1698-80-2Relevant articles and documents
Phenothiazine-based CaaX competitive inhibitors of human farnesyltransferase bearing a cysteine, methionine, serine or valine moiety as a new family of antitumoral compounds
Dumitriu, Gina-Mirabela,B?cu, Elena,Belei, Dalila,Rigo, Beno?t,Dubois, Jo?lle,Farce, Amaury,Ghinet, Alina
, p. 4447 - 4452 (2015)
A new family of CaaX competitive inhibitors of human farnesyltransferase based on phenothiazine and carbazole skeleton bearing a l-cysteine, l-methionine, l-serine or l-valine moiety was designed, synthesized and biologically evaluated. Phenothiazine derivatives proved to be more active than carbazole-based compounds. Phenothiazine 1b with cysteine residue was the most promising inhibitor of human farnesyltransferase in the current study.
Synthesis and analgesic evaluation of some 5-[β-(10-phenothiazinyl) ethyl]-1-(acyl)-1,2,3,4-tetrazoles
Rajasekaran,Thampi
, p. 273 - 279 (2004)
A series of novel 5[β-(phenothiazinyl-10-yl)ethyl]-1-(acyl)-1,2,3,4- tetrazoles (3-14) have been synthesized via condensation of 5-[β- (phenothiazinyl-10-yl)ethyl]-1-2,3,4-tetrazole (2) with various acylating/sulphonating reagents. 5-[β-(phenothiazinyl-10
Electrical communication between glucose oxidase and electrodes mediated by phenothiazine-labeled poly(ethylene oxide) bonded to lysine residues on the enzyme surface
Ban, Kazumichi,Ueki, Takeshi,Tamada, Yoshinori,Saito, Takahiro,Imabayashi, Shin-ichiro,Watanabe, Masayoshi
, p. 910 - 917 (2003)
A series of glucose oxidase (GOx) hybrids (GOx-phenothiazine-labeled poly(ethylene oxide) (PT-PEO)) capable of direct electrical communication with electrodes is synthesized by covalently modifying PT-PEO to lysine residues on the enzyme surface. The length of the PEO chain and the number of PT groups are systematically altered. After the PT-PEO modification, all the hybrids maintain more than 50% of enzyme activity relative to that of native GOx, although loss of the activity becomes greater with increasing PEO chain length. The catalytic current, icat, is observed at a potential more positive than 0.55 V after the addition of glucose, due to the intramolecular electron transfer (ET) from reduced forms of flavin adenine dinucletide (FADH2/FADH) to PT+ that are electrogenerated at the electrode. The icat value increases with the number of PT groups, indicating that most of the modified PT groups act as mediators. The magnitude of the icat increase depends on the PEO chain length and reveals a maximum for PT-PEO with the molecular weight of 3000. In contrast, the icat is almost constant for GOx-2-(10-phenothiazyl)propionic acid (PT-PA) hybrids with more than two PT groups synthesized by covalently modifying PT-PA to surface lysines, indicating that only a few key PT groups function as mediators. The maximum rate constant (130 s-1) for the ET from FADH2/FADH to PT+ is obtained for the GOx hybrid modified with five PT-PEO groups with the molecular weight of 3000.
Synthesis and bio-evaluation of phenothiazine derivatives as new anti-tuberculosis agents
He, Chun-Xian,Meng, Hui,Zhang, Xiang,Cui, Hua-Qing,Yin, Da-Li
, p. 951 - 954 (2015)
Abstract Two series of phenothiazine derivatives were designed and synthesized. All compounds were tested for anti-tuberculosis activities against Mycobacterium tuberculosis H37RV. In comparison with mother compound of chlorpromazine, compound 6e shows promising anti-tuberculosis activity and much less mammalian cell cytotoxicity, compound 6e merits to be further explored as new anti-tuberculosis agents.
Electrochemical primer extension for the detection of single nucleotide polymorphisms in the cardiomyopathy associated MYH7 gene
Debela,Thorimbert,Hasenknopf,O'Sullivan,Ortiz
supporting information, p. 757 - 759 (2016/01/12)
We report the labelling of dideoxy nucleotides (ddNTPs) for use in electrochemical array based primer extension for the detection of single nucleotide polymorphisms (SNPs). The results confirm the extension of the immobilised primers for each of the four ddNTPs, representing a significant advance in achieving a cost-effective platform for screening of disease-specific SNPs.
