Author

J. L. Follmar

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

Signature Assays, Organisms & Methods

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Research Focus:cell signaling & trafficking· 2 Approach:experimental assay· 2 Assay:proteomics· 2 Research Focus:cell type annotation· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

B. E. Thacker· 2 shared C. A. Glass· 2 shared K. Godula· 2 shared R. N. Porell· 2 shared B. M. Timm· 1 shared B. Timm· 1 shared D. Kozirovskiy· 1 shared K. Glass· 1 shared

Activity by Year

2022-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 37 mutual co-author links

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2 shared papersBiochemistry

B. E. Thacker

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2 papers

Recent·Most cited

Human extracellular sulfatases use a dual mechanism for regulation of growth factor interactions with heparan sulfate proteoglycans

B. M. Timm, J. L. Follmar, R. N. Porell, K. Glass, B. E. Thacker, C. A. Glass, K. Godula

This study identifies a dual mechanism by which sulfatases modulate growth factor interactions with heparan sulfate proteoglycans using chemically defined substrates.

bioRxiv · Nov 22, 2023 · PreprintBiochemistry

Biologically-derived neoproteoglycans for profiling protein-glycosaminoglycan interactions

R. N. Porell, J. L. Follmar, S. C. Purcell, B. Timm, L. K. Laubach, D. Kozirovskiy, B. E. Thacker, C. A. Glass, P. L. S. M. Gordts, K. Godula

This paper introduces neoproteoglycans (neoPGs) as biologically-derived probes to study protein-glycosaminoglycan interactions, enabling real-time monitoring and analysis of ligand binding and enzyme specificity.

bioRxiv · Mar 4, 2022Biochemistry