Search results for "Phosphorylation"

Post-Translational Regulation of Fas/CD95 in Cell Death and Survival: Role of Nitric Oxide

2010

Electrochemical Oxidative C – C Bond Formation

2021

Oxidative damages in cho-k1 cells treated with beauvericin

2013

Light Regulation of the Thylakoid LHCII Protein Phosphorylation at the Substrate Level

1998

The distribution of light energy between the two photosystems as well as the light-induced turnover of PSII proteins are regulated by the reversible phosphorylation of LHCII and the PSII-core proteins. The thylakoid protein kinase(s) is activated by a signal transduction system involving the interaction of reduced plastoquinone with the quinol oxidation site of the cytochrome bf complex [1]. Phosphorylation of the mobile pool of LHCII induces dissociation of this antenna from PSII and allows its interaction with the PSI in the stroma exposed membranes (state transition)[21. Dephosphorylation of LHCII by a membrane -bound phosphatase appears to be regulated by a cyclophilinlike protein locat…

Correlative Analysis of the Photosynthetic Capacity and Different Components of the Photosynthetic Apparatus

1984

The majority of higher plants is able to adapt to the ecological factor light in a wide range. Depending on the light intensity and the light quality during growth, plant with an equal genotype develop into so-called low light and high light forms. The photosynthetic adaptation to different light conditions involves complex, balanced changes of many leaf features. The changes of physiological factors of photosynthesis includes differences in the CO2 conductance, in the Calvin cycle enzymes, the capacity of electron transport, the photophosphorylation and the pigments (Boardman, 1977; Wild, 1979; Bjorkman, 1981; Lichtenthaler et al., 1981). The adaptation of individual plants or leaves to lo…

ChemInform Abstract: Aryl Radicals by Copper(II) Oxidation of Hydrazines: A New Method for the Oxidative and Reductive Arylation of Alkenes.

1990

Abstract A new source of aryl radicals interesting from the preparative point of view has been found in the reaction of arylhydrazines and copper(II) sulfate. The process allows selectively both the reductive and oxidative arylation of alkenes.

Oxidative halogenation of substituted pyrroles with cu(II). Part I. Bromination of some 3-acetylpyrroles

1990

3-Acetylpyrroles are brominated with copper(II) bromide. The reaction afforded almost quantitatively only nuclear monobromination. Evidence for the structures of final compounds was by mass spectrometry, 1 H-nuclear magnetic resonance, ir, and elemental analysis

Oxidative halogenation of substituted pyrroles with cu(II). Part II. Bromination of some ethyl 3-pyrrolecarboxylates and corresponding acids

1990

Ethyl 3-pyrrolecarboxylates and their corresponding acids are brominated with copper(II) bromide. The reaction afforded at 0°, with high-yield nuclear monobromination.

Aryl radicals by copper(II) oxidation of hydrazines: A new method for the oxidative and reductive arylation of alkenes

1989

Abstract A new source of aryl radicals interesting from the preparative point of view has been found in the reaction of arylhydrazines and copper(II) sulfate. The process allows selectively both the reductive and oxidative arylation of alkenes.

Phosphorylation of mismatch repair proteins MSH2 and MSH6 affecting MutSα mismatch-binding activity

2002

Mismatch repair (MMR) is involved in the removal of mispaired bases from DNA and thus plays an important role in the maintenance of genomic stability and the prevention of mutations and cancer. Moreover, MMR triggers genotoxicity and apoptosis upon processing of DNA lesions such as O6-methylguanine. Whereas the enzymology of MMR has been elucidated in great detail, only limited data are available concerning its regulation. Here we show that the major mismatch-binding proteins MSH2 and MSH6, forming the MutSalpha complex, are phosphorylated in vitro by protein kinase C and casein kinase II, but not by protein kinase A. Phosphorylation of MSH2 and MSH6 was also found within the cell, with MSH…