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Fas-Associated Death Domain Protein

Known as: Mediator of Receptor-Induced Toxicity, Fas Associating Protein with Death Domain, FADD Protein, Fas Associating 
A signal-transducing adaptor protein that associates with TNF RECEPTOR complexes. It contains a death effector domain that can interact with death… Expand
National Institutes of Health

Papers overview

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Review
2018
Review
2018
Metallothioneins (MTs) are small cysteine-rich proteins that play important roles in metal homeostasis and protection against… Expand
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Highly Cited
2004
Highly Cited
2004
Specific adaptors regulate the activation of initiator caspases; for example, FADD and Apaf-1 engage caspases 8 and 9… Expand
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Highly Cited
2003
Highly Cited
2003
Apoptosis induced by TNF-receptor I (TNFR1) is thought to proceed via recruitment of the adaptor FADD and caspase-8 to the… Expand
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Highly Cited
2000
Highly Cited
2000
Cell death is achieved by two fundamentally different mechanisms: apoptosis and necrosis. Apoptosis is dependent on caspase… Expand
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Highly Cited
1999
Highly Cited
1999
Although the molecular mechanisms of TNF signaling have been largely elucidated, the principle that regulates the balance of life… Expand
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Highly Cited
1998
Highly Cited
1998
We report here the purification of a cytosolic protein that induces cytochrome c release from mitochondria in response to caspase… Expand
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Highly Cited
1997
Highly Cited
1997
The Fas cell surface receptor induces apoptosis upon receptor oligomerization. We have identified a novel signaling protein… Expand
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Highly Cited
1996
Highly Cited
1996
To identify CAP3 and CAP4, components of the CD95 (Fas/APO-1) death-inducing signaling complex, we utilized nano-electrospray… Expand
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Highly Cited
1996
Highly Cited
1996
Fas/APO-1 and p55 tumor necrosis factor (TNF) receptor (p55-R) activate cellular mechanisms that result in cell death. Upon… Expand
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Highly Cited
1995
Highly Cited
1995
Using the cytoplasmic domain of Fas in the yeast two-hybrid system, we have identified a novel interacting protein, FADD, which… Expand
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