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Klaus Reuter

Showing results (1-10 of 37) with videos related to

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Journal of Molecular Biology|February 16, 2025
RNA-modification by Base Exchange: Structure, Function and Application of tRNA-guanine TransglycosylasesKlaus Reuter, Ralf Ficner
Chembiochem : a European Journal of Chemical Biology|October 6, 2005
Mechanism and substrate specificity of tRNA-guanine transglycosylases (TGTs): tRNA-modifying enzymes from the three different kingdoms of life share a common catalytic mechanismBernhard Stengl, Klaus Reuter, Gerhard Klebe
Nature Methods|April 8, 2021
Sensitive protein alignments at tree-of-life scale using DIAMONDBenjamin Buchfink, Klaus Reuter, Hajk-Georg Drost
Acta Crystallographica. Section D, Biological Crystallography|June 3, 2010
A crystallization screen based on alternative polymeric precipitantsClemens Grimm, Ashwin Chari, Klaus Reuter, et al.
The Journal of Chemical Physics|November 8, 2022
TriMem: A parallelized hybrid Monte Carlo software for efficient simulations of lipid membranesMarc Siggel, Sebastian Kehl, Klaus Reuter, et al.
Chembiochem : a European Journal of Chemical Biology|October 3, 2003
Flexible adaptations in the structure of the tRNA-modifying enzyme tRNA-guanine transglycosylase and their implications for substrate selectivity, reaction mechanism and structure-based drug designRuth Brenk, Milton T Stubbs, Andreas Heine, et al.
Biochemical and Biophysical Research Communications|November 7, 2006
Crystal structure of Bacillus subtilis S-adenosylmethionine:tRNA ribosyltransferase-isomeraseClemens Grimm, Ralf Ficner, Tanja Sgraja, et al.
Plos One|May 26, 2010
Synthesis of 5-hydroxyectoine from ectoine: crystal structure of the non-heme iron(II) and 2-oxoglutarate-dependent dioxygenase EctDKlaus Reuter, Marco Pittelkow, Jan Bursy, et al.
Proteins|March 14, 2014
High resolution crystal structure of Clostridium propionicum β-alanyl-CoA:ammonia lyase, a new member of the "hot dog fold" protein superfamilyAndreas Heine, Gloria Herrmann, Thorsten Selmer, et al.
The Journal of Biological Chemistry|August 12, 2003
An essential role for aspartate 264 in catalysis by tRNA-guanine transglycosylase from Escherichia coliJeffrey D Kittendorf, Tanja Sgraja, Klaus Reuter, et al.
Pageof 4

Showing results (1-10 of 37) with videos related to

Sort By:
Pageof 4
Journal of Molecular Biology|February 16, 2025
RNA-modification by Base Exchange: Structure, Function and Application of tRNA-guanine TransglycosylasesKlaus Reuter, Ralf Ficner
Chembiochem : a European Journal of Chemical Biology|October 6, 2005
Mechanism and substrate specificity of tRNA-guanine transglycosylases (TGTs): tRNA-modifying enzymes from the three different kingdoms of life share a common catalytic mechanismBernhard Stengl, Klaus Reuter, Gerhard Klebe
Nature Methods|April 8, 2021
Sensitive protein alignments at tree-of-life scale using DIAMONDBenjamin Buchfink, Klaus Reuter, Hajk-Georg Drost
Acta Crystallographica. Section D, Biological Crystallography|June 3, 2010
A crystallization screen based on alternative polymeric precipitantsClemens Grimm, Ashwin Chari, Klaus Reuter, et al.
The Journal of Chemical Physics|November 8, 2022
TriMem: A parallelized hybrid Monte Carlo software for efficient simulations of lipid membranesMarc Siggel, Sebastian Kehl, Klaus Reuter, et al.
Chembiochem : a European Journal of Chemical Biology|October 3, 2003
Flexible adaptations in the structure of the tRNA-modifying enzyme tRNA-guanine transglycosylase and their implications for substrate selectivity, reaction mechanism and structure-based drug designRuth Brenk, Milton T Stubbs, Andreas Heine, et al.
Biochemical and Biophysical Research Communications|November 7, 2006
Crystal structure of Bacillus subtilis S-adenosylmethionine:tRNA ribosyltransferase-isomeraseClemens Grimm, Ralf Ficner, Tanja Sgraja, et al.
Plos One|May 26, 2010
Synthesis of 5-hydroxyectoine from ectoine: crystal structure of the non-heme iron(II) and 2-oxoglutarate-dependent dioxygenase EctDKlaus Reuter, Marco Pittelkow, Jan Bursy, et al.
Proteins|March 14, 2014
High resolution crystal structure of Clostridium propionicum β-alanyl-CoA:ammonia lyase, a new member of the "hot dog fold" protein superfamilyAndreas Heine, Gloria Herrmann, Thorsten Selmer, et al.
The Journal of Biological Chemistry|August 12, 2003
An essential role for aspartate 264 in catalysis by tRNA-guanine transglycosylase from Escherichia coliJeffrey D Kittendorf, Tanja Sgraja, Klaus Reuter, et al.
Pageof 4