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Erin E. Carlson

Researcher at University of Minnesota

Publications -  97
Citations -  5020

Erin E. Carlson is an academic researcher from University of Minnesota. The author has contributed to research in topics: Penicillin binding proteins & Medicine. The author has an hindex of 24, co-authored 84 publications receiving 3660 citations. Previous affiliations of Erin E. Carlson include University of Wisconsin-Madison & University of North Texas Health Science Center.

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Sharing and community curation of mass spectrometry data with Global Natural Products Social Molecular Networking

Mingxun Wang, +135 more
- 01 Aug 2016 - 
TL;DR: In GNPS, crowdsourced curation of freely available community-wide reference MS libraries will underpin improved annotations and data-driven social-networking should facilitate identification of spectra and foster collaborations.
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Natural Products as Chemical Probes

TL;DR: Recent examples of the use of natural products and their derivatives as chemical probes to explore biological phenomena and assemble biochemical pathways are presented here.
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Profiling of β-Lactam Selectivity for Penicillin-Binding Proteins in Escherichia coli Strain DC2

TL;DR: This study evaluated 22 commercially available β-lactams for inhibition of the PBPs in live Escherichia coli strain DC2 and observed diverse PBP selectivities, with amdinocillin (mecillinam) showing selectivity for PBP2.
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Novel heterocyclic trans olefin analogues of N-{4-[4-(2,3-dichlorophenyl)piperazin-1-yl]butyl}arylcarboxamides as selective probes with high affinity for the dopamine D3 receptor.

TL;DR: In this paper, a series of >30 novel analogues were synthesized, and their binding affinities were evaluated in competition binding assays in HEK 293 cells transfected with either D2L, D3, or D4 human dopamine receptors using the high affinity, selective D2-like receptor antagonist 125I-IABN.
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A unique catalytic mechanism for UDP-galactopyranose mutase

TL;DR: Evidence is provided for a mechanism in which the flavin cofactor assumes a new role, and it is anticipated that the clarification of the catalytic mechanism for UGM will facilitate the development of anti-mycobacterial agents.