Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Miriam M. Ziegler"'
Autor:
Frank M. Raushel, James F. Sinclair, Andrew J. Fisher, Thomas O. Baldwin, Jon A. Christopher, Miriam M. Ziegler, Ivan Rayment
Publikováno v:
Current Opinion in Structural Biology. 5:798-809
The generation of light by living organisms such as fireflies, glow-worms, mushrooms, fish, or bacteria growing on decaying materials has been a subject of fascination throughout the ages, partly because it occurs without the need for high temperatur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0967d83c2cdbd4a65ce014b06beb3914
https://doi.org/10.1016/0959-440x(95)80014-x
https://doi.org/10.1016/0959-440x(95)80014-x
Publikováno v:
Journal of Biological Chemistry. 268:10760-10765
Conditions have been established that allow reversible refolding of luciferase from 5 M urea. The kinetics of formation of the active enzyme showed a concentration-independent lag, suggesting the existence of intermediate structures on the pathway of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::51273059261bdb3a3352a1a6f34e8012
https://doi.org/10.1016/s0021-9258(18)82050-6
https://doi.org/10.1016/s0021-9258(18)82050-6
Publikováno v:
Journal of Biological Chemistry. 268:10766-10772
Bacterial luciferase is an alpha beta heterodimer with a single active center in which the reaction of reduced FMN, O2, and an aliphatic aldehyde yields a photon of blue-green light. We have shown that refolding of the luciferase subunits from 5 M ur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2779ca4f84c35effab7b15212ec0373d
https://doi.org/10.1016/s0021-9258(18)82051-8
https://doi.org/10.1016/s0021-9258(18)82051-8
Publikováno v:
Biochemistry. 36(7)
The kinetic mechanism in vitro of the folding and assembly of the heterodimeric flavin monooxygenase bacterial luciferase has been defined by a unique set of rate constants which describe both the productive refolding pathway and competing off-pathwa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45cca831ac9c32c1fa2290f823316ad3
https://pubmed.ncbi.nlm.nih.gov/9048575
https://pubmed.ncbi.nlm.nih.gov/9048575
Publikováno v:
Nature structural biology. 1(5)
The prevailing view in the field of protein folding holds that the native state is the most stable structure possible. A corollary of this thermodynamic hypothesis is that the native state is in equilibrium with all other conformations of the protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99a8c5aeb11517dee43d2e432ccd9364
https://pubmed.ncbi.nlm.nih.gov/7664038
https://pubmed.ncbi.nlm.nih.gov/7664038
Publikováno v:
Biochemistry. 24:3942-3947
Ziegler-Nicoli et al. [Ziegler-Nicoli, M., Meighen, E. A., & Hastings, J. W. (1974) J. Biol. Chem. 249, 2385-2392] reported that a highly reactive cysteinyl residue on the alpha subunit of bacterial luciferase resides in or near the flavin binding si
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd0a9fad6c46b25d6789572dc2feff26
https://doi.org/10.1021/bi00336a021
https://doi.org/10.1021/bi00336a021
Publikováno v:
Developmental Biology. 25:209-231
The cytoplasmic or nuclear origin of newly synthesized RNA has been investigated during early embryogenesis of Lytechinus variegatus . A large fraction of labeled high molecular weight RNA was recovered in an EDTA- and RNase-resistant form from the c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0e0f2784e83ae0608d2d1e332d3dff82
https://doi.org/10.1016/0012-1606(71)90028-5
https://doi.org/10.1016/0012-1606(71)90028-5
Autor:
Miriam M. Ziegler, Thomas O. Baldwin
Since the publication of Bioluminescence and Chemiluminescence, Part B, genes have been cloned that encode luciferases from an array of bioluminescent organisms, novel applications of these genes have been developed, and much has been learned of the
