Lars C. Pedersen
Affiliations: | 1990-1994 | Structural Biology | NIEHS/NIH, Durham, NC, United States |
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"Lars Pedersen"Bio:
https://books.google.com/books?id=QqIvAQAAIAAJ
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Parents
Sign in to add mentorDavid C. Teller | grad student | 1990-1994 | University of Washington | |
(X-ray structure determination of Factor XIII) | ||||
Hazel Marguerite Holden | post-doc | 1994-1995 | UW Madison |
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Publications
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Min J, Keswani T, LaHood NA, et al. (2024) Design of an Ara h 2 hypoallergen from conformational epitopes. Clinical and Experimental Allergy : Journal of the British Society For Allergy and Clinical Immunology |
Kirby TW, Gabel SA, DeRose EF, et al. (2023) Targeting the Structural Maturation Pathway of HIV-1 Reverse Transcriptase. Biomolecules. 13 |
Min J, Foo ACY, Gabel SA, et al. (2023) Structural and ligand binding analysis of the pet allergens Can f 1 and Fel d 7. Frontiers in Allergy. 4: 1133412 |
Foo ACY, Thompson PM, Chen SH, et al. (2021) The mosquito protein AEG12 displays both cytolytic and antiviral properties via a common lipid transfer mechanism. Proceedings of the National Academy of Sciences of the United States of America. 118 |
Duff MR, Gabel SA, Pedersen LC, et al. (2020) The structural basis for NSAID inhibition of human dihydrofolate reductase. Journal of Medicinal Chemistry |
Pedersen LC, Inoue K, Kim S, et al. (2019) A ubiquitin-like domain is required for stabilizing the N-terminal ATPase module of human SMCHD1. Communications Biology. 2: 255 |
Kim K, Min J, Kirby TW, et al. (2019) Ligand binding characteristics of the Ku80 von Willebrand domain. Dna Repair. 85: 102739 |
Kaminski AM, Chiruvella KK, Ramsden DA, et al. (2019) Unexpected behavior of DNA polymerase Mu opposite template 8-oxo-7,8-dihydro-2'-guanosine. Nucleic Acids Research |
Pedersen LC, Inoue K, Kim S, et al. (2019) A ubiquitin-like domain is required for stabilizing the N-terminal ATPase module of human SMCHD1. Communications Biology. 2: 255 |
Kaminski AM, Tumbale PP, Schellenberg MJ, et al. (2018) Structures of DNA-bound human ligase IV catalytic core reveal insights into substrate binding and catalysis. Nature Communications. 9: 2642 |