Results 171 to 180 of about 1,431 (214)
Some of the next articles are maybe not open access.
Covalent modification of DNA by daunorubicin
Cancer Chemotherapy and Pharmacology, 1993Daunorubicin, a clinically useful antitumor agent, induces mammary adenocarcinoma in Sprague-Dawley rats. As part of an investigation of the mechanism of tumor induction by daunorubicin, the formation of daunorubicin-DNA adducts has been investigated by 32P-postlabeling assay.
M, Purewal, J G, Liehr
openaire +2 more sources
The language of covalent histone modifications
Nature, 2000Histone proteins and the nucleosomes they form with DNA are the fundamental building blocks of eukaryotic chromatin. A diverse array of post-translational modifications that often occur on tail domains of these proteins has been well documented. Although the function of these highly conserved modifications has remained elusive, converging biochemical ...
B D, Strahl, C D, Allis
openaire +2 more sources
Reversible covalent modification of DNA
Archives of Biochemistry and Biophysics, 1974The 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
openaire +2 more sources
Regulated covalent modifications of lipid A
Journal of Endotoxin Research, 2001Regulated 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.
openaire +2 more sources
Covalent modifications of aminophospholipids by 4-hydroxynonenal
Free Radical Biology and Medicine, 1998Lipid 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
openaire +2 more sources
Regulation by Covalent Modification
2009The 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
Advances of Covalent Chemical Modifications of RNA
Chemistry – A European JournalABSTRACT 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
openaire +2 more sources
Posttranslational Covalent Modification of Proteins
Science, 1977A 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
openaire +1 more source
Covalent modification of PTPases
1998Abstract 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].
openaire +1 more source
Covalent Modification of G Proteins by Affinity Labeling
2003The 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