Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Rumit Maini"'
Autor:
Emiko Mihara, Satoshi Watanabe, Nasir K. Bashiruddin, Nozomi Nakamura, Kyoko Matoba, Yumi Sano, Rumit Maini, Yizhen Yin, Katsuya Sakai, Takao Arimori, Kunio Matsumoto, Hiroaki Suga, Junichi Takagi
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
RaPID (Random non-standard Peptides Integrated Discovery) enables discovery of small macrocyclic peptides binding desired targets. Here, the authors propose lasso-grafting: the RaPID-derived peptides are implanted onto diverse proteins and maintain b
Externí odkaz:
https://doaj.org/article/b6402a431ea3401381e2112d57500bf8
Autor:
Nozomi Nakamura, Satoshi Watanabe, Junichi Takagi, Kyoko Matoba, Yizhen Yin, Rumit Maini, Katsuya Sakai, Emiko Mihara, Hiroaki Suga, Kunio Matsumoto, Nasir K Bashiruddin, Takao Arimori, Yumi Sano
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Nature Communications
Nature Communications
Protein engineering has great potential for devising multifunctional recombinant proteins to serve as next-generation protein therapeutics, but it often requires drastic modifications of the parental protein scaffolds e.g., additional domains at the
Publikováno v:
Journal of the American Chemical Society. 141:20004-20008
It has been well established that the ribosome can accept various nucleophiles on the Xacyl-tRNA in the A site during elongation, where X can be amino, N-alkyl-amino, hydroxy, and thiol groups. How...
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 25:4715-4718
The synthesis and incorporation into position 66 of green fluorescent protein (GFP) by in vitro protein translation of novel oxazole and thiazole based dipeptidomimetics are described. The compounds may be regarded as GFP chromophore analogues, and a
Autor:
Shengxi Chen, Sidney M. Hecht, Rakesh Paul, Manikandadas M. Madathil, Sandipan Roy Chowdhury, Larisa M. Dedkova, Rumit Maini
Publikováno v:
Journal of the American Chemical Society. 137:11206-11209
Plasmids containing 23S rRNA randomized at positions 2057-2063 and 2502-2507 were introduced into Escherichia coli, affording a library of clones which produced modified ribosomes in addition to the pre-existing wild-type ribosomes. These clones were
Autor:
Ryan C. Nangreave, Rumit Maini, Sidney M. Hecht, Xiaoguang Bai, Larisa M. Dedkova, Shengxi Chen
Publikováno v:
Journal of the American Chemical Society. 139(40)
Phosphorylated proteins play important roles in the regulation of many different cell networks. However, unlike the preparation of proteins containing unmodiffed proteinogenic amino acids, which can be altered readily by site-directed mutagenesis and
Autor:
Dan T. Nguyen, Rumit Maini, Larisa M. Dedkova, Sandipan Roy Chowdhury, Sidney M. Hecht, Rafael Alcala-Torano, Shengxi Chen
Publikováno v:
Bioorganic & Medicinal Chemistry. 21:1088-1096
Ribosomes containing modifications in three regions of 23S rRNA, all of which are in proximity to the ribosomal peptidyltransferase center (PTC), were utilized previously as a source of S-30 preparations for in vitro protein biosynthesis experiments.
Publikováno v:
Current opinion in chemical biology. 34
Peptide natural products (PNPs) represent a unique class of compounds known for their fascinating structural motifs with important biological activities. Lately, PNPs have garnered a lot of interest for their application in drug discovery. Neverthele
Publikováno v:
Journal of Natural Products. 75:577-585
Structure-activity studies were employed to investigate the stabilization of DNA-topoisomerases I and II covalent binary complexes by topopyrone analogues. The synthesis of five new topopyrone derivatives and study of their ability to stabilize DNA-t
Autor:
Sandipan Roy Chowdhury, Rumit Maini, Sidney M. Hecht, Rakesh Paul, Shengxi Chen, Basab Roy, Sasha M. Daskalova, Larisa M. Dedkova
Publikováno v:
Biochemistry
In an earlier study, β³-puromycin was used for the selection of modified ribosomes, which were utilized for the incorporation of five different β-amino acids into Escherichia coli dihydrofolate reductase (DHFR). The selected ribosomes were able to