Author

G. M. Martin

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· 2 Biophysics· 1 Immunology· 1 Pathology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Assay:cryo-EM· 3 Research Focus:protein structure prediction· 3 Organism:human· 2 Research Focus:cell type annotation· 1 Assay:DNA methylation· 1 Research Focus:host-pathogen & immune response· 1 Assay:proteomics· 1

Frequent Co-Authors

C. Yoshioka· 3 shared S.-L. Shyng· 3 shared B. Kandasamy· 2 shared A. B. Ward· 1 shared A. Geary-Teeter· 1 shared B. Greenhouse· 1 shared C. B. Bau· 1 shared E. A. Rex· 1 shared

Activity by Year

2016-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 15 mutual co-author links

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3 shared papersBiochemistry

C. Yoshioka

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

Broadly inhibitory antibodies against severe malaria virulence proteins

R. A. Reyes, S. S. R. Raghavan, N. K. Hurlburt, V. Introini, I. H. Kana, R. W. Jensen, E. Martinez-Scholze, M. Gestal-Mato, C. B. Bau, M. L. Fernandez-Quintero, J. R. Loeffler, J. A. Ferguson, W.-H. Lee, G. M. Martin, T. G. Theander, , T. Lavstsen

The paper identifies two human monoclonal antibodies that broadly inhibit PfEMP1's binding to EPCR, a key process in severe malaria pathogenesis.

bioRxiv · Jan 25, 2024Immunology

A low-cost and easy-to-use cell preservation reagent for 4{ring}C or room temperature sample storage

S. Shankar, S. Roy, A. Geary-Teeter, G. M. Martin, P. D. Ladd

This paper introduces a low-cost cell preservation reagent inspired by natural mechanisms, showing it preserves mammalian cells for at least one week at 4°C or as dried samples.

bioRxiv · Aug 23, 2019 · PreprintPathology

Mechanism of pharmacochaperoning in KATP channels revealed by cryo-EM

G. M. Martin, M. W. Sung, Z. Yang, L. M. Innes, B. Kandasamy, L. David, C. Yoshioka, S.-L. Shyng

This study reveals how pharmacochaperones stabilize KATP channels by binding to SUR1 and supporting Kir6.2 N-terminus insertion, enabling mutant channel assembly.

bioRxiv · Mar 8, 2019 · PreprintBiophysics

Anti-diabetic drug binding site in KATP channels revealed by Cryo-EM

G. M. Martin, B. Kandasamy, F. DiMaio, C. Yoshioka, S.-L. Shyng

The paper presents a cryo-EM structure of KATP channels bound to glibenclamide and ATP, revealing the drug's binding site and its interaction with the channel.

bioRxiv · Aug 5, 2017Biochemistry

Cryo-EM structure of the ATP-sensitive potassium channel illuminates mechanisms of assembly and gating

G. M. Martin, C. Yoshioka, E. A. Rex, J. F. Fay, Q. Xie, M. R. Whorton, J. Z. Chen, S.-L. Shyng

The paper presents a cryo-EM structure of the KATP channel, revealing assembly and gating mechanisms involving SUR1 and Kir6.2 interactions with ATP and PIP2.

bioRxiv · Dec 16, 2016Biochemistry