Publications
117 results found
Swanton C, Card GL, Mann D, et al., 1999, Overcoming inhibitions: subversion of CKI function by viral cyclins, TRENDS IN BIOCHEMICAL SCIENCES, Vol: 24, Pages: 116-120, ISSN: 0968-0004
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- Citations: 23
Mann DJ, Child ES, Swanton C, et al., 1999, Modulation of p27<SUP>Kip1</SUP> levels by the cyclin encoded by Kaposi's sarcoma-associated herpesvirus, EMBO JOURNAL, Vol: 18, Pages: 654-663, ISSN: 0261-4189
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- Citations: 121
Armstrong CG, Dombradi V, Mann DJ, et al., 1998, Cloning of a novel testis specific protein serine/threonine phosphatase, PPN 58A, from Drosophila melanogaster., Biochim Biophys Acta, Vol: 1399, Pages: 234-238, ISSN: 0006-3002
A gene encoding a novel member of the PPP family of protein serine/threonine phosphatases, termed PPN 58A, was cloned from Drosophila melanogaster. The deduced amino acid sequence of PPN 58A exhibits 59-62% identity to D. melanogaster PP1 isoforms, 51% identity to D. melanogaster PPY 55A and < or = 40% identity to other members of the PPP family. The single copy gene PPN 58A maps to chromosome 2 locus 58A. Analysis of PPN 58A mRNA reveals that, like PPY 55A, PPN 58A is a testis specific enzyme.
Swanton C, Mann DJ, Fleckenstein B, et al., 1997, Herpes viral cyclin/Cdk6 complexes evade inhibition by CDK inhibitor proteins, NATURE, Vol: 390, Pages: 184-187, ISSN: 0028-0836
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- Citations: 275
Mann DJ, Higgins T, Jones NC, et al., 1997, Differential control of cyclins D1 and D3 and the cdk inhibitor p27(Kip1) by diverse signalling pathways in Swiss 3T3 cells, ONCOGENE, Vol: 14, Pages: 1759-1766, ISSN: 0950-9232
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- Citations: 50
Withers DJ, Seufferlein T, Mann D, et al., 1997, Rapamycin dissociates p70S6K activation from DNA synthesis stimulated by bombesin and insulin in swiss 3T3 cells, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 272, Pages: 2509-2514, ISSN: 0021-9258
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- Citations: 41
Seufferlein T, Withers DJ, Mann D, et al., 1996, Dissociation of mitogen-activated protein kinase activation from p125 focal adhesion kinase tyrosine phosphorylation in Swiss 3T3 cells stimulated by bombesin, lysophosphatidic acid, and platelet-derived growth factor, MOLECULAR BIOLOGY OF THE CELL, Vol: 7, Pages: 1865-1875, ISSN: 1059-1524
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- Citations: 59
Robinson C, Light Y, Groves R, et al., 1996, Cell-cycle regulation of B-Myb protein expression: Specific phosphorylation during the S phase of the cell cycle, ONCOGENE, Vol: 12, Pages: 1855-1864, ISSN: 0950-9232
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- Citations: 62
Mann DJ, Jones NC, 1996, E2F-1 but not E2F-4 can overcome p16-induced G1 cell-cycle arrest, CURRENT BIOLOGY, Vol: 6, Pages: 474-483, ISSN: 0960-9822
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- Citations: 61
Armstrong CG, Mann DJ, Berndt N, et al., 1995, Drosophila PPY, a novel male specific protein serine/threonine phosphatase localised in somatic cells of the testis., J Cell Sci, Vol: 108 ( Pt 11), Pages: 3367-3375, ISSN: 0021-9533
Drosophila protein phosphatase Y (PPY) displays 64% amino acid identity to protein serine/threonine phosphatase 1 (PP1) and 39% to protein phosphatase 2A (PP2A). Here we show by expression of cDNA in bacteria, that PPY is a protein serine phosphatase and that its biochemical properties are distinct from PP1 in both substrate specificity and regulation by the thermostable inhibitory proteins inhibitor 1 and inhibitor 2. We also demonstrate that PPY is a novel testis specific protein phosphatase by analysis of both mRNA and protein distribution. More precise immunolocalisation within the testis, using affinity purified anti-PPY protein and anti-PPY peptide antibodies, shows that PPY is present in somatic cyst cells, which encase the germ cells. The predominant location of PPY is in the nuclei of both head and tail cyst cells throughout the length of the testis except for the apical tip. The distribution of PPY, coupled with its unique biochemical properties, suggests that PPY may be required to prevent cyst cell division, increase transcription for provision of nutrients to the germ cells and/or provide a signal for spermatocyte differentiation.
LUKAS J, PARRY D, AAGAARD L, et al., 1995, RETINOBLASTOMA-PROTEIN-DEPENDENT CELL-CYCLE INHIBITION BY THE TUMOR-SUPPRESSOR P16, NATURE, Vol: 375, Pages: 503-506, ISSN: 0028-0836
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- Citations: 870
PARRY D, BATES S, MANN DJ, et al., 1995, LACK OF CYCLIN D-CDK COMPLEXES IN RB-NEGATIVE CELLS CORRELATES WITH HIGH-LEVELS OF P16(INK4/MTS1) TUMOR-SUPPRESSOR GENE-PRODUCT, EMBO JOURNAL, Vol: 14, Pages: 503-511, ISSN: 0261-4189
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- Citations: 391
Mann DJ, Dombrádi V, Cohen PT, 1993, Drosophila protein phosphatase V functionally complements a SIT4 mutant in Saccharomyces cerevisiae and its amino-terminal region can confer this complementation to a heterologous phosphatase catalytic domain., EMBO J, Vol: 12, Pages: 4833-4842, ISSN: 0261-4189
The sequence of a Drosophila melanogaster cDNA encoding a novel 35 kDa protein serine/threonine phosphatase, termed PPV, is presented. PPV is 40-41% identical to Drosophila PP1, 53% identical to Drosophila PP2A and 63% identical to Saccharomyces cerevisiae SIT4. Complementation studies demonstrated that PPV can functionally rescue a temperature sensitive mutant of SIT4, a protein phosphatase required for the G1 to S transition of the cell cycle. When placed under the SIT4 promoter, PPV cDNA is able to replace the SIT4 gene in S. cerevisiae. The amino-terminal domain of PPV fused to another phosphatase catalytic region (PP1) also rescues the temperature sensitive SIT4 mutant and the SIT4 deletion mutant, implicating this region in binding to regulatory subunits and/or altering specificity. In Drosophila, a substantial transient increase in both PPV mRNA and protein occurs in late syncytial and early cellular blastoderm embryos. At the latter stage PPV is localized to the cytoplasm of cells at the cortex. This increase in PPV correlates with introduction of the G2 phase of the cell cycle, elevated zygotic transcription and cellularization, indicating that PPV may play a role in one or more of these processes.
Dombrádi V, Mann DJ, Saunders RD, et al., 1993, Cloning of the fourth functional gene for protein phosphatase 1 in Drosophila melanogaster from its chromosomal location., Eur J Biochem, Vol: 212, Pages: 177-183, ISSN: 0014-2956
Complementary DNA encoding a catalytic subunit of protein phosphatase 1, PP1 87B, hybridises at four positions (87B, 9C, 13C and 96A) to Drosophila melanogaster polytene chromosomes, three of which are known to be expressed [Dombrádi, V., Axton, J.M., Brewis, N.D., Da Cruz e Silva, E.F., Alphey, L. & Cohen, P.T.W. (1990) Eur. J. Biochem. 194, 739-745]. The fourth gene has been isolated by screening a genomic library of cosmid clones, representing division 13 of the X-chromosome of D. melanogaster, with a PP1 87B probe. This library was constructed as part of the Drosophila genome mapping project [Sidén-Kiamos, I., Saunders, R.D.C., Spanos, L., Majerus, T., Trenear, J., Savakis, C., Louis, C., Glover, D.M., Ashburner, M. & Kafatos, F.C. (1990) Nucleic Acids Res. 18, 6261-6270]. The 5' non-coding region of the isolated gene hybridised to cytological position 13C1-2. By combining reverse transcription and the polymerase chain reaction, the gene was shown to be expressed at a very low level. The PP1 13C gene encodes a protein of 302 amino acids with a predicted molecular mass of 34.5 kDa. It shows 85-94% amino acid identity to the other three protein phosphatase 1 catalytic subunits (PP1 87B, PP1 96A and PP1 9C) described previously, being most closely related to the isoform PP1 87B, which is involved in the control of chromosome separation at cell division and the regulation of chromosome condensation at interphase.
Mann DJ, Strain AJ, Bailey E, 1992, Hormonal induction of malic enzyme in rat hepatocytes cultured on laminin-rich gels., J Mol Endocrinol, Vol: 8, Pages: 235-242, ISSN: 0952-5041
The levels of malic-enzyme mRNA and activity were determined in primary cultures of adult rat hepatocytes maintained on either rat-tail collagen or a laminin-rich substratum. Cells plated on laminin-rich gels exhibited substantially improved patterns of albumin and malic-enzyme expression when compared with cells maintained on rat-tail collagen. Moreover, hepatocytes plated on the laminin-rich matrix displayed marked malic-enzyme inducibility in response to tri-iodothyronine and dichloroacetate, especially in the presence of insulin. However, Northern blot analysis revealed that the ratio of the amounts of the two major malic-enzyme mRNA species (2.0 and 3.1 kb) was reversed when compared with that found in the liver in vivo, the altered levels of these two species being closer to those found in non-hepatic tissues. These findings indicate that, although the hormonal responsiveness of isolated hepatocytes maintained on laminin-rich gels is markedly improved, and approaches the degree of induction demonstrated in the liver in vivo, the mechanisms of control differ, indicating a loss of liver-specific expression.
Mann DJ, Campbell DG, McGowan CH, et al., 1992, Mammalian protein serine/threonine phosphatase 2C: cDNA cloning and comparative analysis of amino acid sequences., Biochim Biophys Acta, Vol: 1130, Pages: 100-104, ISSN: 0006-3002
Complementary DNA encoding rat protein phosphatase 2C alpha was obtained from a liver library and used to isolate the homologous cDNAs from rabbit liver and human teratocarcinoma libraries. The amino acid sequences of the three enzymes deduced from the cDNA (382 amino acids) were extremely similar (greater than 99% identity), the maximum number of differences (between rat and human) being four. Amino acid sequences of peptides corresponding to 238 residues (61%) of the protein phosphatase 2C beta isoform from rabbit skeletal muscle were determined and showed 12 differences from the recently published sequence of the rat liver enzyme deduced from the cDNA (95% identity).
Mann DJ, Bailey E, 1991, Pre-translational control of hepatic malic enzyme expression during the development of the rat., Biochem J, Vol: 279 ( Pt 2), Pages: 407-412, ISSN: 0264-6021
The expression of hepatic cytosolic malic enzyme in the developing rat has been studied by molecular-biological techniques. Malic enzyme mRNA was barely detectable throughout the neonatal period, but increased to significant levels immediately before weaning. Northern-blot analysis demonstrated that the two major malic enzyme mRNA species displayed non-co-ordinate control during development, with the 2.0 kb form accumulating to a greater extent than the 3.1 kb form. A novel 1.6 kb mRNA species was found to predominate in foetal samples. Tri-iodothyronine treatment of neonatal rats caused premature induction of all three malic enzyme mRNA species. Dietary studies also showed precocious induction of the mRNA with diets high in carbohydrate, but not with those high in fat.
Cohen PT, Brewis ND, Hughes V, et al., 1990, Protein serine/threonine phosphatases; an expanding family., FEBS Lett, Vol: 268, Pages: 355-359, ISSN: 0014-5793
Five protein serine/threonine phosphatases (PP) have been identified by cloning cDNA from mammalian and Drosophila libraries. These novel enzymes, which have not yet been detected by the techniques of protein chemistry and enzymology, are termed PPV, PP2Bw, PPX, PPY and PPZ. The complete amino acid sequences of PPX, PPY and PPZ and an almost complete sequence of PPV are presented. In the catalytic domain PPV and PPX are more similar to PP2A (57-69% identity) than PP1 (45-49% identity), while PPY and PPZ are more similar to PP1 (66-68% identity) than PP2A (44% identity). The cDNA for PP2Bw encodes a novel Ca2+/calmodulin-dependent protein phosphatase only 62% identical to PP2B in the catalytic domain. Approaches for determining the cellular functions of these protein phosphatases are discussed.
Mann D, Bartley W, Bailey E, 1990, Regulation of hepatic malic enzyme mRNAs during development., Biochem Soc Trans, Vol: 18, Pages: 652-653, ISSN: 0300-5127
Mann D, Bartley W, Strain AJ, et al., 1990, Regulation of malic enzyme expression in hepatocytes in culture., Biochem Soc Trans, Vol: 18, ISSN: 0300-5127
Ho KK, Mann DJ, The Role of Nuclear PtdIns(4,5)P2 turnover in Mammalian Cell Cycle, Gordon Research Conference on Signal Transduction Within the Nucleus
Mann DJ, Jones NC, Use of cdk-specific inhibitors to analyse the G1/S transition in mammalian cells, DNA Tumour Viruses
Child ES, Mann DJ, Role of the cyclin encoded by human Herpesvirus 8 in the deregulation of the cell cycle, UK Molecular Biology and Cancer Network meeting
Mann DJ, Cohen PTW, Identification of a novel Drosophila protein phosphatase, PPV, EMBO-FEBS meeting on Protein Phosphatases
Mann DJ, Cohen PTW, Protein serine/threonine phosphatase V, the D. melanogaster homologue of S. cerevisiae SIT4, FASEB meeting on Protein Phosphatases
Mann DJ, Jones NC, E2F-1 but not E2F-4 can overcome p16-induced cell cycle arrest., Cold Spring Harbor meeting on The Cell Cycle
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