Author

M. Moritz

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· 3 Biophysics· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:protein structure prediction· 2 Approach:statistical model· 2 Organism:virus· 2 Assay:cryo-EM· 1 Approach:deep learning· 1 Assay:proteomics· 1 Assay:structural biology· 1

Frequent Co-Authors

G. E. Merz· 2 shared H. T. Kratochvil· 2 shared I. D. Young· 2 shared J. K. Peters· 2 shared N. Herrera· 2 shared T. W. Owens· 2 shared U. Schulze-Gahmen· 2 shared A. Aimon· 1 shared

Activity by Year

2020-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 43 mutual co-author links

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2 shared papersBiophysics

G. E. Merz

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

Assay for characterizing adsorption-properties of surfaces (APS) used for sample preparation prior to quantitative omics

B. Siebels, M. Moritz, D. Hübler, A. Gocke, H. L. Voss, H. Schlüter

The paper develops an assay to quantify adsorption effects of surfaces on analytes during sample preparation, using LC-MS/MS-based proteomics to identify and measure peptide adsorption to different vial materials.

bioRxiv · Aug 3, 2023 · PreprintBiochemistry

CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes.

M. Gupta, C. M. Azumaya, M. Moritz, S. Pourmal, A. Diallo, G. E. Merz, G. M. Jang, M. Bouhaddou, A. Fossati, A. F. Brilot, D. Diwanji, E. Hernandez, N. Herrera, H. T. Kratochvil, V. L. Lam, , K. I Pawar

The paper uses cryo-EM and AlphaFold2 to determine the structure of SARS-CoV-2 Nsp2, revealing its zinc-binding site and potential interactions with host proteins.

bioRxiv · May 10, 2021 · PreprintBiophysics

Fragment binding to the Nsp3 macrodomain of SARS-CoV-2 identified through crystallographic screening and computational docking

M. Schuller, G. J. Correy, S. Gahbauer, D. Fearon, T. Wu, R. E. Diaz, I. D. Young, L. Carvalho Martins, D. H. Smith, U. Schulze-Gahmen, T. W. Owens, I. Deshpande, G. E. Merz, A. C. Thwin, J. T. Biel, , Smi

The paper identifies new chemical fragments binding to the SARS-CoV-2 Nsp3 macrodomain through crystallographic screening and computational docking, validating their binding with biophysical techniques.

bioRxiv · Nov 24, 2020Biochemistry

Microtubules form by progressively faster tubulin accretion, not by nucleation-elongation

L. Rice, M. Moritz, D. A. Agard

The paper proposes a new model for microtubule formation that explains their assembly through accretion and straightening penalties, fitting experimental data better than traditional nucleation-elongation models.

bioRxiv · Aug 18, 2020Cell Biology

XMAP215 and γ-tubulin additively promote microtubule nucleation in purified solutions

B. R. King, M. Moritz, H. Kim, D. Agard, C. L. Asbury, T. N. Davis

This study investigates whether XMAP215 and γ-tubulin synergize in microtubule nucleation and finds they act additively, not synergistically, in purified solutions.

bioRxiv · May 21, 2020Biochemistry