Disease relevance of NSC92512

• Reversible modification of Escherichia coli ribosomes with 2,3-dimethylmaleic anhydride. A new method to obtain protein-deficient ribosomal particles [1].
• Solubilization of membrane-bound transpeptidase from Streptomyces strain K-11 with 2,3-dimethylmaleic anhydride [2].

High impact information on NSC92512

• The synthesis of DIVEMA-TNF-alpha could be controlled by the addition of 2,3-dimethylmaleic anhydride (DMMAn), which binds to or separates from amino groups when the pH is changed [3].
• These multimers could be disaggregated by sulfhydryl reagents and by dimethylmaleic anhydride, and treatment of high density ECM by these reagents prevented the induction of endocytosis [4].
• Modification of yeast ribosomes with dimethylmaleic anhydride, a reagent for protein amino groups, is accompanied by loss of polypeptide-synthesizing activity [5].
• Biological activity in both types of antisera was mediated by immunoglobulin binding to one or more intrinsic proteins of the adipocyte plasma membrane since fat cells were unresponsive to all antisera absorbed with dimethylmaleic anhydride-extracted membranes [6].
• Immunodiffusion experiments performed in agarose containing Triton X-100 (0.1%) revealed a precipitin reaction between anti-membrane serum and the detergent-solubilized proteins from either intact adipocyte plasma membranes or membranes extracted with dimethylmaleic anhydride [7].

Biological context of NSC92512

• The electrophoretic pattern of DMA-treated serum was changed only with concentrations of DMA many times that affecting cell aggregation or mobility [8].
• Partial acylation of 1 with 1.3 equiv of 2,3-dimethylmaleic anhydride followed by complete acetylation with acetic anhydride produces a mixture consisting largely of mono- and bis(dimethylmaleyl)peracetyl-1 [9].

Anatomical context of NSC92512

• Plasma membrane vesicles from rat adipocytes were treated with dimethylmaleic anhydride to remove extrinsic proteins and then used to immunize rabbits [7].
• Modification of chromatin from chicken erythrocytes with dimethylmaleic anhydride is accompanied by its solubilization and the dissociation of histones H1, H5, H2A and H2B [10].
• Modification of calf thymus chromatin with the protein reagent dimethylmaleic anhydride is accompanied by dissociation of histones and non-histone proteins [11].

Associations of NSC92512 with other chemical compounds

• EXPERIMENTAL DESIGN: PVD was radically synthesized with vinylpyrrolidone and 2,3-dimethylmaleic anhydride, which is known to be a pH-reversible amino-protecting reagent [12].
• A pH-reversible amino-protective reagent, dimethylmaleic anhydride (DMMAn), was used for polymer conjugation of tumor necrosis factor-alpha (TNF-alpha) with polyethylene glycol (PEG) [13].
• The lethal activity of the toxin was also lost after treatment with 2,3-dimethylmaleic anhydride (DMA) or 2,4,6-trinitrobenzenesulfonic acid (TNBS) [14].
• The extensive modification of histone H1 from calf thymus with the amino-group reagent dimethylmaleic anhydride (over 35 lysine residues modified per molecule) produces no effect on its secondary structure detectable by circular dichroism (far UV) [15].
• Both control and insulin-activated D-glucose transport activities were retained by plasma membrane vesicles extracted with dimethylmaleic anhydride [16].

Gene context of NSC92512

• Insulin, acylated with dimethylmaleic anhydride, was conjugated to transferrin (Tf) via a disulfide linkage [17].
• Dissociation of proteins from Escherichia coli ribosomes after dimethylmaleic anhydride treatment. Effects of elongation factor G and antibiotics [18].
• The novel PEG-conjugated IL-6 (DmPEG-IL-6), which had been pretreated with DMMAn before PEGylation, showed up to a 140% increase in in vitro specific activity compared with PEG-IL-6 that had been synthesized by the previous method [19].

Analytical, diagnostic and therapeutic context of NSC92512

• In addition, cellulose acetate electrophoresis was carried out on samples of serum containing DMA, and the incorporation of 14C-amino acids into DMA-treated cells studied [8].
• The effect of reversible protection of the free amino groups of poly- and monoclonal antibodies by dimethylmaleic anhydride on their binding activity following immobilization onto various carriers was studied [20].

References