Author

M. Lakemeyer

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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Microbiology· 3

Signature Assays, Organisms & Methods

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Approach:biophysical modeling· 3 Organism:bacteria (other)· 2 Research Focus:drug response / drug discovery· 2 Approach:experimental assay· 2 Assay:proteomics· 2 Research Focus:host-pathogen & immune response· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

K. M. Lum· 2 shared M. Bogyo· 2 shared A. j. O'Donoghue· 1 shared A. S. Bhatt· 1 shared B. M. Babin· 1 shared D. J. Gelsinger· 1 shared D. Thomy· 1 shared F. Faucher· 1 shared

Activity by Year

2020-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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2 shared papersMicrobiology

K. M. Lum

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Chemoproteomic identification of a dipeptidyl peptidase 4 (DPP4) homolog in Bacteroides thetaiotaomicron important for envelope integrity and fitness

L. J. Keller, T. H. Nguyen, L. Liu, M. Lakemeyer, D. J. Gelsinger, R. Chanin, N. Ngo, K. M. Lum, F. Faucher, P. Ipock, M. Niphakis, A. S. Bhatt, A. j. O'Donoghue, K. Huang, M. Bogyo

The paper identifies a DPP4 homolog in Bacteroides thetaiotaomicron important for envelope integrity and fitness, showing it is inhibited by diabetes drugs.

bioRxiv · Jul 25, 2022 · PreprintMicrobiology

Antibiotic acyldepsipeptides stimulate the Streptomyces Clp-ATPase/ClpP complex for accelerated proteolysis

L. Reinhardt, D. Thomy, M. Lakemeyer, J. Ortega, S. A. Sieber, P. Sass, H. Broetz-Oesterhelt

This paper identifies the composition of the Streptomyces Clp protease complex and reveals a new mechanism by which ADEP antibiotics accelerate proteolysis by binding to ClpP1 and Clp-ATPases.

bioRxiv · May 13, 2022Microbiology

Toxoplasma gondii serine hydrolases regulate parasite lipid mobilization during growth and replication within the host

O. Onguka, B. M. Babin, M. Lakemeyer, I. T. Foe, N. Amara, S. M. Terrell, K. M. Lum, P. Cieplak, M. J. Niphakis, J. Z. Long, M. Bogyo

This study identifies serine hydrolases in Toxoplasma gondii that hydrolyze lipid esters, showing their role in lipid metabolism and potential as therapeutic targets.

bioRxiv · Nov 24, 2020Microbiology