نتایج جستجو برای: fadd

تعداد نتایج: 1166  

Journal: :Journal of Biological Chemistry 2000

Journal: :The Journal of Experimental Medicine 1999
Lars E. French Jürg Tschopp

C ell death by apoptosis is a tightly regulated physiological process that enables the elimination of unwanted cells. It is crucial for embryonic development and the maintenance of tissue homeostasis, but also for defense against certain infectious diseases and cancer. Apoptosis can be triggered from outside the cell, generally after cell–cell contact, by a family of transmembrane proteins call...

Journal: :The Journal of Experimental Medicine 1999
Keith B. Elkon

U ncontrolled lymphoproliferation is a characteristic feature of lymphomas and leukemias. Nonmalignant lym-phoproliferative diseases are also observed in humans as well as in lpr (lymphoproliferation) and gld (generalized lymphad-enopathy) mice. The discoveries that spontaneous mutations of Fas (APO-1/CD95) or its ligand (FasL) were associated with the lpr and gld phenotypes led to a satisfying...

Journal: :The Journal of biological chemistry 2003
Nicholas Harper Michelle A Hughes Stuart N Farrow Gerald M Cohen Marion MacFarlane

We have further examined the mechanism by which phorbol ester-mediated protein kinase C (PKC) activation protects against tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL)-induced cytotoxicity. We now report that activation of PKC targets death receptor signaling complex formation. Pre-treatment with 12-O-tetradecanoylphorbol-13-acetate (PMA) led to inhibition of TRAIL-induc...

2016
Bliss J. Chang Alexandra B. Samal Jiri Vlach Timothy F. Fernandez Dewey Brooke Peter E. Prevelige Jamil S. Saad Paul C. Driscoll

The extrinsic apoptotic pathway is initiated by binding of a Fas ligand to the ectodomain of the surface death receptor Fas protein. Subsequently, the intracellular death domain of Fas (FasDD) and that of the Fas-associated protein (FADD) interact to form the core of the death-inducing signaling complex (DISC), a crucial step for activation of caspases that induce cell death. Previous studies h...

2012
Clare McCourt Pamela Maxwell Roberta Mazzucchelli Rodolfo Montironi Marina Scarpelli Manuel Salto-Tellez Joe M. O'Sullivan Daniel B. Longley David J.J. Waugh

Purpose: To characterize the importance of cellular Fas-associated death domain (FADD)–like interleukin 1b-converting enzyme (FLICE) inhibitory protein (c-FLIP), a key regulator of caspase-8 (FLICE)– promoted apoptosis, inmodulating the response of prostate cancer cells to androgen receptor (AR)–targeted

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