Author

M. P. Jacobson

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 1 Biophysics· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Research Focus:host-pathogen & immune response· 2 Organism:human· 2 Approach:experimental assay· 1 Approach:mechanistic / dynamical model· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Assay:proteomics· 1 Approach:statistical model· 1

Frequent Co-Authors

B. E. Tourdot· 1 shared B. Tian· 1 shared C. Kalyanaraman· 1 shared D. L. Barber· 1 shared F. Oltrabella· 1 shared H. Liu· 1 shared J. C. Freedman· 1 shared J. M. Bruning· 1 shared

Activity by Year

2018-2020 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 16 mutual co-author links

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1 shared paperBiochemistry

B. E. Tourdot

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Altered specificity of 15-LOX-1 in the biosynthesis of 7S,14S-diHDHA implicates 15-LOX-2 in biosynthesis of resolvin D5

S. C. Perry, C. Kalyanaraman, B. E. Tourdot, W. S. Conrad, O. Akinkugbe, J. C. Freedman, M. Holinstat, M. P. Jacobson, T. R. Holman

This paper identifies that h15-LOX-2 preferentially produces RvD5 from 7S-HDHA with faster kinetics than h15-LOX-1, suggesting a greater role for h15-LOX-2 in biosynthesizing resolvin D5.

bioRxiv · Mar 25, 2020Biochemistry

Conserved tau microtubule-binding repeat histidines confer pH-dependent tau-microtubule association

R. A. Charafeddine, W. A. Cortopassi, P. Lak, M. P. Jacobson, D. L. Barber, T. Wittmann

This study identifies conserved histidine residues in tau that act as pH sensors modulating tau-microtubule binding through electrostatic and hydrophobic interactions.

bioRxiv · Dec 4, 2018Cell Biology

Covalent Modification and Regulation of the Nuclear Receptor Nurr1 by a Dopamine Metabolite

J. M. Bruning, Y. Wang, F. Oltrabella, B. Tian, S. A. Kholodar, H. Liu, P. Bhattacharya, S. Guo, J. M. Holton, R. J. Fletterick, M. P. Jacobson, P. M. England

The paper identifies 5,6-dihydroxyindole (DHI) as a dopamine metabolite that covalently modifies and activates Nurr1, a nuclear receptor critical for dopaminergic neuron function, offering potential therapeutic strategies for Parkinson's disease.

bioRxiv · Nov 7, 2018Biophysics