Cited by 130

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Oligomerization and Regulated Proteolytic Processing of Angiopoietin-like Protein 4

Ge, Hongfei, Yang, Guoqing, Huang, Lu, Motola, Daniel L., Pourbahrami, Tiffany, Li, Cai·2004·Journal of Biological Chemistry

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Crossref · 10.1074/jbc.m307583200

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  • The N-terminal coiled-coil domain of ANGPTL4 mediates the formation of oligomers, mostly dimers and tetramers.

    “The N-terminal coiled-coil domain of ANGPTL4 mediates the formation of oligomers, mostly dimers and tetramers (22, 89, 96).”
  • When cleaved, the C-terminal domain dissociates to monomers, but the N-terminal region can remain oligomerized.

    “When cleaved, the C-terminal domain dissociates to monomers, but the N-terminal region can remain oligomerized (89, 96).”
  • ANGPTL4 can be cleaved by furin-like proteases, separating the N-terminal coiled-coil domain from the C-terminal fibrinogen-like domain.

    “ANGPTL4 can be cleaved by furin-like proteases, separating the N-terminal coiled-coil domain from the C-terminal fibrinogen-like domain (96).”

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Research works printed but not linked: 23

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Metadata

Authors
Ge, H., Yang, G., Huang, L., Motola, D. L., Pourbahrami, T., & Li, C.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2004-01
Volume
279
Issue
3
Pages
2038-2045
ISSN
0021-9258
Cited by
130
References
1
Language
en

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