Author

J. A. Melby

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· 4

Signature Assays, Organisms & Methods

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Assay:proteomics· 4 Approach:deep learning· 3 Organism:human· 3 Research Focus:protein folding & dynamics· 3 Research Focus:cell type annotation· 2 Approach:experimental assay· 2 Approach:statistical model· 2 Organism:virus· 1

Frequent Co-Authors

D. S. Roberts· 4 shared Y. Ge· 4 shared E. J. Larson· 3 shared E. A. Chapman· 2 shared K. A. Brown· 2 shared S. Jin· 2 shared Y. Zhu· 2 shared A. J. Alpert· 1 shared

Activity by Year

2021-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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4 shared papersBiochemistry

D. S. Roberts

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Author profile →

4 papers

Recent·Most cited

Structure and dynamics of endogenous protein complexes in human heart tissue captured by native nanoproteomics

E. A. Chapman, D. S. Roberts, T. N. Tiambeng, J. Andrews, M.-D. Wang, E. A. Reasoner, J. A. Melby, B. H. Li, D. Kim, A. J. Alpert, S. Jin, Y. Ge

This study develops a native nanoproteomics method to characterize the structure and dynamics of endogenous cardiac troponin complexes in human heart tissue using native top-down mass spectrometry.

bioRxiv · Jun 13, 2023 · PreprintBiochemistry

Comprehensive Characterization of Endogenous Phospholamban Proteoforms Enabled by Photocleavable Surfactant and Top-down Proteomics

H. T. Rogers, D. S. Roberts, E. J. Larson, J. A. Melby, K. J. Rossler, A. V. Carr, K. A. Brown, Y. Ge

This paper develops a top-down proteomics method to characterize endogenous phospholamban proteoforms in cardiac tissue, revealing site-specific PTMs.

bioRxiv · Apr 12, 2023Biochemistry

High Sensitivity Top-down Proteomics Captures Single Muscle Cell Heterogeneity in Large Proteoforms

J. A. Melby, K. A. Brown, Z. R. Gregorich, D. S. Roberts, E. A. Chapman, L. E. Ehlers, Z. Gao, E. J. Larson, Y. Jin, J. Lopez, J. Hartung, Y. Zhu, D. Wang, W. Guo, G. M. Diffee, Y. Ge

This study develops a sensitive top-down proteomics method to analyze large proteoforms in single muscle cells, revealing heterogeneity and linking it to muscle fiber types.

bioRxiv · Dec 29, 2022 · PreprintBiochemistry

Structural O-Glycoform Heterogeneity of the SARS-CoV-2 Spike Protein Receptor-Binding Domain Revealed by Native Top-Down Mass Spectrometry

D. S. Roberts, M. W. Mann, J. A. Melby, E. J. Larson, Y. Zhu, A. R. Brasier, S. Jin, Y. Ge

This study uses native top-down mass spectrometry to characterize O-glycoforms of the SARS-CoV-2 S-RBD, identifying seven glycoforms and their relative abundance.

bioRxiv · Feb 28, 2021Biochemistry