Phosphorylation by cdc2 kinase modulates DNA binding activity of high mobility group I nonhistone chromatin protein.
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[1] B. Beutler,et al. Interactive effects of the tumor necrosis factor promoter and 3'-untranslated regions. , 1991, Journal of immunology.
[2] M. Nissen,et al. Phosphorylation of the DNA-binding domain of nonhistone high-mobility group I protein by cdc2 kinase: reduction of binding affinity. , 1991, Proceedings of the National Academy of Sciences of the United States of America.
[3] J. Schalken,et al. Identification of high mobility group protein I(Y) as potential progression marker for prostate cancer by differential hybridization analysis. , 1991, Cancer research.
[4] H. Piwnica-Worms,et al. cdc2 gene expression at the G1 to S transition in human T lymphocytes. , 1990, Science.
[5] D. Marshak,et al. Cell cycle control of DNA replication by a homologue from human cells of the p34cdc2 protein kinase. , 1990, Science.
[6] T. Chambers,et al. Purification and characterization of growth-associated H1 histone kinase from Novikoff hepatoma cells. , 1990, The Journal of biological chemistry.
[7] G. Draetta,et al. Cell cycle control in eukaryotes: molecular mechanisms of cdc2 activation. , 1990, Trends in biochemical sciences.
[8] R. Clegg,et al. Binding characteristics of Hoechst 33258 with calf thymus DNA, poly[d(A-T)], and d(CCGGAATTCCGG): multiple stoichiometries and determination of tight binding with a wide spectrum of site affinities. , 1990, Biochemistry.
[9] S. Laland,et al. The metaphase specific phosphorylation of HMG I. , 1990, Biochemical and biophysical research communications.
[10] A. Jerzmanowski,et al. Flanking sequences of Xenopus 5 S RNA genes determine differential inhibition of transcription by H1 histone in vitro. Mitotic phosphorylation of H1 decreases its inhibitory power. , 1990, The Journal of biological chemistry.
[11] M. Nissen,et al. The A.T-DNA-binding domain of mammalian high mobility group I chromosomal proteins. A novel peptide motif for recognizing DNA structure. , 1990, The Journal of biological chemistry.
[12] S. Moreno,et al. Substrates for p34 cdc2 : In vivo veritas? , 1990, Cell.
[13] C. Hill,et al. Phosphorylation at clustered ‐Ser‐Pro‐X‐Lys/Arg‐ motifs in sperm‐specific histones H1 and H2B. , 1990, The EMBO journal.
[14] R. Reeves,et al. Expression of mRNAs encoding mammalian chromosomal proteins HMG-I and HMG-Y during cellular proliferation. , 1990, Experimental cell research.
[15] F. Studier,et al. Use of T7 RNA polymerase to direct expression of cloned genes. , 1990, Methods in enzymology.
[16] J. Wienberg,et al. Cis-acting sequences from mouse rDNA promote plasmid DNA amplification and persistence in mouse cells: implication of HMG-I in their function. , 1989, Nucleic acids research.
[17] M. Suzuki,et al. ‘SPKK’ motifs prefer to bind to DNA at A/T‐rich sites. , 1989, The EMBO journal.
[18] R. Reeves,et al. High-mobility group protein HMG-I localizes to G/Q- and C-bands of human and mouse chromosomes , 1989, The Journal of cell biology.
[19] J. Palvimo,et al. Identification of sites on chromosomal protein HMG‐I phosphorylated by casein kinase II , 1989, FEBS letters.
[20] A. Balmain,et al. Analysis of the HMGI nuclear proteins in mouse neoplastic cells induced by different procedures. , 1989, Experimental cell research.
[21] J. Maller,et al. Mammalian growth-associated H1 histone kinase: a homolog of cdc2+/CDC28 protein kinases controlling mitotic entry in yeast and frog cells , 1989, Molecular and cellular biology.
[22] M. Birnstiel,et al. Cloning of cDNAs coding for human HMG I and HMG Y proteins: both are capable of binding to the octamer sequence motif. , 1989, Nucleic acids research.
[23] M. Suzuki. SPXX, a frequent sequence motif in gene regulatory proteins. , 1989, Journal of molecular biology.
[24] R. Reeves,et al. Alternative processing of mRNAs encoding mammalian chromosomal high-mobility-group proteins HMG-I and HMG-Y , 1989, Molecular and cellular biology.
[25] David Beach,et al. cdc2 protein kinase is complexed with both cyclin A and B: Evidence for proteolytic inactivation of MPF , 1989, Cell.
[26] M. Suzuki,et al. SPKK, a new nucleic acid‐binding unit of protein found in histone. , 1989, The EMBO journal.
[27] R. Reeves,et al. Complete murine cDNA sequence, genomic structure, and tissue expression of the high mobility group protein HMG-I(Y). , 1988, The Journal of biological chemistry.
[28] L. Meijer,et al. cdc2 is a component of the M phase-specific histone H1 kinase: Evidence for identity with MPF , 1988, Cell.
[29] M. Ptashne. How eukaryotic transcriptional activators work , 1988, Nature.
[30] J. Labbé,et al. Activation at M-phase of a protein kinase encoded by a starfish homologue of the cell cycle control gene cdc2+ , 1988, Nature.
[31] H. Yang-Yen,et al. Purification and characterization of a high-mobility-group-like DNA-binding protein that stimulates rRNA synthesis in vitro , 1988, Molecular and cellular biology.
[32] Jean Gautier,et al. Purified maturation-promoting factor contains the product of a Xenopus homolog of the fission yeast cell cycle control gene cdc2 + , 1988, Cell.
[33] D. Beach,et al. The Xenopus cdc2 protein is a component of MPF, a cytoplasmic regulator of mitosis , 1988, Cell.
[34] M. Weiner,et al. A simple and rapid method for the selection of oligodeoxynucleotide-directed mutants. , 1988, Gene.
[35] C. Astell,et al. Interaction of the mouse chromosomal protein HMG-I with the 3' ends of genes in vitro. , 1988, The Journal of biological chemistry.
[36] J. Palvimo,et al. Selective decrease in low‐M r HMG proteins HMG I and HMG Y during differentiation of mouse teratocarcinoma cells , 1988, FEBS letters.
[37] D. Poccia,et al. Interaction of sperm histone variants and linker DNA during spermiogenesis in the sea urchin. , 1988, Biochemistry.
[38] M. Nissen,et al. Posttranscriptional gene regulation and specific binding of the nonhistone protein HMG-I by the 3' untranslated region of bovine interleukin 2 cDNA. , 1987, Proceedings of the National Academy of Sciences of the United States of America.
[39] A. Fusco,et al. Elevated levels of a specific class of nuclear phosphoproteins in cells transformed with v‐ras and v‐mos oncogenes and by cotransfection with c‐myc and polyoma middle T genes. , 1987, The EMBO journal.
[40] S. Laland,et al. Fractionation and identification of metaphase-specific phosphorylated forms of high-mobility-group proteins. , 1987, European journal of biochemistry.
[41] P. Nurse,et al. Complementation used to clone a human homologue of the fission yeast cell cycle control gene cdc2 , 1987, Nature.
[42] M. Nissen,et al. Specific A . T DNA sequence binding of RP-HPLC purified HMG-I. , 1987, Biochemical and biophysical research communications.
[43] S W Lin,et al. Vectors for selective expression of cloned DNAs by T7 RNA polymerase. , 1987, Gene.
[44] R. Reeves,et al. Purification and postsynthetic modifications of Friend erythroleukemic cell high mobility group protein HMG-I. , 1986, Analytical biochemistry.
[45] M. Nissen,et al. Molecular cloning of a functional bovine interleukin 2 cDNA. , 1986, Proceedings of the National Academy of Sciences of the United States of America.
[46] M. Solomon,et al. A mammalian high mobility group protein recognizes any stretch of six A.T base pairs in duplex DNA. , 1986, Proceedings of the National Academy of Sciences of the United States of America.
[47] D. Poccia,et al. Phosphorylation of sea urchin sperm H1 and H2B histones precedes chromatin decondensation and H1 exchange during pronuclear formation. , 1985, Developmental biology.
[48] S. Laland,et al. On the phosphorylation of low molecular mass HMG (high mobility group) proteins in Ehrlich ascites cells , 1985, FEBS letters.
[49] P. Nurse. Cell cycle control genes in yeast , 1985 .
[50] M. Record,et al. Ions as regulators of protein-nucleic acid interactions in vitro and in vivo. , 1985, Advances in biophysics.
[51] A. Varshavsky,et al. A protein binds to a satellite DNA repeat at three specific sites that would be brought into mutual proximity by DNA folding in the nucleosome , 1984, Cell.
[52] J. Sambrook,et al. Molecular Cloning: A Laboratory Manual , 2001 .
[53] S. Laland,et al. On the presence of two new high mobility group‐like proteins in HeLa S3 cells , 1983, FEBS letters.
[54] T. Langan. Characterization of highly phosphorylated subcomponents of rat thymus H1 histone. , 1982, The Journal of biological chemistry.
[55] R. Rai,et al. A bifunctional gene product involved in two phases of the yeast cell cycle , 1982, Nature.
[56] J. Broach,et al. The Molecular biology of the yeast saccharomyces, life cycle and inheritance , 1981 .
[57] C. E. Zeilig,et al. Studies on the mechanism of activation of mitotic histone H1 kinase. , 1980, Biochemical and biophysical research communications.
[58] R. Baserga,et al. [20] Cell synchronization , 1979 .
[59] M. Sung,et al. Sites of in vivo phosphorylation of histone H5. , 1978, Biochemistry.
[60] T. Lohman,et al. Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: the roles of ion association or release, screening, and ion effects on water activity , 1978, Quarterly Reviews of Biophysics.
[61] E. Bradbury,et al. Control of Cell Division by Very Lysine Rich Histone (F1) Phosphorylation , 1974, Nature.
[62] L. R. Gurley,et al. CELL CYCLE-SPECIFIC CHANGES IN HISTONE PHOSPHORYLATION ASSOCIATED WITH CELL PROLIFERATION AND CHROMOSOME CONDENSATION , 1974, The Journal of cell biology.
[63] E. Bradbury,et al. Phosphorylation of very-lysine-rich histone in Physarum polycephalum. Correlation with chromosome condensation. , 1973, European journal of biochemistry.
[64] N. Salzman,et al. Occurrence and properties of a chromatin-associated F1-histone phosphokinase in mitotic Chinese hamster cells. , 1972, Biochemistry.