Author

D. M. Holtzman

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· 1 Biophysics· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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

Frequent Co-Authors

B. Baban· 1 shared C. B. Lessard· 1 shared C. E. Kluender· 1 shared C. Frieden· 1 shared C. R. Hodge· 1 shared D. F. Steinberg· 1 shared D. L. Kober· 1 shared E. D. Roberson· 1 shared

Activity by Year

2018-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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Curved chords = mutual co-authorship

1 shared paperBiophysics

B. Baban

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Author profile →

3 papers

Recent·Most cited

Apolipoprotein E O-glycosylation is associated with amyloid plaques and APOE genotype.

P. E. Lawler, J. G. Bollinger, S. E. Schindler, C. R. Hodge, N. J. Iglesias, V. Krishnan, J. B. Coulton, Y. Li, D. M. Holtzman, R. J. Bateman

The paper quantifies apoE glycosylation in plasma and CSF, finding associations with APOE genotype, total apoE levels, and amyloid status in older individuals.

bioRxiv · Jan 3, 2023 · PreprintBiochemistry

Functional insights from biophysical study of TREM2 interactions with ApoE and Aβ1-42

D. L. Kober, M. D. Stuchell-Brereton, C. E. Kluender, H. B. Dean, M. R. Strickland, D. F. Steinberg, S. S. Nelson, B. Baban, D. M. Holtzman, C. Frieden, J. M. Alexander-Brett, E. D. Roberson, Y. Song, T. J. Brett

This study investigates TREM2 interactions with ApoE and Aβ1-42 using biophysical methods, revealing distinct binding surfaces and a potential role for sTREM2 in inhibiting Aβ polymerization.

Alzheimer's & Dementia · Oct 8, 2020Peer-reviewedBiophysics

High affinity interactions and signal transduction between Aβ oligomers and TREM2

C. B. Lessard, S. L. Malnik, Y. Zhou, T. B. Ladd, P. E. Cruz, Y. Ran, P. Chakrabaty, T. E. Mahan, D. M. Holtzman, J. D. Ulrich, M. Colonna, T. Golde

This study investigates the high-affinity interaction between TREM2 and Aβ oligomers, showing that AD-associated TREM2 variants have reduced signaling and internalization capacity.

bioRxiv · Feb 22, 2018Cell Biology