KBTBD7, a novel human BTB-kelch protein, activates transcriptional activities of SRE and AP-1.
暂无分享,去创建一个
K. Ocorr | R. Bodmer | Yun Deng | W. Yuan | Yuequn Wang | X. Mo | Yongqing Li | Xiushan Wu | M. Tang | Xiongwei Fan | Y. Wan | Junjian Hu | Zaochu Ying
[1] K. Ocorr,et al. A novel human BTB-kelch protein KLHL31, strongly expressed in muscle and heart, inhibits transcriptional activities of TRE and SRE. , 2008, Molecules and cells.
[2] I. Shih,et al. A BTB/POZ protein, NAC-1, is related to tumor recurrence and is essential for tumor growth and survival , 2006, Proceedings of the National Academy of Sciences.
[3] C. Vedeler,et al. Detection of Autoantibodies to the BTB‐kelch Protein KLHL7 in Cancer Sera , 2006, Scandinavian journal of immunology.
[4] Weishi Yu,et al. hnulp1, a basic helix-loop-helix protein with a novel transcriptional repressive domain, inhibits transcriptional activity of serum response factor. , 2006, Biochemical and biophysical research communications.
[5] D. Ginty,et al. Restricted inactivation of serum response factor to the cardiovascular system. , 2004, Proceedings of the National Academy of Sciences of the United States of America.
[6] P. Stogios,et al. The BACK domain in BTB-kelch proteins. , 2004, Trends in biochemical sciences.
[7] Masayuki Yamamoto,et al. Oxidative Stress Sensor Keap1 Functions as an Adaptor for Cul3-Based E3 Ligase To Regulate Proteasomal Degradation of Nrf2 , 2004, Molecular and Cellular Biology.
[8] Dali Li,et al. Inhibition of transcriptional activities of AP-1 and c-Jun by a new zinc finger protein ZNF394. , 2004, Biochemical and biophysical research communications.
[9] J. Concordet,et al. Targeted Inactivation of Serum Response Factor in the Developing Heart Results in Myocardial Defects and Embryonic Lethality , 2004, Molecular and Cellular Biology.
[10] Masayuki Yamamoto,et al. Scaffolding of Keap1 to the actin cytoskeleton controls the function of Nrf2 as key regulator of cytoprotective phase 2 genes , 2004, Proceedings of the National Academy of Sciences of the United States of America.
[11] Soren Prag,et al. Molecular phylogeny of the kelch-repeat superfamily reveals an expansion of BTB/kelch proteins in animals , 2003, BMC Bioinformatics.
[12] J. Yates,et al. BTB/POZ domain proteins are putative substrate adaptors for cullin 3 ubiquitin ligases. , 2003, Molecular cell.
[13] E. Nishida,et al. Molecular recognitions in the MAP kinase cascades. , 2003, Cellular signalling.
[14] F. Laski,et al. The bric à brac locus consists of two paralogous genes encoding BTB/POZ domain proteins and acts as a homeotic and morphogenetic regulator of imaginal development in Drosophila. , 2002, Development.
[15] T. Hasson,et al. A human homologue of Drosophila kelch associates with myosin-VIIa in specialized adhesion junctions. , 2002, Cell motility and the cytoskeleton.
[16] R. Tjian,et al. Transcription factor MIZ-1 is regulated via microtubule association. , 2001, Molecular cell.
[17] X. Estivill,et al. Identification and characterization of BTBD1, a novel BTB domain containing gene on human chromosome 15q24. , 2001, Gene.
[18] M. Koenig,et al. The gene encoding gigaxonin, a new member of the cytoskeletal BTB/kelch repeat family, is mutated in giant axonal neuropathy , 2000, Nature Genetics.
[19] J. Licht,et al. In-Depth Mutational Analysis of the Promyelocytic Leukemia Zinc Finger BTB/POZ Domain Reveals Motifs and Residues Required for Biological and Transcriptional Functions , 2000, Molecular and Cellular Biology.
[20] Y. Jan,et al. The Polar T1 Interface Is Linked to Conformational Changes that Open the Voltage-Gated Potassium Channel , 2000, Cell.
[21] Robert A. H. White,et al. Characterization of Mayven, a novel actin-binding protein predominantly expressed in brain. , 1999, Molecular biology of the cell.
[22] J. D. Engel,et al. Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain. , 1999, Genes & development.
[23] E. Krebs,et al. Association of mitogen-activated protein kinase with the microtubule cytoskeleton. , 1995, Proceedings of the National Academy of Sciences of the United States of America.
[24] J. Thompson,et al. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. , 1994, Nucleic acids research.
[25] A. Nordheim,et al. Occupation of the c-fos serum response element in vivo by a multi-protein complex is unaltered by growth factor induction , 1989, Nature.