Author

E. Pretorius

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

Signature Assays, Organisms & Methods

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Research Focus:cell type annotation· 3 Approach:experimental assay· 3 Assay:proteomics· 3 Organism:human· 2 Approach:biophysical modeling· 1 Research Focus:host-pathogen & immune response· 1 Assay:imaging· 1

Frequent Co-Authors

D. B. Kell· 4 shared C. Venter· 1 shared C. W. Theron· 1 shared G. Tarr· 1 shared J. A. Bezuidenhout· 1 shared J. E. Salcedo-Sora· 1 shared J. M. Grixti· 1 shared L. Hendricks· 1 shared

Activity by Year

2017-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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4 shared papersBiochemistry

D. B. Kell

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Proteomic evidence for amyloidogenic cross-seeding in fibrinaloid microclots

D. B. Kell, E. Pretorius

The paper provides proteomic evidence that fibrinaloid microclots involve cross-seeding of non-fibrin proteins into amyloid structures, suggesting a complex mechanism beyond simple entrapment.

bioRxiv · Jul 16, 2024Biochemistry

Automated microscopic measurement of fibrinaloid microclots and their degradation by nattokinase, the main natto protease

J. M. Grixti, C. W. Theron, J. E. Salcedo-Sora, E. Pretorius, D. B. Kell

The paper describes an automated method to measure fibrinaloid microclots and shows nattokinase degrades them in vitro.

bioRxiv · Apr 6, 2024Biochemistry

The Atypical Fibrin Fibre Network in Rheumatoid Arthritis and its Relation to Autoimmunity, Inflammation and Thrombosis

J. A. Bezuidenhout, C. Venter, T. J. Roberts, G. Tarr, D. B. Kell, E. Pretorius

This study compares coagulation, inflammation, and fibrin structure in RA patients and controls, finding denser fibrin networks and citrullination in RA.

bioRxiv · May 28, 2020 · PreprintBiochemistry

Both Lipopolysaccharide And Lipoteichoic Acids Potently Induce Anomalous Fibrin Amyloid Formation: Assessment With Novel Amytracker™ Stains

E. Pretorius, M. J. Page, L. Hendricks, N. B. Nkosi, S. R. Benson, D. B. Kell

The paper shows that LPS and LTAs induce amyloid-like fibrin formation, detected by Amytracker™ stains and viscometry, suggesting a role in inflammatory coagulopathies.

bioRxiv · Sep 4, 2017Biophysics