Search Results - "Nicholas R. Helps" :: K.UTB vyhledávací portál | TBU Library Retrieval Portal

Phylogeny-wide analysis of social amoeba genomes highlights ancient origins for complex intercellular communication

Phylogeny-wide analysis of social amoeba genomes highlights ancient origins for complex intercellular communication

by Heidel, Andrew J, Lawal, Hajara M, Felder, Marius, Schilde, Christina, Helps, Nicholas R, Tunggal, Budi, Rivero, Francisco, John, Uwe, Schleicher, Michael, Eichinger, Ludwig, Platzer, Matthias, Noegel, Angelika A, Schaap, Pauline, Glöckner, Gernot
Published in Genome research (01.11.2011)

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SARP, a new alternatively spliced protein phosphatase 1 and DNA interacting protein

SARP, a new alternatively spliced protein phosphatase 1 and DNA interacting protein

by Browne, Gareth J, Fardilha, Margarida, Oxenham, Senga K, Wu, Wenjuan, Helps, Nicholas R, da Cruz E Silva, Odete A B, Cohen, Patricia T W, da Cruz E Silva, Edgar F
Published in Biochemical journal (15.02.2007)

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NIMA-related kinase 2 (Nek2), a cell-cycle-regulated protein kinase localized to centrosomes, is complexed to protein phosphatase 1

NIMA-related kinase 2 (Nek2), a cell-cycle-regulated protein kinase localized to centrosomes, is complexed to protein phosphatase 1

by HELPS, Nicholas R., LUO, Xinmei, BARKER, Hazel M., COHEN, Patricia T. W.
Published in Biochemical journal (15.07.2000)

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Cellular Mechanisms Regulating Protein Phosphatase-1

Cellular Mechanisms Regulating Protein Phosphatase-1

by Connor, John H., Frederick, Deborah, Huang, Hsien-bin, Yang, Jie, Helps, Nicholas R., Cohen, Patricia T.W., Nairn, Angus C., DePaoli-Roach, Anna, Tatchell, Kelly, Shenolikar, Shirish
Published in The Journal of biological chemistry (23.06.2000)

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5′‐AMP inhibits dephosphorylation, as well as promoting phosphorylation, of the AMP‐activated protein kinase. Studies using bacterially expressed human protein phosphatase‐2Cα and native bovine protein phosphatase‐2Ac

5′‐AMP inhibits dephosphorylation, as well as promoting phosphorylation, of the AMP‐activated protein kinase. Studies using bacterially expressed human protein phosphatase‐2Cα and native bovine protein phosphatase‐2Ac

by Davies, S P, Helps, N R, Cohen, P T, Hardie, D G
Published in FEBS letters (27.12.1995)

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NIMA-related kinase 2 (Nek2), a cell-cycle-regulated protein kinase localized to centrosomes, is complexed to protein phosphatase 1

NIMA-related kinase 2 (Nek2), a cell-cycle-regulated protein kinase localized to centrosomes, is complexed to protein phosphatase 1

by Helps, N R, Luo, X, Barker, H M, Cohen, P T
Published in Biochemical journal (15.07.2000)

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Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 A resolution

Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 A resolution

by Das, A. K., Helps, N. R., Cohen, P. T., Barford, D.
Published in The EMBO journal (16.12.1996)

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Protein phosphatase 1 interacts with p53BP2, a protein which binds to the tumour suppressor p53

Protein phosphatase 1 interacts with p53BP2, a protein which binds to the tumour suppressor p53

by Helps, Nicholas R., Barker, Hazel M., Elledge, Stephen J., Cohen, Patricia T.W.
Published in FEBS letters (27.12.1995)

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Protein phosphatase 4 is an essential enzyme required for organisation of microtubules at centrosomes in Drosophila embryos

Protein phosphatase 4 is an essential enzyme required for organisation of microtubules at centrosomes in Drosophila embryos

by Helps, N.R, Brewis, N.D, Lineruth, K, Davis, T, Kaiser, K, Cohen, P.T.W
Published in Journal of cell science (01.05.1998)

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Cellular mechanisms regulating protein phosphatase-1. A key functional interaction between inhibitor-2 and the type 1 protein phosphatase catalytic subunit

Cellular mechanisms regulating protein phosphatase-1. A key functional interaction between inhibitor-2 and the type 1 protein phosphatase catalytic subunit

by Connor, J H, Frederick, D, Huang, H b, Yang, J, Helps, N R, Cohen, P T, Nairn, A C, DePaoli-Roach, A, Tatchell, K, Shenolikar, S
Published in The Journal of biological chemistry (23.06.2000)

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Drosophila melanogaster protein phosphatase inhibitor-2: identification of a site important for PP1 inhibition

Drosophila melanogaster protein phosphatase inhibitor-2: identification of a site important for PP1 inhibition

by Helps, Nicholas R., Cohen, Patricia T.W.
Published in FEBS letters (10.12.1999)

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Interaction with Protein Phosphatase 1 Is Essential for bifocal Function during the Morphogenesis of theDrosophila Compound Eye

Interaction with Protein Phosphatase 1 Is Essential for bifocal Function during the Morphogenesis of theDrosophila Compound Eye

by Nicholas R. Helps, Patricia T. W. Cohen, Sami M. Bahri, William Chia, Kavita Babu
Published in Molecular and Cellular Biology (15.03.2001)

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Interaction with Protein Phosphatase 1 Is Essential for bifocal Function during the Morphogenesis of the Drosophila Compound Eye

Interaction with Protein Phosphatase 1 Is Essential for bifocal Function during the Morphogenesis of the Drosophila Compound Eye

by Helps, Nicholas R., Cohen, Patricia T. W., Bahri, Sami M., Chia, William, Babu, Kavita
Published in Molecular and cellular biology (01.03.2001)

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Characterisation of a novel Drosophila melanogaster testis specific PP1 inhibitor related to mammalian inhibitor-2: identification of the site of interaction with PP1

Characterisation of a novel Drosophila melanogaster testis specific PP1 inhibitor related to mammalian inhibitor-2: identification of the site of interaction with PP1

by Helps, Nicholas R., Vergidou, Cornillia, Gaskell, Terri, Cohen, Patricia T.W.
Published in FEBS letters (30.10.1998)

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Cloning of the complete coding region for human protein phosphatase inhibitor 2 using the two hybrid system and expression of inhibitor 2 in E. coli

Cloning of the complete coding region for human protein phosphatase inhibitor 2 using the two hybrid system and expression of inhibitor 2 in E. coli

by Helps, Nicholas R., Street, Alasdair J., Elledge, Stephen J., Cohen, Patricia T.W.
Published in FEBS letters (28.02.1994)

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5′-AMP inhibits dephosphorylation, as well as promoting phosphorylation, of the AMP-activated protein kinase. Studies using bacterially expressed human protein phosphatase-2C α and native bovine protein phosphatase-2A c

5′-AMP inhibits dephosphorylation, as well as promoting phosphorylation, of the AMP-activated protein kinase. Studies using bacterially expressed human protein phosphatase-2C α and native bovine protein phosphatase-2A c

by Davies, Stephen P., Helps, Nicholas R., Cohen, Patricia T.W., Hardie, D. Grahame
Published in FEBS letters (27.12.1995)

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