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March 18, 2010
Atomic resolution crystallography of a complex of triosephosphate isomerase with a reaction-intermediate analog: new insight in the proton transfer reaction mechanism
Markus 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 resolution
Inari Kursula, Rik K Wierenga
Current Opinion in Structural Biology
|
August 5, 2023
Enzymes of the crotonase superfamily: Diverse assembly and diverse function
Subhadra 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 pathway
Rajaram 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 CdsD
Gitte Meriläinen, Rik K Wierenga
Acta Crystallographica. Section D, Structural Biology
|
July 10, 2024
Managing macromolecular crystallographic data with a laboratory information management system
Edward 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 isomerase
Mirja Krause, Peter Neubauer, Rik K Wierenga
Trends in Biochemical Sciences
|
December 17, 2005
The thiolase superfamily: condensing enzymes with diverse reaction specificities
Antti 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 trachomatis
Gitte 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 enzyme
Gitte Meriläinen, Werner Schmitz, Rik K Wierenga, et al.
Page
of 9
Search research articles
Search
Showing results (1-10 of 88) with videos related to
Sort By:
Page
of 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 mechanism
Markus 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 resolution
Inari Kursula, Rik K Wierenga
Current Opinion in Structural Biology
|
August 5, 2023
Enzymes of the crotonase superfamily: Diverse assembly and diverse function
Subhadra 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 pathway
Rajaram 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 CdsD
Gitte Meriläinen, Rik K Wierenga
Acta Crystallographica. Section D, Structural Biology
|
July 10, 2024
Managing macromolecular crystallographic data with a laboratory information management system
Edward 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 isomerase
Mirja Krause, Peter Neubauer, Rik K Wierenga
Trends in Biochemical Sciences
|
December 17, 2005
The thiolase superfamily: condensing enzymes with diverse reaction specificities
Antti 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 trachomatis
Gitte 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 enzyme
Gitte Meriläinen, Werner Schmitz, Rik K Wierenga, et al.
Page
of 9