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Rik K Wierenga

Showing results (1-10 of 88) with videos related to

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Proteins|March 18, 2010
Atomic resolution crystallography of a complex of triosephosphate isomerase with a reaction-intermediate analog: new insight in the proton transfer reaction mechanismMarkus Alahuhta, Rik K Wierenga
The Journal of Biological Chemistry|January 11, 2003
Crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83-A resolutionInari Kursula, Rik K Wierenga
Current Opinion in Structural Biology|August 5, 2023
Enzymes of the crotonase superfamily: Diverse assembly and diverse functionSubhadra Dalwani, Rik K Wierenga
ACS Chemical Biology|March 19, 2013
Structure of mycobacterial β-oxidation trifunctional enzyme reveals its altered assembly and putative substrate channeling pathwayRajaram Venkatesan, Rik K Wierenga
Acta Crystallographica. Section F, Structural Biology Communications|October 8, 2014
Crystallization and preliminary X-ray diffraction studies of the C-terminal domain of Chlamydia trachomatis CdsDGitte Meriläinen, Rik K Wierenga
Acta Crystallographica. Section D, Structural Biology|July 10, 2024
Managing macromolecular crystallographic data with a laboratory information management systemEdward Daniel, Rik K Wierenga, Lari Lehtiö
Protein Engineering, Design & Selection : PEDS|March 14, 2015
Structure-based directed evolution of a monomeric triosephosphate isomerase: toward a pentose sugar isomeraseMirja Krause, Peter Neubauer, Rik K Wierenga
Trends in Biochemical Sciences|December 17, 2005
The thiolase superfamily: condensing enzymes with diverse reaction specificitiesAntti M Haapalainen, Gitte Meriläinen, Rik K Wierenga
Protein Science : a Publication of the Protein Society|February 26, 2016
The extended structure of the periplasmic region of CdsD, a structural protein of the type III secretion system of Chlamydia trachomatisGitte Meriläinen, M Kristian Koski, Rik K Wierenga
The FEBS Journal|November 20, 2008
The sulfur atoms of the substrate CoA and the catalytic cysteine are required for a productive mode of substrate binding in bacterial biosynthetic thiolase, a thioester-dependent enzymeGitte Meriläinen, Werner Schmitz, Rik K Wierenga, et al.
Pageof 9

Showing results (1-10 of 88) with videos related to

Sort By:
Pageof 9
Proteins|March 18, 2010
Atomic resolution crystallography of a complex of triosephosphate isomerase with a reaction-intermediate analog: new insight in the proton transfer reaction mechanismMarkus Alahuhta, Rik K Wierenga
The Journal of Biological Chemistry|January 11, 2003
Crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83-A resolutionInari Kursula, Rik K Wierenga
Current Opinion in Structural Biology|August 5, 2023
Enzymes of the crotonase superfamily: Diverse assembly and diverse functionSubhadra Dalwani, Rik K Wierenga
ACS Chemical Biology|March 19, 2013
Structure of mycobacterial β-oxidation trifunctional enzyme reveals its altered assembly and putative substrate channeling pathwayRajaram Venkatesan, Rik K Wierenga
Acta Crystallographica. Section F, Structural Biology Communications|October 8, 2014
Crystallization and preliminary X-ray diffraction studies of the C-terminal domain of Chlamydia trachomatis CdsDGitte Meriläinen, Rik K Wierenga
Acta Crystallographica. Section D, Structural Biology|July 10, 2024
Managing macromolecular crystallographic data with a laboratory information management systemEdward Daniel, Rik K Wierenga, Lari Lehtiö
Protein Engineering, Design & Selection : PEDS|March 14, 2015
Structure-based directed evolution of a monomeric triosephosphate isomerase: toward a pentose sugar isomeraseMirja Krause, Peter Neubauer, Rik K Wierenga
Trends in Biochemical Sciences|December 17, 2005
The thiolase superfamily: condensing enzymes with diverse reaction specificitiesAntti M Haapalainen, Gitte Meriläinen, Rik K Wierenga
Protein Science : a Publication of the Protein Society|February 26, 2016
The extended structure of the periplasmic region of CdsD, a structural protein of the type III secretion system of Chlamydia trachomatisGitte Meriläinen, M Kristian Koski, Rik K Wierenga
The FEBS Journal|November 20, 2008
The sulfur atoms of the substrate CoA and the catalytic cysteine are required for a productive mode of substrate binding in bacterial biosynthetic thiolase, a thioester-dependent enzymeGitte Meriläinen, Werner Schmitz, Rik K Wierenga, et al.
Pageof 9