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Cited by 292

The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.

Covalently Engineered Nanobody Chimeras for Targeted Membrane Protein Degradation

Open access
Zhang, Heng, Han, Yu, Yang, Yuanfan, Lin, Feng, Li, Kexin, Kong, Linghao, Liu, Hongxiang, Dang, Yongjun, Lin, Jian, Chen, Peng R.·2021·Journal of the American Chemical Society

Abstract

The targeted degradation of membrane proteins would afford an attractive and general strategy for treating various diseases that remain difficult with the current proteolysis-targeting chimera (PROTAC) methodology. We herein report a covalent nanobody-based PROTAC strategy, termed GlueTAC, for targeted membrane protein degradation with high specificity and efficiency. We first established a mass-spectrometry-based screening platform for the rapid development of a covalent nanobody (GlueBody) that allowed proximity-enabled cross-linking with surface antigens on cancer cells. By conjugation with a cell-penetrating peptide and a lysosomal-sorting sequence, the resulting GlueTAC chimera triggered the internalization and degradation of programmed death-ligand 1 (PD-L1), which provides a new avenue to target and degrade cell-surface proteins.

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Metadata

Authors
Zhang, H., Han, Y., Yang, Y., Lin, F., Li, K., Kong, L., Liu, H., Dang, Y., Lin, J., & Chen, P. R.
Venue
Journal of the American Chemical Society
Published
2021-10-01
Volume
143
Issue
40
Pages
16377-16382
ISSN
  • 0002-7863 (ISSN-L)
  • 1520-5126
OpenAlex
W3172027657
Cited by
292
References
32
FWCI
8.86
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Covalently Engineered Nanobody Chimeras for Targeted Membrane Protein Degradation. https://app.cochat.ai/papers/10.1021/jacs.1c08521
The paper
Zhang, H., Han, Y., Yang, Y., Lin, F., Li, K., Kong, L., Liu, H., Dang, Y., Lin, J., & Chen, P. R. (2021). Covalently Engineered Nanobody Chimeras for Targeted Membrane Protein Degradation. Journal of the American Chemical Society. https://doi.org/10.1021/jacs.1c08521

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