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Reversible covalent modification of DNA

Archives of Biochemistry and Biophysics, 1974
The reaction of bromomethylbenzoyl esters of choline and dimethylaminoethanol with DNA and model compounds led predominantly to phosphotriester formation. In model compounds the phosphotriester formation was verified by uv spectrometry. The bromomethylbenzoyl cationic esters reacted with DNA at room temperature at neutral pH values.
R N, Gohil, A C, Roth, R A, Day
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Covalent Surface Modification of Oxide Surfaces

Angewandte Chemie - International Edition, 2014
AbstractThe modification of surfaces by the deposition of a robust overlayer provides an excellent handle with which to tune the properties of a bulk substrate to those of interest. Such control over the surface properties becomes increasingly important with the continuing efforts at down‐sizing the active components in optoelectronic devices, and the ...
Han Zuilhof   +2 more
exaly   +4 more sources

Covalent modifications of aminophospholipids by 4-hydroxynonenal

Free Radical Biology and Medicine, 1998
Lipid oxidation is implicated in a wide range of pathophysiological disorders, which leads to reactive compounds such as aldehydes. Among them 4-hydroxynonenal (4-HNE) reacts strongly with the NH2 groups of amino acids and forms mainly Michael adducts and minor Schiff-base adducts. Such reactions occur also with compounds containing thiol groups.
M, Guichardant   +3 more
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Regulated covalent modifications of lipid A

Journal of Endotoxin Research, 2001
Regulated covalent modifications of lipid A are implicated in virulence of pathogenic Gram-negative bacteria. The Salmonella PhoP/PhoQ-activated gene pagP is required for resistance to cationic antimicrobial peptides and for biosynthesis of hepta-acylated lipid A species containing palmitate.
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Regulation by Covalent Modification

2009
The preceding chapter showed that the regulation of enzymatic activity can be carried out through a variety of mechanisms. Regulation involving covalent processes is even more diverse. These processes include various co- and post-translational events such as limited proteolysis and various chemical modifications (glycosylation, carboxylation, ADP ...
Jeannine Yon-Kahn, Guy Hervé
openaire   +1 more source

Posttranslational Covalent Modification of Proteins

Science, 1977
A search for derivatized amino acids in proteins has shown that the extent of posttranslational modification of proteins is quite substantial. While only 20 primary amino acids are specified in the genetic code and are involved as monomer building blocks in the assembly of the polypeptide chain, about 140 amino acids and amino acid derivatives have ...
Rosa Uy, Finn Wold
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Covalent modification of PTPases

1998
Abstract The large, transmembrane PTPases have been shown in several cases to undergo proteolytic processing of a proprotein that produces protein subunits, including LAR, RPTP-k and RPTP-σ. The site and determinants of LAR proprotein cleavage have recently been evaluated [105, 110, 116].
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Covalent Modification of G Proteins by Affinity Labeling

2003
The activation of heterotrimeric G-proteins is tightly regulated by the exchange of GTP for GDP in the alpha-subunit; mostly--but not exclusively--seven-transmembrane receptors function as the guanine nucleotide exchange factors (GEFs). A research goal may be to determine which G-protein alpha-subunit is activated by the receptor under investigation ...
Martin, Hohenegger   +2 more
openaire   +3 more sources

Advances of Covalent Chemical Modifications of RNA

Chemistry – A European Journal
ABSTRACT Chemical modification of RNA can endow RNA molecules with novel structures and functions, enabling broader clinical application potential. RNA chemical modification is a systematic and controllable engineering approach, particularly at the cellular or tissue level, requiring precise modification strategies to reduce off ...
Yong Li   +7 more
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Non-covalent and covalent modifications modulate the reactivity of monomeric mammalian globins

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2013
Multimeric globins (e.g., hemoglobin) are considered to be the prototypes of allosteric enzymes, whereas monomeric globins (e.g., myoglobin; Mb) usually are assumed to be non-allosteric. However, the modulation of the functional properties of monomeric globins by non-covalent (or allosteric) and covalent modifications casts doubts on this general ...
Ascenzi, P   +10 more
openaire   +4 more sources

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