Genetic Analysis of Growth Inhibition by GAL 4-IKB-o . . in Saccharomyces cerevisiae
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[1] L. Guarente,et al. ADA3, a putative transcriptional adaptor, consists of two separable domains and interacts with ADA2 and GCN5 in a trimeric complex , 1995, Molecular and cellular biology.
[2] L. Guarente,et al. Yeast ADA2 protein binds to the VP16 protein activation domain and activates transcription. , 1994, Proceedings of the National Academy of Sciences of the United States of America.
[3] T. Rabbitts,et al. Chromosomal translocations in human cancer , 1994, Nature.
[4] B. Cullen,et al. Mutational analysis of the transcription activation domain of RelA: identification of a highly synergistic minimal acidic activation module , 1994, Molecular and cellular biology.
[5] T. Gilmore,et al. Interaction of the v-Rel oncoprotein with cellular transcription factor Sp1 , 1994, Journal of virology.
[6] P. Baeuerle,et al. A proteasome inhibitor prevents activation of NF‐kappa B and stabilizes a newly phosphorylated form of I kappa B‐alpha that is still bound to NF‐kappa B. , 1994, The EMBO journal.
[7] S. Berger,et al. Functional similarity and physical association between GCN5 and ADA2: putative transcriptional adaptors. , 1994, The EMBO journal.
[8] T. Gilmore,et al. NF-kappa B p100 is one of the high-molecular-weight proteins complexed with the v-Rel oncoprotein in transformed chicken spleen cells , 1993, Journal of virology.
[9] R. Taub,et al. I kappa B alpha can localize in the nucleus but shows no direct transactivation potential. , 1993, Oncogene.
[10] K. Middleton,et al. An essential yeast protein, CBF5p, binds in vitro to centromeres and microtubules , 1993, Molecular and cellular biology.
[11] P. Morin,et al. GAL4-lϰBα and GAL4-lϰBγ activate transcription by different mechanisms , 1993 .
[12] G. Mosialos,et al. v-Rel and c-Rel are differentially affected by mutations at a consensus protein kinase recognition sequence. , 1993, Oncogene.
[13] S. Berger,et al. Genetic isolation of ADA2: A potential transcriptional adaptor required for function of certain acidic activation domains , 1992, Cell.
[14] P. Morin,et al. The C terminus of the NF-χB p50 precursor and an IχB isoform contain transcription activation domains , 1992 .
[15] V. Bennett,et al. The ANK repeat: a ubiquitous motif involved in macromolecular recognition. , 1992, Trends in cell biology.
[16] M. Boguski,et al. Comparative analysis of the β transducin family with identification of several new members including PWP1, a nonessential gene of Saccharomyces cerevisiae that is divergently transcribed from NMT1 , 1992, Proteins.
[17] M. Miyagi,et al. NH2-terminal acetylation of ribosomal proteins of Saccharomyces cerevisiae. , 1992, The Journal of biological chemistry.
[18] E. Otaka,et al. Sequence and functional similarity between a yeast ribosomal protein and the Escherichia coli S5 ram protein , 1990, Molecular and cellular biology.
[19] H. Ronne,et al. Yeast MIG1 repressor is related to the mammalian early growth response and Wilms' tumour finger proteins. , 1990, The EMBO journal.
[20] A. Capobianco,et al. Cloning and expression of a chicken c-rel cDNA: unlike p59v-rel, p68c-rel is a cytoplasmic protein in chicken embryo fibroblasts. , 1990, Oncogene.
[21] Susumu,et al. Identification and characterization of genes and mutants for an N‐terminal acetyltransferase from yeast. , 1989, The EMBO journal.
[22] K. Isono,et al. Ribosomal protein modification in Escherichia coli , 2004, Molecular and General Genetics MGG.
[23] A. Goldberg,et al. The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B. , 1994, Cell.
[24] I. Wool. The Bifunctional Nature of Ribosomal Proteins and Speculations on Their Origins , 1993 .
[25] P. Morin,et al. The I kappa B proteins: members of a multifunctional family. , 1993, Trends in genetics : TIG.