Author

M. Schoof

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 Cell Biology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:cell signaling & trafficking· 2 Organism:bacteria (other)· 1 Research Focus:drug response / drug discovery· 1 Assay:protein structure· 1 Assay:proteomics· 1

Frequent Co-Authors

M. Boone· 3 shared A. Frost· 2 shared L. Wang· 2 shared P. Walter· 2 shared A. A. Anand· 1 shared A. F. Brilot· 1 shared A. M. Smith· 1 shared A. N. Rizo· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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3 shared papersBiochemistry

M. Boone

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Lysis cassette-mediated exoprotein release in Yersinia entomophaga is controlled by a PhoB-like regulator

M. Schoof, M. O'Callghan, C. A. Hefer, T. Glare, A. R. Paulson, M. R. H. Hurst

This study identifies the role of the RoeA regulator and an ALC lysis cassette in exoprotein release in Yersinia entomophaga, showing their transcriptional activation and hierarchical regulation of toxin complex secretion.

bioRxiv · Feb 8, 2023Microbiology

Viral Evasion of the Integrated Stress Response Through Antagonistic eIF2-P Mimicry

M. Schoof, L. Wang, J. Z. Cogan, R. Lawrence, M. Boone, J. D. Wuerth, A. Frost, P. Walter

This study shows that SFSV NSs protein evades the ISR by competing with eIF2-P for binding to eIF2B, preserving its activity and allowing viral protein synthesis.

bioRxiv · Jun 7, 2021Biochemistry

eIF2B Conformation and Assembly State Regulate the Integrated Stress Response

M. Schoof, M. Boone, L. Wang, R. E. Lawrence, A. Frost, P. Walter

This study shows that eIF2B assembly and conformation regulate the ISR, with ISRIB affecting eIF2B through decamer stabilization and allosteric modulation.

bioRxiv · Dec 28, 2020Cell Biology

An ultra-potent synthetic nanobody neutralizes SARS-CoV-2 by locking Spike into an inactive conformation

M. Schoof, B. Faust, R. A. Saunders, S. Sangwan, V. V. Rezelj, N. Hoppe, M. Boone, C. Billesboelle, C. Puchades, C. M. Azumaya, H. T. Kratochvil, M. Zimanyi, I. Deshpande, J. Liang, S. Dickinson, , Barile-H

This paper develops a potent synthetic nanobody that neutralizes SARS-CoV-2 by locking its Spike protein in an inactive conformation, enabling aerosol delivery as a prophylactic or therapeutic agent.

bioRxiv · Aug 8, 2020Biochemistry