Author

C. Lancaster

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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Approach:experimental assay· 3 Research Focus:cell signaling & trafficking· 2 Organism:human· 2 Research Focus:cancer & tumor microenvironment· 1 Research Focus:cell type annotation· 1 Research Focus:development & morphogenesis· 1 Research Focus:drug response / drug discovery· 1 Assay:imaging· 1

Frequent Co-Authors

A. B. Nixon· 1 shared A. D. MacKerell· 1 shared A. des Georges· 1 shared A. Fountain· 1 shared A. Grishaev· 1 shared A. Krsitopeit· 1 shared A. Kumari· 1 shared A. S. Choi· 1 shared

Activity by Year

2019-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 14 mutual co-author links

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Curved chords = mutual co-authorship

1 shared paperBiochemistry

A. B. Nixon

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Heparan sulfate modifications of betaglycan promote TIMP3-dependent ectodomain shedding to fine-tune TGF-β signaling.

A. S. Choi, L. M. Jenkins-Lane, W. Barton, A. Kumari, C. Lancaster, C. Raulerson, H. Ji, D. Altomare, M. D. Starr, R. Whitaker, R. Phaeton, R. C. Arend, M. Shtutman, A. B. Nixon, N. Hempel, , K. Mythreye

This study identifies heparan sulfate modifications as critical for betaglycan ectodomain shedding, which regulates TGF-β signaling and has clinical implications in ovarian cancer.

bioRxiv · Aug 29, 2023 · PreprintBiochemistry

Phagosome resolution regenerates lysosomes and maintains the degradative capacity in phagocytes

C. Lancaster, A. Fountain, R. Dayam, E. Somerville, J. Sheth, V. Jacobelli, A. Somerville, M. Terebiznik, R. J. Botelho

This study shows that phagosome resolution through clathrin-dependent fragmentation regenerates lysosomes and maintains macrophage degradative capacity after multiple rounds of phagocytosis.

bioRxiv · May 14, 2020Cell Biology

Structure of the cell-binding component of the Clostridium difficile binary toxin reveals a novel macromolecular assembly

X. Xu, R. Ruiz, K. A. Adipietro, C. Peralta, D. Ben-Hail, K. M. Varney, M. E. Cook, B. M. Roth, P. T. Wilder, T. Cleveland, A. Grishaev, H. Neu, S. Michel, W. Yu, D. Beckett, , D. J. Weber

This paper determines the atomic structures of the C. difficile binary toxin CDTb using cryoEM and X-ray crystallography, revealing novel di-heptamer forms and critical domains for toxicity and stability.

bioRxiv · Nov 10, 2019 · PreprintBiophysics