Solution structure of the cysteine-rich domain in Fn14, a member of the tumor necrosis factor receptor superfamily (Q27653928)

Takanori Kigawa

7

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Shigeyuki Yokoyama

Shigeyuki Yokoyama

10

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Yutaka Muto

9

Yutaka Muto

0 references

Naohiro Kobayashi

5

Naohiro Kobayashi

0 references

Weirong Dang

2

Weirong Dang

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author name string

Fahu He

1

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Kohei Saito

3

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Satoru Watanabe

4

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Akiko Tanaka

TWEAK binding to the Fn14 cysteine-rich domain depends on charged residues located in both the A1 and D2 modules

8

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publication date

March 2009

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published in

Protein Science

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volume

18

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issue

3

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page(s)

650-6

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cites work

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Structures of the extracellular domain of the type I tumor necrosis factor receptor

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Protein backbone angle restraints from searching a database for chemical shift and sequence homology

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TWEAK, a member of the TNF superfamily, is a multifunctional cytokine that binds the TweakR/Fn14 receptor

20 March 2017

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The TNF and TNF receptor superfamilies: integrating mammalian biology

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The mitogen-inducible Fn14 gene encodes a type I transmembrane protein that modulates fibroblast adhesion and migration

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Structures of APRIL-receptor complexes: like BCMA, TACI employs only a single cysteine-rich domain for high affinity ligand binding

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TWEAK, a new secreted ligand in the tumor necrosis factor family that weakly induces apoptosis

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