Results 341 to 350 of about 205,153 (377)

Isomerization-Controlled Dephosphorylation

Science Signaling, 2000
The protein Pin1 is a peptidyl-prolyl cis/trans isomerase and is thought to function in control of mitosis. The enzyme specifically acts on phosphorylated Ser- or Thr-Pro bonds, and such phosphporylated motifs occur in various signaling pathways that control cell division and other functions. Zhou et al.
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Enzymatic Dephosphorylation of Adenosine Tetraphosphate

Nature, 1961
ADENOSINE tetraphosphate was discovered as an impurity in some commercial preparations of adenosine triphosphate1,2 where its concentration may exceed 10 per cent of the total adenine3. It was also found in horse muscle4 and possibly in rat liver5.
C, LIEBECQ, K, JAROSZEWICZ, A, LALLEMAND
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Protein phosphatase 1 dephosphorylates Orc2

Biochemical and Biophysical Research Communications, 2014
Phosphorylation of Thr(116) and Thr(226) on Orc2, one of the six subunits of the origin recognition complex (ORC), by cyclin A/CDK2 during S phase leads to the dissociation of Orc2, Orc3, Orc4, and Orc5 subunits (Orc2-5) from human chromatin and replication origins. The phosphorylated Orc2 becomes dephosphorylated in the late M phase of the cell cycle.
Kyung Yong, Lee, June Sung, Bae, Gwang Su, Kim, Deog Su, Hwang   +3 more
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Isomer-Specific Dephosphorylation

Science, 2000
STKE The protein Pin1 is an isomerase that catalyzes interconversion of cis and trans forms of proline in polypeptides and is thought to function in signaling pathways that control cell division. Zhou et al . propose a mechanism by which Pin1 might influence signaling through such pathways.
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Phosphorylation-dephosphorylation of apolipoprotein B

1986
Publisher Summary There is little doubt of the physiologic importance of apolipoprotein B (apoB). In addition to being essential for the secretion of very low-density lipoprotein (VLDL), apoB plays a fundamental role in targeting cholesterol, as a component of LDL, to tissues via specific high-affinity receptors.
R A, Davis, R A, Borchardt
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Enzymatic dephosphorylation of triphosphopyridine nucleotide

Archives of Biochemistry and Biophysics, 1952
Summary o 1. An enzyme preparation which hydrolyzes TPN to DPN and inorganic phosphate has been purified from pig kidney by ammonium sulfate fractionation and trypsin digestion. 2. The enzyme activity is optimal at pH 9.5 and it is activated by Mg ++ and to a lesser extent by Mn ++ and Ca ++ .
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An Unusual Dephosphorylation Reaction

Nucleosides, Nucleotides and Nucleic Acids, 1989
Abstract In the course of our work to prepare l1, Z2-seco-nucleotides, an unusual dephosphorylation reaction took place. When compound 1 was subjected to transfer hydrogenation conditions, the expected product was not obtained. Instead, a crystalline solid that proved not to have phosphorus was isolated in 78% yield.
Anne Cichy, Purushotham Vemishetti, Elie Abushanab   +2 more
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Enzymic Dephosphorylation of Cozymase

Nature, 1938
FOLLOWING the observations1,2,3 that cozymase is inactivated by vegetable as well as animal tissues it was considered to be of interest to study the mechanism of inactivation. Euler, Adler, Gunther and Hellstrom4 found that cozymase was inactivated by dialysed muscle extract, but that the latter was active in glycolysis only when cozymase and adenylic ...
N. B. DAS, H. V. EULER
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Protein Dephosphorylation and Protein Phosphorylation

2002
The phosphorylation of proteins, at serine, threonine or tyrosine residues, serves multiple roles in the regulation of cell function. However, dephosphorylation is as important as phosphorylation, and it follows that the phosphoprotein phosphatases are integral components of the signaling systems operated by protein kinases.
Bastien D. Gomperts, Ijsbrand M. Kramer, Peter E.R. Tatham   +2 more
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Dephosphorylation to Die For

Science Signaling, 2010
Induction of apoptosis requires dephosphorylation of a regulatory protein in the mitochondrial outer membrane.
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