Zobrazeno 1 - 10
of 89
pro vyhledávání: '"A. H. Boxer"'
Autor:
Alan H. Boxer
Publikováno v:
Economic Record. 41:639-649
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bbb944ddea7b3d86fdb91ff9718e0d12
https://doi.org/10.1111/j.1475-4932.1965.tb03112.x
https://doi.org/10.1111/j.1475-4932.1965.tb03112.x
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::016f4f5fa635f5bc548fcefc821d48f5
https://doi.org/10.1016/s0022-2836(02)01358-x
https://doi.org/10.1016/s0022-2836(02)01358-x
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3463281a4c6ce3574f46f908d698bec8
https://doi.org/10.1111/j.1574-6968.2003.tb11517.x
https://doi.org/10.1111/j.1574-6968.2003.tb11517.x
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f7ab480a0648b8f5a75501935accfedd
https://doi.org/10.1074/jbc.m201005200
https://doi.org/10.1074/jbc.m201005200
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29b7a827c647b7fbda7c2d186dee7d62
https://doi.org/10.1016/s0167-4781(97)00145-0
https://doi.org/10.1016/s0167-4781(97)00145-0
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::229218955fc40c207dd7238a5e60836b
https://doi.org/10.1111/j.1432-1033.1997.t01-1-00690.x
https://doi.org/10.1111/j.1432-1033.1997.t01-1-00690.x
Autor:
Tracy Palmer, Richard N. Pau, Stephen Bornemann, Nicholas C. Price, David H. Boxer, Lisa A. Anderson
Publikováno v:
European Journal of Biochemistry. 246:119-126
Molybdenum-dependent repression of transcription of the Escherichia coli modABCD operon, which encodes the high-affinity molybdate transporter, is mediated by the ModE protein. This regulatory protein was purified as an N-terminal His6-tagged derivat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3cc85f7271c9b61739274e0d54a03584
https://doi.org/10.1111/j.1432-1033.1997.00119.x
https://doi.org/10.1111/j.1432-1033.1997.00119.x
Publikováno v:
FEBS Letters. 392:81-86
The cellular location of membrane-bound NiFe-hydrogenase 2 (HYD2) from Escherichia coli was studied by immunoblot analysis and by activity staining. Treatment of spheroplasts with trypsin was able to release active HYD2 into the soluble fraction, ind
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::243d0ff00dd1628c8c6961cbb9c1b8f5
https://doi.org/10.1016/0014-5793(96)00788-0
https://doi.org/10.1016/0014-5793(96)00788-0
Publikováno v:
Journal of Bacteriology. 174:7934-7940
All molybdoenzyme activities are absent in chlB mutants because of their inability to synthesize molybdopterin guanine dinucleotide, which together with molybdate constitutes the molybdenum cofactor in Escherichia coli. The chlB mutants are able to s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa169a0277fed33921fe33bd08bbb9fa
https://doi.org/10.1128/jb.174.24.7934-7940.1992
https://doi.org/10.1128/jb.174.24.7934-7940.1992
Autor:
David H. Boxer, K. P. Baker
Publikováno v:
Molecular Microbiology. 5:901-907
The chlA locus encodes functions required for the biosynthesis of the molybdopterin part of the molybdenum cofactor. Mutants, carrying gene fusions at the chlA locus, which place beta-galactosidase expression under the control of the chlA promoter, h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cef13a28ac672677934a9eec5e02a273
https://doi.org/10.1111/j.1365-2958.1991.tb00764.x
https://doi.org/10.1111/j.1365-2958.1991.tb00764.x