Author

A. L. Burlingame

University of California, San Francisco

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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Cell Biology· 3 Cancer Biology· 2 Biophysics· 1 Physiology· 1 Plant Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 8 Research Focus:cell signaling & trafficking· 5 Assay:proteomics· 4 Research Focus:development & morphogenesis· 3 Organism:human· 3 Research Focus:cell type annotation· 2 Research Focus:chromatin & epigenetic regulation· 2 Organism:mouse· 2

Frequent Co-Authors

J. A. Oses-Prieto· 2 shared M. J. Trnka· 2 shared A. Blees· 1 shared A. E. Roehrigh· 1 shared A. Frost· 1 shared A. Hergovich· 1 shared A. Pfeiffer· 1 shared A. Urisman· 1 shared

Activity by Year

2018-2025 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 12 mutual co-author links

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2 shared papersCancer Biology

J. A. Oses-Prieto

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Author profile →

8 papers

Recent·Most cited

O-GlcNAc modifications regulate lamin A tail processing

Katherine Augspurger, Elizabeth Martin, Jason C. Maynard, Kevin A. Welle, Sina Ghaemmaghami, A. L. Burlingame, Barbara Panning, Abigail L. Buchwalter

This study investigates how O-GlcNAc modifications influence lamin A tail processing and identifies a potential link between glucose metabolism and lamina biogenesis.

bioRxiv · Mar 11, 2025 · PreprintCell Biology

O-GlcNAc glycosylation orchestrates fate decision and niche function of bone marrow stromal progenitors

Z. Zhang, Z. Huang, M. Awad, M. Elsalanty, J. Cray, L. E. Ball, J. Maynard, A. L. Burlingame, H. Zeng, K. C. Mansky, H.-B. Ruan

This study identifies O-GlcNAc glycosylation as a regulator of bone marrow stromal progenitor fate and niche function, influencing osteogenic/adipogenic differentiation and hematopoiesis.

bioRxiv · Dec 21, 2022Physiology

Deconvoluting signals downstream of growth and immune receptor kinases by phosphocodes of the BSU1 family phosphatases

C. H. Park, Y. Bi, J.-H. Youn, S.-H. Kim, J.-G. Kim, N. Xu, R. Shrestha, A. L. Burlingame, S.-L. Xu, M. B. Mudgett, S.-K. Kim, T.-W. Kim, Z.-Y. Wang

This study shows that BSU1 phosphatase uses different phosphorylation sites to transduce signals from brassinosteroid and flagellin receptors in plants.

bioRxiv · May 2, 2022Plant Biology

Role for Merlin/NF2 in transcription elongation through interaction with the PAF complex

A. E. Roehrigh, K. Klupsch, J. A. Oses-Prieto, S. Chaib, S. Henderson, W. Emmett, L. C. Young, S. Surinova, A. Blees, A. Pfeiffer, M. Tijani, F. Brunk, N. Hartig, M. Munoz-Alegre, A. Hergovich, , P. Rodriguez-Viciana

This study shows Merlin interacts with the PAF complex to regulate transcription elongation, linking cell-cell adhesion to tumor suppression.

bioRxiv · Jul 28, 2019 · PreprintCancer Biology

Targeted phosphoproteomics of the Ras signaling network reveal regulatory mechanisms mediated by oncogenic KRAS

A. Urisman, T. L. Yuan, M. Trinidad, J. H. Morris, S. Afghani, J. A. Oses-Prieto, C. D. Ritchie, M. S. Zahari, C. H. Benes, A. L. Burlingame, F. McCormick

This study uses targeted phosphoproteomics to analyze KRAS signaling network regulation in lung cancer cells, identifying unique phosphorylation changes and their roles in transcriptional silencing.

bioRxiv · Jul 9, 2019 · PreprintCancer Biology

A NOVEL MECHANISM FOR NF-κB-ACTIVATION VIA IκB-AGGREGATION: IMPLICATIONS FOR HEPATIC MALLORY-DENK-BODY INDUCED INFLAMMATION

Y. Liu, M. J. Trnka, S. Guan, D. Kwon, D.-H. Kim, J.-J. Chen, P. A. Greer, A. L. Burlingame, M. A. Correia

This study identifies a novel mechanism of NF-κB activation through IκB sequestration into insoluble aggregates along with aggregation-prone proteins in MDB-inducing models.

bioRxiv · Mar 21, 2019Cell Biology

A role for liquid-liquid phase separation in ESCRT-mediated nuclear envelope reformation.

A. von Appen, D. Lajoie, I. E. Johnson, M. Trnka, S. M. Pick, A. L. Burlingame, K. S. Ullman, A. Frost

This study shows how LEM2 uses liquid-liquid phase separation and ESCRT pathways to facilitate nuclear envelope reformation during mitotic exit.

bioRxiv · Mar 14, 2019Cell Biology

Disorganization of the histone core promotes organization of heterochromatin into phase-separated droplets

S. Sanulli, M. J. Trnka, V. Dharmarajan, R. W. Tibble, B. D. Pascal, A. L. Burlingame, P. R. Griffin, J. D. Gross, G. J. Narlikar

This study shows that the S. pombe HP1 protein Swi6 promotes chromatin compaction through phase-separated droplets by disorganizing the histone core and increasing histone residue accessibility.

bioRxiv · Nov 18, 2018 · PreprintBiophysics