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A Weijland

Showing results (1-10 of 12) with videos related to

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Trends in Biochemical Sciences|May 1, 1994
Why do two EF-Tu molecules act in the elongation cycle of protein biosynthesis?A Weijland, A Parmeggiani
Science (New York, N.Y.)|February 26, 1993
Toward a model for the interaction between elongation factor Tu and the ribosomeA Weijland, A Parmeggiani
Biochemistry|September 6, 1994
Elongation factor Tu D138N, a mutant with modified substrate specificity, as a tool to study energy consumption in protein biosynthesisA Weijland, G Parlato, A Parmeggiani
Nature Structural Biology|March 31, 2000
Crosstalk between the catalytic and regulatory domains allows bidirectional regulation of SrcS Gonfloni, A Weijland, J Kretzschmar, et al.
FEBS Letters|September 20, 1993
Asparagine-135 of elongation factor Tu is a crucial residue for the folding of the guanine nucleotide binding pocketA Weijland, R Sarfati, O Bârzu, et al.
Biochimica Et Biophysica Acta|August 27, 1990
Mutagenesis of the NH2-terminal domain of elongation factor TuF Gümüşel, R H Cool, A Weijland, et al.
Molecular Microbiology|March 1, 1992
Elongation factor Tu: a molecular switch in protein biosynthesisA Weijland, K Harmark, R H Cool, et al.
The EMBO Journal|February 21, 1998
The role of the linker between the SH2 domain and catalytic domain in the regulation and function of SrcS Gonfloni, J C Williams, K Hattula, et al.
Proceedings of the National Academy of Sciences of the United States of America|April 15, 1997
Src regulated by C-terminal phosphorylation is monomericA Weijland, J C Williams, G Neubauer, et al.
European Journal of Biochemistry|September 15, 1996
The purification and characterization of the catalytic domain of Src expressed in Schizosaccharomyces pombe. Comparison of unphosphorylated and tyrosine phosphorylated speciesA Weijland, G Neubauer, S A Courtneidge, et al.
Pageof 2

Showing results (1-10 of 12) with videos related to

Sort By:
Pageof 2
Trends in Biochemical Sciences|May 1, 1994
Why do two EF-Tu molecules act in the elongation cycle of protein biosynthesis?A Weijland, A Parmeggiani
Science (New York, N.Y.)|February 26, 1993
Toward a model for the interaction between elongation factor Tu and the ribosomeA Weijland, A Parmeggiani
Biochemistry|September 6, 1994
Elongation factor Tu D138N, a mutant with modified substrate specificity, as a tool to study energy consumption in protein biosynthesisA Weijland, G Parlato, A Parmeggiani
Nature Structural Biology|March 31, 2000
Crosstalk between the catalytic and regulatory domains allows bidirectional regulation of SrcS Gonfloni, A Weijland, J Kretzschmar, et al.
FEBS Letters|September 20, 1993
Asparagine-135 of elongation factor Tu is a crucial residue for the folding of the guanine nucleotide binding pocketA Weijland, R Sarfati, O Bârzu, et al.
Biochimica Et Biophysica Acta|August 27, 1990
Mutagenesis of the NH2-terminal domain of elongation factor TuF Gümüşel, R H Cool, A Weijland, et al.
Molecular Microbiology|March 1, 1992
Elongation factor Tu: a molecular switch in protein biosynthesisA Weijland, K Harmark, R H Cool, et al.
The EMBO Journal|February 21, 1998
The role of the linker between the SH2 domain and catalytic domain in the regulation and function of SrcS Gonfloni, J C Williams, K Hattula, et al.
Proceedings of the National Academy of Sciences of the United States of America|April 15, 1997
Src regulated by C-terminal phosphorylation is monomericA Weijland, J C Williams, G Neubauer, et al.
European Journal of Biochemistry|September 15, 1996
The purification and characterization of the catalytic domain of Src expressed in Schizosaccharomyces pombe. Comparison of unphosphorylated and tyrosine phosphorylated speciesA Weijland, G Neubauer, S A Courtneidge, et al.
Pageof 2