Results 91 to 100 of about 3,569 (120)

MacroD1 sustains mitochondrial integrity and oxidative metabolism. [PDF]

Nat Commun
Hopp AK, Ferretti LP, Schlicker L, Ruiz-Serrano A, Hetzel U, Prisco F, Kipar A, Muskalla L, Ferrari E, Scholz CC, Hiller K, Verdeguer F, Leslie Pedrioli DM, Hottiger MO.   +13 more
europepmc   +1 more source

ADP-ribosyltransferase-based biocatalysis of nonhydrolyzable NAD+ analogs. [PDF]

J Biol Chem
Sakari M, Bhadane R, Kumar S, Azevedo R, Malakoutikhah M, Masoumi A, Littler DR, Härmä H, Kopra K, Pulliainen AT.   +9 more
europepmc   +1 more source

NAD + metabolism and function in innate and adaptive immune cells. [PDF]

J Inflamm (Lond)
Mann R, Stavrou V, Dimeloe S.
europepmc   +1 more source

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ADP-Ribosylation of Neurofilaments by a Cytoplasmic ADP-Ribose Transferase Associated with Free mRNP

Biochemical and Biophysical Research Communications, 1993
ADP-ribosylation of neurofilaments by an ADP-ribose transferase isolated from cytoplasmic ribonucleoprotein particles is demonstrated. The 150 kDa neurofilament subunit appears to be the main ADP-ribose acceptor with the transfer of ADP-ribose dimers or monomers.
M, Jesser, F, Hog, C, Chypre, J F, Leterrier, P, Mandel   +4 more
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Intrinsic ADP-Ribose Transferase Activity versus Levels of Mono(ADP-Ribose)Protein Conjugates in Proliferating Ehrlich Ascites Tumor Cells

Hoppe-Seyler´s Zeitschrift für physiologische Chemie, 1979
Transition of proliferating Ehrlich ascites tumor cells (3 days after transplantation) to the non-proliferating status (8--14 days after transplantation) was associated with an increase in total mono (ADP-ribose) protein conjugates. This increase was largely confined to the NH2OH-resistant subfraction.
Bredehorst, R, Goebel, M, Renzi, F, Kittler, M, Klapproth, A, Hilz, H   +5 more
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Poly(ADP-Ribose) Transferase in Lizard Oviduct

1989
Poly(ADP-ribose) transferase often undergoes a drastic change in its activity following the action of various biological effectors in a variety of cell systems or tissues. An increase in poly(ADP-ribose) transferase activity was usually observed in those systems in which the biological effectors were followed with cell proliferation, for instance, in ...
Gaetano Ciarcia, Hisanori Suzuki, Massimo Lancieri   +2 more
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Loss of poly(ADP-ribose) synthetase activity without change in arginine-specific ADP-ribosyltransferase activity by acid-treatment; application of the treatment to simple assay for transferase in the presence of poly(ADP-ribose) synthetase

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1993
We investigated the effects of acid treatment (pH 3.5) on the activities of arginine-specific ADP-ribosyltransferase (mono(ADP-ribosyl)transferase) (EC 2.4.2.31) and poly(ADP-ribose) synthetase (EC 2.4.2.30) purified from chicken liver, and we observed that the former enzyme retained completely its activity while there was no evidence for activity of ...
S, Doi, Y, Tanigawa, M, Tsuchiya, M, Shimoyama   +3 more
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Ecto-ADP-ribose Transferases: Cell-Surface Response to Local Tissue Injury

Physiology, 2005
Ecto-ADP-ribose transferases (ecto-ARTs) catalyze the transfer of ADP-ribose from NAD+to arginine residues in cell-surface proteins. Since the concentration of extracellular NAD+is very low under normal physiological conditions but rises significantly upon tissue injury or membrane stress, it is postulated that the main role of ecto-ARTs is to ADP ...
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Differential radiosensitization by the poly(ADP-ribose) transferase inhibitor 3-aminobenzamide in human tumor cells of varying radiosensitivity

International Journal of Radiation Oncology*Biology*Physics, 1988
Four newly-established human tumor cell lines, have been irradiated at dose rates of 150 and 3.2 cGy/min to compare their capacity to repair radiation damage. They included a neuroblastoma, a germ-cell carcinoma of the testis, a large cell carcinoma of the lung, and a carcinoma of the cervix. The four lines varied in their sensitivity to high dose-rate
L R, Kelland, L, Burgess, G G, Steel
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