Skip to main content
Utility Menu
Search
scholar.ulethbridge.ca
Dr. Hans-Joachim Wieden
Associate Professor of Physical Biochemistry
Department of Chemistry and Biochemistry
Welcome
Publications
HOME
/
Publications
2013
Chen XL, Serrano D, Mayhue M, Wieden H-J, Stankova J, Boulay G, Ilangumaran S, Ramanathan S
.
GTPase of the immune-associated nucleotide-binding protein 5 (GIMAP5) regulates calcium influx in T-lymphocytes by promoting mitochondrial calcium accumulation.
Biochem J. 2013;449(2):353-364.
2012
Becker M, Gzyl K, A.M. A, Vuong A, Urban K, Wieden H-J
.
The 70S ribosome modulates the ATPase activity of Escherichia coli YchF.
RNA Biology . 2012;9(10):1288-1301.
Fischer JJ, Coatham ML, Eagle Bear S, Brandon HE, De Laurentiis EI, Shields MJ, Wieden H-J
.
The ribosome modulates the structural dynamics of the conserved GTPase HflX and triggers tight nucleotide binding
. Biochimie. 2012;94(8):1647-1659.
Gruninger RJ, Dobing S, Smith AD, Bruder LM, Selinger LB, Wieden H-J, Mosimann SC
.
Substrate binding in protein tyrosine phosphatase-like inositol polyphosphatases.
J. Biol. Chem . 2012;287(13):9722-9730.
2011
De Laurentiis EI, Mo F, Wieden H-J
.
Construction of a fully active Cys-less Elongation Factor Tu: Functional role of the conserved Cystein 81
. Biochim. Biophys. Acta. 2011;1814:684-692.
2010
Wieden H-J, Mercier E, Gray J, Steed B, Yawney D
.
A combined molecular dynamics and rapid kinetics approach to identify conserved 3 dimensional communication networks in Elongation Factor Tu.
Biophys J. 2010;99:3735-3743.
2009
Shields M, Fischer JJ, Wieden H-J
.
Toward understanding the function of the universally conserved GTPase HflX from Escherichia coli: A kinetic approach
. Biochemistry. 2009;48:10793-10802.
2006
Dahl LD, Wieden H-J, Rodnina MV, Knudsen CR
.
The importance of P-loop and domain movements in EF-Tu for guanine nucleotide exchange
. J. Biol. Chem . 2006;281:21139-21146.
2005
Buskiewicz I, Peske F, Wieden H-J, Gryczynski I, Rodnina MV, Wintermeyer W
.
Conformations of the Signal Recognition Particle Protein Ffh from Escherichia coli as Determined by FRET.
J. Mol. Biol. 2005;351:417-430.
Rodnina MV, Gromadski KB, Kothe U, Wieden H-J
.
Recognition and selection of tRNA in translation
. FEBS Lett. 2005;579:938-942.
2004
Kothe U, Wieden H-J, Mohr D, Rodnina MV
.
Interaction of helix D of elongation factor Tu with helices 4 and 5 of protein L7/12 on the ribosome.
J Mol Biol. 2004;336:1011-1021.
2003
Juranek S, Wieden H-J, Lipps HJ
.
De novo cytosine methylation in the differentiating macronucleus of the stichotrichous ciliate Stylonychia lemnae
. Nuc. Acids Res. 2003;31:1387-1391.
Daviter T, Wieden H-J, Rodnina MV
.
Essential role of histidine 84 in elongation factor Tu for the chemical step of GTP hydrolysis on the ribosome
. J. Mol. Biol. 2003;332:689-699.
Gu S-Q, Peske F, Wieden H-J, Rodnina MV, Wintermeyer W
.
The signal recognition particle binds to protein L23 at the peptide exit of the E. coli ribosome
. RNA. 2003;9:566-573.
2002
Schirmer J, Wieden H-J, Rodnina MV, Aktories K
.
Inactivation of the elongation factor Tu by mosquitocidal toxin catalyzed mono-ADP-ribosylation
. Appl. Environ. Microbiol. 2002;68:4894-4899.
Gromadski KB, Wieden H-J, Rodnina MV
.
Kinetic mechanism of elongation factor Ts-catalyzed nucleotide exchange in elongation factor Tu
. Biochemistry. 2002;41:162-169.
Wieden H-J, Gromadski KB, Rodnin DN, Rodnina MV
.
Mechanism of EF-Ts-catalzed nucleotide exchange in EF-Tu: Contribution of contacts at the guanine base
. J. Biol. Chem . 2002;277:6032-6036.
Stark H, Rodnina MV, Wieden H-J, Zemlin F, Wintermeyer W, van Heel M
.
Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon recognition complex.
Nat. Struct. Biol. 2002;9:849-854.
2001
Wieden H-J, Wintermeyer W, Rodnina MV
.
A common structural motif in elongation factor Ts and ribosomal protein L7/12 may be involved in the interaction with elongation factor Tu
. J. Mol. Evol. 2001;52:129-136.
Knudsen CR, Wieden H-J, Rodnina MV
.
Importance of structural transitions of the switch II region for the functions of elongation factor Tu on the ribosome
. J. Biol. Chem . 2001;276:22183-22190.
Stark H, Rodnina MV, Wieden H-J, van Heel M, Wintermeyer W
.
Large-scale movement of elongation factor G and extensive conformational changes of the ribosome during translocation
. Cell. 2001;100:301-309.
2000
Rodnina MV, Stark H, Savelsbergh A, Wieden H-J, Mohr D, Matassova NB, Peske F, Daviter T, Gualerzi CO, Wintermeyer W
.
GTPase mechanisms and functions of translation factors on the ribosome
. Biol. Chem. 2000;381:377-387.
Search
Recent Publications
GTPase of the immune-associated nucleotide-binding protein 5 (GIMAP5) regulates calcium influx in T-lymphocytes by promoting mitochondrial calcium accumulation.
The 70S ribosome modulates the ATPase activity of Escherichia coli YchF.
The ribosome modulates the structural dynamics of the conserved GTPase HflX and triggers tight nucleotide binding
Substrate binding in protein tyrosine phosphatase-like inositol polyphosphatases.
Construction of a fully active Cys-less Elongation Factor Tu: Functional role of the conserved Cystein 81
A combined molecular dynamics and rapid kinetics approach to identify conserved 3 dimensional communication networks in Elongation Factor Tu.
More