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pro vyhledávání: '"GroES Protein"'
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Publikováno v:
EMBO reports. 3(9)
The Escherichia coli chaperonin machine is composed of two members, GroEL and GroES. The GroEL chaperonin can bind 10-15% of E. coli's unfolded proteins in one of its central cavities and help them fold in cooperation with the GroES cochaperonin. Bot
Publikováno v:
Peptides ISBN: 9789401042956
Peptides
Peptides
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::44aaae9d9f85d7fb9e34d51f59108061
https://doi.org/10.1007/978-94-011-0683-2_253
https://doi.org/10.1007/978-94-011-0683-2_253
Autor:
Shinnick TM; Division of Bacterial Diseases, Centers for Disease Control, Atlanta, GA 30333., Plikaytis BB, Hyche AD, Van Landingham RM, Walker LL
Publikováno v:
Nucleic acids research [Nucleic Acids Res] 1989 Feb 11; Vol. 17 (3), pp. 1254.
Autor:
Takashi Higurashi, Kaoru Ichimura, Yuzuru Hiragi, Yasutaka Seki, Tomohiro Mizobata, Yasushi Kawata, Kunitsugu Soda
Publikováno v:
Journal of Molecular Biology. 333:605-620
The GroES protein from Escherichia coli is a well-known member of the molecular chaperones. GroES consists of seven identical 10 kDa subunits, and forms a dome-like oligomeric structure. In order to obtain information on the structural stability and
Autor:
Chiduru Matsumoto, Katsuaki Inoue, Mitsuyoshi Ikeda, Takashi Higurashi, Kunihiro Hongo, Yasushi Kawata, Isao Sakane, Tomohiro Mizobata
Publikováno v:
Journal of Molecular Biology. 344:1123-1133
Chaperonin 10 (cpn10) is a well-conserved subgroup of the molecular chaperone family. GroES, the cpn10 from Escherichia coli, is composed of seven 10kDa subunits, which form a dome-like oligomeric ring structure. From our previous studies, it was fou
Autor:
Cécile A. C. M. van Els, Martien C. M. Poelen, Rachel M. Stenger, Claire J. P. Boog, Ad P. J. M. de Jong, Hugo D. Meiring, Betsy Kuipers, Jacqueline A. M. van Gaans-van den Brink
Knowledge of naturally processed Bordetella pertussis -specific T cell epitopes may help to increase our understanding of the basis of cell-mediated immune mechanisms to control this reemerging pathogen. Here, we elucidate for the first time the domi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a5e737651b8cca46c2907b5789af93c
https://europepmc.org/articles/PMC4018886/
https://europepmc.org/articles/PMC4018886/
Autor:
John S. Philo, Matsujiro Ishibashi, Hiroko Tokunaga, Masao Tokunaga, Makoto Mizukami, Tsutomu Arakawa, Hiroaki Takagi, Yoichi Shiraishi, Ryoichi Tanaka, Masatake Odachi
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 65:1379-1387
The groESL locus of a protein-hypersecreting bacterium, Bacillus brevis, was cloned by PCR using primers designed based on the DNA sequence of a B. subtilis homolog. GroEL protein was purified to apparent homogeneity and its ATPase activity was chara
Publikováno v:
Journal of Biotechnology. 127:244-257
During production in recombinant Escherichia coli, the human basic fibroblast growth factor (hFGF-2) partly aggregates into stable cytoplasmic inclusion bodies. These inclusion bodies additionally contain significant amounts of the heat-shock chapero
Publikováno v:
FEMS microbiology letters. 227(1)
Primers designed on the basis of nucleotide sequences conserved in DnaK and GroEL from Gram-positive organisms were used to PCR amplify internal regions of the cognate genes from the anaerobic ruminal cellulolytic bacterium Ruminococcus flavefaciens