dynamically controls the PARP1/2 balance between initiating and elongating ADP-ribose modifications. Nature Communications. 12: 6675
Sun Y, Chen J, Huang SN, et al. (2021) PARylation prevents the proteasomal degradation of topoisomerase I DNA-protein crosslinks and induces their deubiquitylation. Nature Communications. 12: 5010
Rashid I, Hammel M, Sverzhinsky A, et al. (2021) Direct interaction of DNA repair protein tyrosyl DNA phosphodiesterase 1 and the DNA ligase III catalytic domain is regulated by phosphorylation of its flexible N-terminus. The Journal of Biological Chemistry. 100921
Ogden TEH, Yang JC, Schimpl M, et al. (2021) Dynamics of the HD regulatory subdomain of PARP-1; substrate access and allostery in PARP activation and inhibition. Nucleic Acids Research
Hammel M, Rashid I, Sverzhinsky A, et al. (2020) An atypical BRCT-BRCT interaction with the XRCC1 scaffold protein compacts human DNA Ligase IIIα within a flexible DNA repair complex. Nucleic Acids Research
Rouleau-Turcotte É, Pascal JM. (2020) Bridging a DNA Break to Leave a Poly(ADP-Ribose) Mark on Chromatin. Molecular Cell. 80: 560-561
Matsumoto Y, Brooks RC, Sverzhinsky A, et al. (2020) Dynamic DNA-bound PCNA complexes co-ordinate Okazaki fragment synthesis, processing and ligation. Journal of Molecular Biology
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