Zobrazeno 1 - 10
of 73
pro vyhledávání: '"GUNTHER L. EICHHORN"'
Publikováno v:
Biochemistry. 36:14794-14798
Standard preparations of Escherichia coli RNA polymerase harbor a 70 kDa protein with NTPase (beta-gamma cleavage) activity that is not a recognized polymerase subunit. The NTPase activity of this component, before and after separation from the polym
Autor:
Patricia Clark, Gunther L. Eichhorn
Publikováno v:
Journal of Inorganic Biochemistry. 59:765-772
When DNA is treated with Cu(II) and then heated, the melting temperature (Tm) of the DNA is dramatically decreased (8). The Cu(II) binds to the DNA in such a way as to destabilize the double helix and help to break the hydrogen bonds between the base
Autor:
Peter P. Chuknyisky, Richard B. Beal, Christopher P. Janzen, Carl Garland, Gunther L. Eichhorn, Patricia L. Clark, James J. Butzow, Edward Tarien
Publikováno v:
Proceedings of the National Academy of Sciences. 91:7613-7617
Distances between the metal ions bound to the product terminus i site and the substrate i + 1 site of Escherichia coli RNA polymerase range from 5.0 to 5.6 A when the substrate is complementary to a template base and from 6.5 to 7.0 A for a noncomple
Autor:
Gunther L. Eichhorn
Publikováno v:
Coordination Chemistry Reviews. 128:167-173
The structure of a metal complex may be determined by the structure of the ligand or by the electronic configuration of the metal. In the latter case, the metal can induce a conformational change in the ligand. Such a conformational change is a usual
Autor:
Gunther L. Eichhorn
Publikováno v:
ChemInform. 25
The structure of a metal complex may be determined by the structure of the ligand or by the electronic configuration of the metal. In the latter case, the metal can induce a conformational change in the ligand. Such a conformational change is a usual
Publikováno v:
Biochemistry. 30:6454-6464
Escherichia coli RNA polymerase (RNAP) exhibits a strong selectivity for the secondary structure of its template DNA, as shown by the influence both of the DNA conformation on the transcription cycle and of the enzyme on the DNA conformation itself.
Publikováno v:
Biochemistry. 29:5987-5994
The two substrates between which an internucleotide bond is formed in RNA synthesis occupy two subsites, i and i + 1, on the active site of Escherichia coli RNA polymerase, and each subsite is associated with a metal ion. These ions are therefore use
Autor:
Gunther L. Eichhorn, Edward Tarien, Ramadas Nirmala, Patricia Clark, Carl Garland, Joseph M. Rifkind
Publikováno v:
Biochemistry. 38(11)
A frequently used schematic model of transcriptional elongation shows an RNA polymerase molecule moving along a linear DNA. This model is of course highly idealized and not compatible with promoter sequences [Gralla, J. D. (1991) Cell 66, 415-418; Sc
Autor:
Gunther L. Eichhorn
Publikováno v:
Experimental gerontology. 28(4-5)
The controversial role of aluminum in Alzheimer's disease (AD) is reviewed. While current data would suggest the lack of a causative role, alterations in the brain and other organ systems caused by AD might increase the penetration of aluminum as wel
Autor:
Edward Tarien, Abraham Levy, Gunther L. Eichhorn, Rajasekharan P. Pillai, Peter P. Chuknyisky, Richard B. Beal
Publikováno v:
Biochemistry. 29(25)
Since a major function of RNA polymerase must be to bring together substrates in the optimal configuration for internucleotide bond formation, studies have been undertaken to understand the geometrical relationship of the two substrates. A model has