Zobrazeno 1 - 10
of 923
pro vyhledávání: '"A. H. Boxer"'
Autor:
Beckhart, Benjamin Haggott
Publikováno v:
The Journal of Finance, 1965 Sep 01. 20(3), 566-569.
Externí odkaz:
https://www.jstor.org/stable/2978033
Autor:
Mahajani, Usha
Publikováno v:
Pacific Affairs, 1971 Apr 01. 44(1), 151-152.
Externí odkaz:
https://www.jstor.org/stable/2755879
Publikováno v:
International Affairs (Royal Institute of International Affairs 1944-), 1971 Jan 01. 47(1), 234-235.
Externí odkaz:
https://www.jstor.org/stable/2614791
Publikováno v:
The Economic Journal, 1965 Mar 01. 75(297), 150-151.
Externí odkaz:
https://www.jstor.org/stable/2229251
Autor:
Alan H. Boxer
Publikováno v:
Economic Record. 41:639-649
Publikováno v:
Journal of Molecular Biology. 326:761-767
ModE is a bacterial transcriptional regulator that orchestrates many aspects of molybdenum metabolism by binding to specific DNA sequences in a molybdate-dependent fashion. We present the crystal structure of Escherichia coli ModE in complex with mol
Autor:
David H. Boxer, Günter Schwarz, Jochen Kuper, Bernd Vödisch, Ralf R. Mendel, Sonja Meyer zu Berstenhorst
Publikováno v:
FEMS Microbiology Letters. 218:187-193
Molybdenum is an important trace element as it forms the essential part of the active site in all molybdenum-containing enzymes. We have designed an assay for the in vivo detection of molybdate binding to proteins in Escherichia coli. The assay is ba
Publikováno v:
Journal of Biological Chemistry. 277:15013-15020
MopII from Clostridium pasteurianumis a molbindin family member. These proteins may serve as intracellular storage facilities for molybdate, which they bind with high specificity. High resolution structures of MopII in a number of states, including t
Autor:
R. Elizabeth Sockett, Tracy Palmer, Alastair G. McEwan, Ian Gordon Goodfellow, David H. Boxer
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1395:135-140
A clone carrying the mob locus from Rb. sphaeroides WS8 has been isolated from a cosmid library by Southern blotting with a probe covering the mob genes of Escherichia coli. The mob DNA has been subcloned and partially restores molybdoenzyme activiti
Publikováno v:
European Journal of Biochemistry. 246:690-697
The mob mutants of Escherichia coli are pleiotropically defective in molybdoenzyme activities because they are unable to catalyse the conversion of molybdopterin to molybdopterin guanine dinucleotide, the active form of the molybdenum cofactor. The m