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Acta Crystallographica. Section D, Biological Crystallography
|
October 8, 1998
The FNR-like domain of the Escherichia coli sulfite reductase flavoprotein component: crystallization and preliminary X-ray analysis
A Gruez, M Zeghouf, J Bertrand, et al.
Chemical Science
|
November 17, 2017
A noble metal-free proton-exchange membrane fuel cell based on bio-inspired molecular catalysts
P D Tran, A Morozan, S Archambault, et al.
The Journal of Biological Chemistry
|
September 26, 1997
Activation of the anaerobic ribonucleotide reductase from Escherichia coli. The essential role of the iron-sulfur center for S-adenosylmethionine reduction
S Ollagnier, E Mulliez, P P Schmidt, et al.
European Journal of Biochemistry
|
January 5, 1999
Reactivity studies of the tyrosyl radical in ribonucleotide reductase from Mycobacterium tuberculosis and Arabidopsis thaliana--comparison with Escherichia coli and mouse
E Elleingand, C Gerez, S Un, et al.
The Journal of Biological Chemistry
|
March 22, 1996
The free radical of the anaerobic ribonucleotide reductase from Escherichia coli is at glycine 681
X Sun, S Ollagnier, P P Schmidt, et al.
Journal of Materials Chemistry. A
|
January 10, 2014
Dye-Sensitized Nanostructured Crystalline Mesoporous Tin-doped Indium Oxide Films with Tunable Thickness for Photoelectrochemical Applications
W Hamd, M Chavarot-Kerlidou, J Fize, et al.
Nature
|
June 28, 2013
Biomimetic assembly and activation of [FeFe]-hydrogenases
G Berggren, A Adamska, C Lambertz, et al.
Page
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Search research articles
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Showing results (101-110 of 107) with videos related to
Sort By:
Page
of 11
You have reached the last page of results.
This site can display upto 107 results.
Acta Crystallographica. Section D, Biological Crystallography
|
October 8, 1998
The FNR-like domain of the Escherichia coli sulfite reductase flavoprotein component: crystallization and preliminary X-ray analysis
A Gruez, M Zeghouf, J Bertrand, et al.
Chemical Science
|
November 17, 2017
A noble metal-free proton-exchange membrane fuel cell based on bio-inspired molecular catalysts
P D Tran, A Morozan, S Archambault, et al.
The Journal of Biological Chemistry
|
September 26, 1997
Activation of the anaerobic ribonucleotide reductase from Escherichia coli. The essential role of the iron-sulfur center for S-adenosylmethionine reduction
S Ollagnier, E Mulliez, P P Schmidt, et al.
European Journal of Biochemistry
|
January 5, 1999
Reactivity studies of the tyrosyl radical in ribonucleotide reductase from Mycobacterium tuberculosis and Arabidopsis thaliana--comparison with Escherichia coli and mouse
E Elleingand, C Gerez, S Un, et al.
The Journal of Biological Chemistry
|
March 22, 1996
The free radical of the anaerobic ribonucleotide reductase from Escherichia coli is at glycine 681
X Sun, S Ollagnier, P P Schmidt, et al.
Journal of Materials Chemistry. A
|
January 10, 2014
Dye-Sensitized Nanostructured Crystalline Mesoporous Tin-doped Indium Oxide Films with Tunable Thickness for Photoelectrochemical Applications
W Hamd, M Chavarot-Kerlidou, J Fize, et al.
Nature
|
June 28, 2013
Biomimetic assembly and activation of [FeFe]-hydrogenases
G Berggren, A Adamska, C Lambertz, et al.
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of 11