Expression, purification, and biochemical characterization of SAG, a ring finger redox-sensitive protein.

[1]  S. Elledge,et al.  Rbx1, a component of the VHL tumor suppressor complex and SCF ubiquitin ligase. , 1999, Science.

[2]  S. Elledge,et al.  Reconstitution of G1 cyclin ubiquitination with complexes containing SCFGrr1 and Rbx1. , 1999, Science.

[3]  Z. Ronai,et al.  Recruitment of a ROC1–CUL1 Ubiquitin Ligase by Skp1 and HOS to Catalyze the Ubiquitination of IκBα , 1999 .

[4]  Y. Xiong,et al.  ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity. , 1999, Molecular cell.

[5]  M. Swaroop,et al.  SAG, a Novel Zinc RING Finger Protein That Protects Cells from Apoptosis Induced by Redox Agents , 1999, Molecular and Cellular Biology.

[6]  E. Fearon,et al.  Siah-1 N-Terminal RING Domain Is Required for Proteolysis Function, and C-Terminal Sequences Regulate Oligomerization and Binding to Target Proteins , 1999, Molecular and Cellular Biology.

[7]  J. Rouvinen,et al.  Activation and Oligomerization of Aspartylglucosaminidase* , 1998, The Journal of Biological Chemistry.

[8]  G. Cheng,et al.  An Intact Zinc Ring Finger Is Required for Tumor Necrosis Factor Receptor-associated Factor-mediated Nuclear Factor-κB Activation but Is Dispensable for c-Jun N-terminal Kinase Signaling* , 1998, The Journal of Biological Chemistry.

[9]  D. Baltimore,et al.  Essential role of CED-4 oligomerization in CED-3 activation and apoptosis. , 1998, Science.

[10]  Tao Yan,et al.  Overexpression of Manganese Superoxide Dismutase Suppresses Tumor Necrosis Factor-induced Apoptosis and Activation of Nuclear Transcription Factor-κB and Activated Protein-1* , 1998, The Journal of Biological Chemistry.

[11]  H. Steller.  Artificial death switches: induction of apoptosis by chemically induced caspase multimerization. , 1998, Proceedings of the National Academy of Sciences of the United States of America.

[12]  A. Kristjuhan,et al.  Oligomerization of p53 is necessary to inhibit its transcriptional transactivation property at high protein concentration , 1998, Oncogene.

[13]  Kohei Miyazono,et al.  Mammalian thioredoxin is a direct inhibitor of apoptosis signal‐regulating kinase (ASK) 1 , 1998, The EMBO journal.

[14]  J C Reed,et al.  A Single BIR Domain of XIAP Sufficient for Inhibiting Caspases* , 1998, The Journal of Biological Chemistry.

[15]  G. Storz,et al.  Activation of the OxyR transcription factor by reversible disulfide bond formation. , 1998, Science.

[16]  B. Mignotte,et al.  Mitochondria and apoptosis. , 1998, European journal of biochemistry.

[17]  Xiantao Wang,et al.  Dopamine Induces Apoptosis through an Oxidation-involved SAPK/JNK Activation Pathway* , 1998, The Journal of Biological Chemistry.

[18]  G. Powis,et al.  Thioredoxin, a gene found overexpressed in human cancer, inhibits apoptosis in vitro and in vivo. , 1997, Cancer research.

[19]  J. Thorner,et al.  Ste5 RING-H2 domain: role in Ste4-promoted oligomerization for yeast pheromone signaling. , 1997, Science.

[20]  J. Lazo,et al.  Enhanced apoptosis in metallothionein null cells. , 1997, Molecular pharmacology.

[21]  R van Driel,et al.  RING1 is associated with the polycomb group protein complex and acts as a transcriptional repressor , 1997, Molecular and cellular biology.

[22]  Yi Sun.  Induction of glutathione synthetase by 1,10‐phenanthroline , 1997, FEBS letters.

[23]  K. Mori,et al.  AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[24]  Yi Sun,et al.  Activation of p53 transcriptional activity by 1,10-phenanthroline, a metal chelator and redox sensitive compound , 1997, Oncogene.

[25]  L. Packer,et al.  Redox regulation of NF-kappa B activation. , 1997, Free radical biology & medicine.

[26]  Anne M. Bowcock,et al.  Identification of a RING protein that can interact in vivo with the BRCA1 gene product , 1996, Nature Genetics.

[27]  H. Hanafusa,et al.  Evidence for a transcriptional activation function of BRCA1 C-terminal region. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[28]  I. Verma,et al.  Transcriptional activation by BRCA1 , 1996, Nature.

[29]  A. Levine,et al.  The MDM2 Oncoprotein Binds Specifically to RNA through its RING Finger Domain , 1996, Molecular medicine.

[30]  P. Freemont,et al.  Does this have a familiar RING? , 1996, Trends in biochemical sciences.

[31]  P. Freemont,et al.  The RING finger domain: a recent example of a sequence-structure family. , 1996, Current opinion in structural biology.

[32]  D. Vaux,et al.  Cloning and expression of apoptosis inhibitory protein homologs that function to inhibit apoptosis and/or bind tumor necrosis factor receptor-associated factors. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[33]  Y. Matsuzawa,et al.  The protective role of glutathione peroxidase in apoptosis induced by reactive oxygen species. , 1996, Journal of biochemistry.

[34]  I. Kola,et al.  Elevation in the ratio of Cu/Zn-superoxide dismutase to glutathione peroxidase activity induces features of cellular senescence and this effect is mediated by hydrogen peroxide. , 1996, Human molecular genetics.

[35]  Y. Sun,et al.  Redox regulation of transcriptional activators. , 1996, Free radical biology & medicine.

[36]  A. Levine,et al.  Two domains of p53 interact with the TATA-binding protein, and the adenovirus 13S E1A protein disrupts the association, relieving p53-mediated transcriptional repression , 1995, Molecular and cellular biology.

[37]  R. J. Clem,et al.  Control of programmed cell death by the baculovirus genes p35 and iap , 1994, Molecular and cellular biology.

[38]  P. Freemont,et al.  The p53-associated protein MDM2 contains a newly characterized zinc-binding domain called the RING finger. , 1994, Trends in biochemical sciences.

[39]  A. V. von Arnim,et al.  Ring finger motif of Arabidopsis thaliana COP1 defines a new class of zinc-binding domain. , 1993, The Journal of biological chemistry.

[40]  Z. Dong,et al.  Dosage‐dependent dominance over wild‐type p53 of a mutant p53 isolated from nasopharyngeal carcinoma 1 , 1993, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[41]  R. Lovering,et al.  Identification and preliminary characterization of a protein motif related to the zinc finger. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[42]  M. Aviram.  Modified forms of low density lipoprotein and atherosclerosis. , 1993, Atherosclerosis.

[43]  N. Colburn,et al.  A simple method using PCR for direct sequencing of genomic DNA from frozen tumor tissue embedded in optimal cutting temperature compound. , 1992, BioTechniques.

[44]  Yang Shi,et al.  Transcriptional repression by YY1, a human GLI-Krüippel-related protein, and relief of repression by adenovirus E1A protein , 1991, Cell.

[45]  J. Trowsdale,et al.  A novel gysteine-rich sequence motif , 1991, Cell.

[46]  K. Nose,et al.  Stimulation by hydrogen peroxide of DNA synthesis, competence family gene expression and phosphorylation of a specific protein in quiescent Balb/3T3 cells. , 1990, Oncogene.

[47]  Y. Sun,et al.  Free radicals, antioxidant enzymes, and carcinogenesis. , 1990, Free radical biology & medicine.

[48]  A. Holmgren,et al.  Thioredoxin and glutaredoxin systems. , 2019, The Journal of biological chemistry.

[49]  H. Esterbauer,et al.  A spectrophotometric assay for lipid peroxides in serum lipoproteins using a commercially available reagent. , 1989, Journal of lipid research.

[50]  R. G. Allen,et al.  Oxidative influence on development and differentiation: an overview of a free radical theory of development. , 1989, Free radical biology & medicine.

[51]  Jun Ma,et al.  GAL4-VP16 is an unusually potent transcriptional activator , 1988, Nature.

[52]  S. McKnight,et al.  Functional dissection of VP16, the trans-activator of herpes simplex virus immediate early gene expression. , 1988, Genes & development.

[53]  F S Mathews,et al.  The structure, function and evolution of cytochromes. , 1985, Progress in biophysics and molecular biology.

[54]  S. Aust,et al.  Microsomal lipid peroxidation. , 1978, Methods in enzymology.

[55]  E. Margoliash,et al.  [61] Cytochrome c from vertebrate and invertebrate sources , 1967 .