Other search tools

About this data

The publication data currently available has been vetted by Vanderbilt faculty, staff, administrators and trainees. The data itself is retrieved directly from NCBI's PubMed and is automatically updated on a weekly basis to ensure accuracy and completeness.

If you have any questions or comments, please contact us.

Results: 51 to 53 of 53

Publication Record

Connections

NMR structure and mutagenesis of the inhibitor-of-apoptosis protein XIAP.
Sun C, Cai M, Gunasekera AH, Meadows RP, Wang H, Chen J, Zhang H, Wu W, Xu N, Ng SC, Fesik SW
(1999) Nature 401: 818-22
MeSH Terms: Amino Acid Sequence, Amino Acids, Caspase 3, Caspase Inhibitors, Caspases, Enzyme Inhibitors, Escherichia coli, Humans, In Vitro Techniques, Jurkat Cells, Models, Molecular, Molecular Sequence Data, Mutagenesis, Site-Directed, Nuclear Magnetic Resonance, Biomolecular, Protein Conformation, Protein Structure, Tertiary, Proteins, Recombinant Proteins, Sequence Homology, Amino Acid, X-Linked Inhibitor of Apoptosis Protein
Show Abstract · Added March 5, 2014
The inhibitor-of-apoptosis (IAP) family of proteins, originally identified in baculoviruses, regulate programmed cell death in a variety of organisms. IAPs inhibit specific enzymes (caspases) in the death cascade and contain one to three modules of a common 70-amino-acid motif called the BIR domain. Here we describe the nuclear magnetic resonance structure of a region encompassing the second BIR domain (BIR2) of a human IAP family member, XIAP (also called hILP or MIHA). The structure of the BIR domain consists of a three-stranded antiparallel beta-sheet and four alpha-helices and resembles a classical zinc finger. Unexpectedly, conserved amino acids within the linker region between the BIR1 and BIR2 domains were found to be critical for inhibiting caspase-3. The absence or presence of these residues may explain the differences in caspase inhibition observed for different truncated and full-length IAPs. Our data further indicate that these residues may bind to the active site and that the BIR domain may interact with an adjacent site on the enzyme.
0 Communities
1 Members
0 Resources
20 MeSH Terms
Three-dimensional structures of proteins involved in programmed cell death.
Liang H, Fesik SW
(1997) J Mol Biol 274: 291-302
MeSH Terms: Animals, Apoptosis, Caspase 3, Caspases, Cysteine Endopeptidases, Humans, Models, Molecular, Protein Conformation, Proteins, Proto-Oncogene Proteins c-bcl-2, Receptors, Tumor Necrosis Factor
Show Abstract · Added March 5, 2014
Programmed cell death (apoptosis) is a controlled process by which unwanted cells are selectively eliminated. Several families of proteins including the Bcl-2, tumor necrosis factor receptor 1, and caspase families play essential roles in the regulation, signaling, and execution of the genetic cell death program. The recently described three-dimensional structures of members of these families elucidate the structural basis of their functions and provide insights into the mechanisms by which these proteins regulate apoptosis.
Copyright 1997 Academic Press Limited.
0 Communities
1 Members
0 Resources
11 MeSH Terms
Comparison of apoptosis in wild-type and Fas-resistant cells: chemotherapy-induced apoptosis is not dependent on Fas/Fas ligand interactions.
Eischen CM, Kottke TJ, Martins LM, Basi GS, Tung JS, Earnshaw WC, Leibson PJ, Kaufmann SH
(1997) Blood 90: 935-43
MeSH Terms: Affinity Labels, Antineoplastic Agents, Antineoplastic Agents, Phytogenic, Apoptosis, Biotin, Camptothecin, Caspase 3, Caspase 7, Caspases, Cisplatin, Cysteine Endopeptidases, Doxorubicin, Drug Resistance, Neoplasm, Enzyme Inhibitors, Etoposide, Fas Ligand Protein, Flow Cytometry, Humans, Lamin Type B, Lamins, Leukemia-Lymphoma, Adult T-Cell, Membrane Glycoproteins, Methotrexate, Neoplasm Proteins, Nuclear Proteins, Oligopeptides, Poly(ADP-ribose) Polymerases, Staurosporine, Topoisomerase II Inhibitors, Topotecan, Tumor Cells, Cultured, fas Receptor
Show Abstract · Added March 5, 2014
The Fas/Fas ligand (FasL) pathway is widely involved in apoptotic cell death in lymphoid and nonlymphoid cells. It has recently been postulated that many chemotherapeutic agents also induce cell death by activating the Fas/FasL pathway. In the present study we compared apoptotic pathways induced by anti-Fas or chemotherapeutic agents in the Jurkat human T-cell leukemia line. Immunoblotting showed that treatment of wild-type Jurkat cells with anti-Fas or the topoisomerase II-directed agent etoposide resulted in proteolytic cleavage of precursors for the cysteine-dependent aspartate-directed proteases caspase-3 and caspase-7 and degradation of the caspase substrates poly(ADP-ribose) polymerase (PARP) and lamin B1. Likewise, affinity labeling with N-(N(alpha)-benzyloxycarbonylglutamyl-N(epsilon)-biotinyllysyl+ ++)aspartic acid [(2,6-dimethyl-benzoyl)oxy]methyl ketone [Z-EK(bio)D-amok] labeled the same five active caspase species after each treatment, suggesting that the same downstream apoptotic pathways have been activated by anti-Fas and etoposide. Treatment with ZB4, an antibody that inhibits Fas-mediated cell death, failed to block etoposide-induced apoptosis, raising the possibility that etoposide does not initiate apoptosis through Fas/FasL interactions. To further explore the relationship between Fas- and chemotherapy-induced apoptosis, Fas-resistant Jurkat cells were treated with various chemotherapeutic agents. Multiple independently derived Fas-resistant Jurkat lines underwent apoptosis that was indistinguishable from that of the Fas-sensitive parental cells after treatment with etoposide, doxorubicin, topotecan, cisplatin, methotrexate, staurosporine, or gamma-irradiation. These results indicate that antineoplastic treatments induce apoptosis through a Fas-independent pathway even though Fas- and chemotherapy-induced pathways converge on common downstream apoptotic effector molecules.
0 Communities
1 Members
0 Resources
32 MeSH Terms