Purification and molecular cloning of the APO-1 cell surface antigen, a member of the tumor necrosis factor/nerve growth factor receptor superfamily. Sequence identity with the Fas antigen.
A. Oehm,Iris Behrmann,Werner Falk,Michael Pawlita,Gerhard Maier,C. Klas,Min Li-Weber,S. Richards,Jens Dhein,B. C. Trauth +9 more
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TLDR
The APO-1 antigen was expressed upon transfection of APo-1 cDNA into BL60-P7 Burkitt's lymphoma cells and conferred sensitivity towards anti-APO- 1-induced apoptosis to the transfectants.About:
This article is published in Journal of Biological Chemistry.The article was published on 1992-05-25 and is currently open access. It has received 886 citations till now. The article focuses on the topics: B-cell receptor & T-cell receptor.read more
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Apoptosis by death factor.
TL;DR: This work was supported in part by Grants-in-Aid from the Ministry of Education, Science, and Culture of Japan and by a Research Grant from the Princess Takamatsu Cancer Research Fund, and performed in part through Special Coordination Funds of the Science and Technology Agency of the Japanese Government.
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The Fas Death Factor
Shigekazu Nagata,Pierre Golstein +1 more
TL;DR: Fas ligand (FasL), a cell surface molecule belonging to the tumor necrosis factor family, binds to its receptor Fas, thus inducing apoptosis of Fas-bearing cells.
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FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death--inducing signaling complex.
Marta Muzio,Arul M. Chinnaiyan,Frank C. Kischkel,Karen O'Rourke,Andrej Shevchenko,Jian Ni,Carsten Scaffidi,James D. Bretz,Mei Zhang,Reiner L. Gentz,Matthias Mann,Peter H. Krammer,Marcus E. Peter,Vishva M. Dixit +13 more
TL;DR: This work utilized nano-electrospray tandem mass spectrometry to identify CAP3 and CAP4, components of the CD95 (Fas/APO-1) death-inducing signaling complex, and found a novel 55 kDa protein, designated FLICE, which has homology to both FADD and the ICE/CED-3 family of cysteine proteases.
Journal ArticleDOI
Molecular cloning and expression of the fas ligand, a novel member of the tumor necrosis factor family
TL;DR: Northern hybridization revealed that Fas ligand is expressed in activated splenocytes and thymocytes, consistent with its involvement in T cell-mediated cytotoxicity and in several nonlymphoid tissues, such as testis.
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Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor.
Frank C. Kischkel,Stefan Hellbardt,Iris Behrmann,Matthias Germer,Michael Pawlita,Peter H. Krammer,Marcus E. Peter +6 more
TL;DR: The data suggest that in vivo CAP1–4 are the APO‐1 apoptosis‐transducing molecules.
References
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
TL;DR: This assay is very reproducible and rapid with the dye binding process virtually complete in approximately 2 min with good color stability for 1 hr with little or no interference from cations such as sodium or potassium nor from carbohydrates such as sucrose.
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DNA sequencing with chain-terminating inhibitors
TL;DR: A new method for determining nucleotide sequences in DNA is described, which makes use of the 2',3'-dideoxy and arabinon nucleoside analogues of the normal deoxynucleoside triphosphates, which act as specific chain-terminating inhibitors of DNA polymerase.
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Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.
TL;DR: A method has been devised for the electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets that results in quantitative transfer of ribosomal proteins from gels containing urea.
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A simple method for displaying the hydropathic character of a protein
Jack Kyte,Russell F. Doolittle +1 more
TL;DR: A computer program that progressively evaluates the hydrophilicity and hydrophobicity of a protein along its amino acid sequence has been devised and its simplicity and its graphic nature make it a very useful tool for the evaluation of protein structures.