Author

T. Anzai

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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Biophysics· 2 Cancer Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:cell type annotation· 2 Organism:human· 2 Assay:bulk RNA-seq· 1 Research Focus:cancer & tumor microenvironment· 1 Assay:protein structure· 1 Assay:proteomics· 1 Organism:rat· 1

Frequent Co-Authors

Y. Matsumura· 3 shared M. Yasunaga· 2 shared S. Saijou· 2 shared H. Kurosawa· 1 shared H. Takashima· 1 shared M. Hara· 1 shared S. Hanaoka· 1 shared Y. Ohnuki· 1 shared

Activity by Year

2019-2021 · peak 1/yr

Co-Author Collaboration Network

8 top collaborators · 22 mutual co-author links

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3 shared papersBiophysics

Y. Matsumura

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Identification of CD73 as the antigen of an antigen-unknown monoclonal antibody established by exosome immunization, and its antibody-drug conjugate exerts an antitumor effect on glioblastoma cell lines

T. Anzai, S. Saijou, H. Takashima, M. Hara, S. Hanaoka, Y. Matsumura, M. Yasunaga

This paper identifies CD73 as the antigen of a monoclonal antibody generated by exosome immunization and shows its antibody-drug conjugate has antitumor effects on glioblastoma cell lines.

bioRxiv · Sep 30, 2021 · PreprintBiophysics

TMEM180 contributes to colorectal cancer proliferation through intracellular metabolic pathways

T. Anzai, S. Saijou, Y. Ohnuki, H. Kurosawa, M. Yasunaga, Y. Matsumura

This study shows TMEM180 promotes colorectal cancer growth by enhancing glucose and glutamine metabolism, despite not affecting oxygen consumption or phosphorylation.

bioRxiv · Jul 16, 2020Cancer Biology

Topological analysis of TMEM180, a newly identified membrane protein that is highly expressed in colorectal cancer cells

T. Anzai, Y. Matsumura

This paper identifies TMEM180 as a 12-transmembrane protein with extracellular N- and C-termini and a conserved cation-binding site, suggesting it functions as a cation symporter in colorectal cancer.

bioRxiv · Oct 2, 2019Biophysics