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Fabrice Agou

Researcher at Pasteur Institute

Publications -  40
Citations -  2644

Fabrice Agou is an academic researcher from Pasteur Institute. The author has contributed to research in topics: Ubiquitin binding & IκB kinase. The author has an hindex of 18, co-authored 35 publications receiving 2439 citations.

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Complementation Cloning of NEMO, a Component of the IκB Kinase Complex Essential for NF-κB Activation

TL;DR: A flat cellular variant of HTLV-1 Tax-transformed rat fibroblasts, 5R, which is unresponsive to all tested NF-κB activating stimuli is characterized, and its genetic complementation is reported.
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NEMO specifically recognizes K63-linked poly-ubiquitin chains through a new bipartite ubiquitin-binding domain

TL;DR: It is demonstrated that together they form a bipartite high‐affinity K63‐specific ubiquitin‐binding domain, which suggests that the main function of the C‐terminal half of NEMO is to specifically bind K 63‐linked poly‐ubiquitin chains.
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NEMO trimerizes through its coiled-coil C-terminal domain.

TL;DR: In vivo cross-linking experiments indicate that native N EMO in association with IKK is in equilibrium between a dimeric and a trimeric form, suggesting that the association of NEMO with Ikk or with Hsp70 prevents incorrect interdomain pairing reactions that could lead to aggregation or to an non-native oligomeric state of rNEMO.
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The Zinc Finger of NEMO Is a Functional Ubiquitin-binding Domain

TL;DR: Functional complementation assays and in vivo pull-down experiments further show that ZF residues involved in ubiquitin binding are functionally important and required for NF-κB signaling in response to tumor necrosis factor-α.