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Chromosome Research : an International Journal on the Molecular, Supramolecular and Evolutionary Aspects of Chromosome Biology|March 25, 2009

RAD50, an SMC family member with multiple roles in DNA break repair: how does ATP affect function?Eri Kinoshita, Eddy van der Linden, Humberto Sanchez, et al.

Biochimica Et Biophysica Acta|March 5, 2003

Quantitative amino acid analysis of bovine NADH:ubiquinone oxidoreductase (Complex I) and related enzymes. Consequences for the number of prosthetic groupsSimon P J Albracht, Eddy van der Linden, Bart W Faber

Nucleic Acids Research|January 20, 2009

RAD50 and NBS1 form a stable complex functional in DNA binding and tetheringEddy van der Linden, Humberto Sanchez, Eri Kinoshita, et al.

The Journal of Biological Chemistry|September 3, 2004

The auxiliary protein HypX provides oxygen tolerance to the soluble [NiFe]-hydrogenase of ralstonia eutropha H16 by way of a cyanide ligand to nickelBoris Bleijlevens, Thorsten Buhrke, Eddy van der Linden, et al.

Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry|May 28, 2004

The soluble [NiFe]-hydrogenase from Ralstonia eutropha contains four cyanides in its active site, one of which is responsible for the insensitivity towards oxygenEddy Van der Linden, Tanja Burgdorf, Michael Bernhard, et al.

European Journal of Biochemistry|February 7, 2004

Selective release and function of one of the two FMN groups in the cytoplasmic NAD+-reducing [NiFe]-hydrogenase from Ralstonia eutrophaEddy van der Linden, Bart W Faber, Boris Bleijlevens, et al.

Journal of Molecular Microbiology and Biotechnology|April 29, 2006

[NiFe]-hydrogenases of Ralstonia eutropha H16: modular enzymes for oxygen-tolerant biological hydrogen oxidationTanja Burgdorf, Oliver Lenz, Thorsten Buhrke, et al.

Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry|January 19, 2006

An improved purification procedure for the soluble [NiFe]-hydrogenase of Ralstonia eutropha: new insights into its (in)stability and spectroscopic propertiesEddy van der Linden, Tanja Burgdorf, Antonio L de Lacey, et al.

Journal of the American Chemical Society|January 13, 2005

Structural and oxidation-state changes at its nonstandard Ni-Fe site during activation of the NAD-reducing hydrogenase from Ralstonia eutropha detected by X-ray absorption, EPR, and FTIR spectroscopyTanja Burgdorf, Simone Löscher, Peter Liebisch, et al.

Journal of Bacteriology|April 20, 2005

The soluble NAD+-Reducing [NiFe]-hydrogenase from Ralstonia eutropha H16 consists of six subunits and can be specifically activated by NADPHTanja Burgdorf, Eddy van der Linden, Michael Bernhard, et al.

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Showing results (1-10 of 10) with videos related to

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Chromosome Research : an International Journal on the Molecular, Supramolecular and Evolutionary Aspects of Chromosome Biology|March 25, 2009

RAD50, an SMC family member with multiple roles in DNA break repair: how does ATP affect function?Eri Kinoshita, Eddy van der Linden, Humberto Sanchez, et al.

Biochimica Et Biophysica Acta|March 5, 2003

Quantitative amino acid analysis of bovine NADH:ubiquinone oxidoreductase (Complex I) and related enzymes. Consequences for the number of prosthetic groupsSimon P J Albracht, Eddy van der Linden, Bart W Faber

Nucleic Acids Research|January 20, 2009

RAD50 and NBS1 form a stable complex functional in DNA binding and tetheringEddy van der Linden, Humberto Sanchez, Eri Kinoshita, et al.

The Journal of Biological Chemistry|September 3, 2004

The auxiliary protein HypX provides oxygen tolerance to the soluble [NiFe]-hydrogenase of ralstonia eutropha H16 by way of a cyanide ligand to nickelBoris Bleijlevens, Thorsten Buhrke, Eddy van der Linden, et al.

Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry|May 28, 2004

The soluble [NiFe]-hydrogenase from Ralstonia eutropha contains four cyanides in its active site, one of which is responsible for the insensitivity towards oxygenEddy Van der Linden, Tanja Burgdorf, Michael Bernhard, et al.

European Journal of Biochemistry|February 7, 2004

Selective release and function of one of the two FMN groups in the cytoplasmic NAD+-reducing [NiFe]-hydrogenase from Ralstonia eutrophaEddy van der Linden, Bart W Faber, Boris Bleijlevens, et al.

Journal of Molecular Microbiology and Biotechnology|April 29, 2006

[NiFe]-hydrogenases of Ralstonia eutropha H16: modular enzymes for oxygen-tolerant biological hydrogen oxidationTanja Burgdorf, Oliver Lenz, Thorsten Buhrke, et al.

Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry|January 19, 2006

An improved purification procedure for the soluble [NiFe]-hydrogenase of Ralstonia eutropha: new insights into its (in)stability and spectroscopic propertiesEddy van der Linden, Tanja Burgdorf, Antonio L de Lacey, et al.

Journal of the American Chemical Society|January 13, 2005

Structural and oxidation-state changes at its nonstandard Ni-Fe site during activation of the NAD-reducing hydrogenase from Ralstonia eutropha detected by X-ray absorption, EPR, and FTIR spectroscopyTanja Burgdorf, Simone Löscher, Peter Liebisch, et al.

Journal of Bacteriology|April 20, 2005

The soluble NAD+-Reducing [NiFe]-hydrogenase from Ralstonia eutropha H16 consists of six subunits and can be specifically activated by NADPHTanja Burgdorf, Eddy van der Linden, Michael Bernhard, et al.

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