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The purification and characterization of the catalytic domain of Src expressed in Schizosaccharomyces pombe. Comparison of unphosphorylated and tyrosine phosphorylated species.
Weijland A, Neubauer G, Courtneidge SA, Mann M, Wierenga RK, Superti-Furga G. Weijland A, et al. Eur J Biochem. 1996 Sep 15;240(3):756-64. doi: 10.1111/j.1432-1033.1996.0756h.x. Eur J Biochem. 1996. PMID: 8856081 Free article.
Crosstalk between the catalytic and regulatory domains allows bidirectional regulation of Src.
Gonfloni S, Weijland A, Kretzschmar J, Superti-Furga G. Gonfloni S, et al. Among authors: weijland a. Nat Struct Biol. 2000 Apr;7(4):281-6. doi: 10.1038/74041. Nat Struct Biol. 2000. PMID: 10742171
The role of the linker between the SH2 domain and catalytic domain in the regulation and function of Src.
Gonfloni S, Williams JC, Hattula K, Weijland A, Wierenga RK, Superti-Furga G. Gonfloni S, et al. Among authors: weijland a. EMBO J. 1997 Dec 15;16(24):7261-71. doi: 10.1093/emboj/16.24.7261. EMBO J. 1997. PMID: 9405355 Free PMC article.
The 2.35 A crystal structure of the inactivated form of chicken Src: a dynamic molecule with multiple regulatory interactions.
Williams JC, Weijland A, Gonfloni S, Thompson A, Courtneidge SA, Superti-Furga G, Wierenga RK. Williams JC, et al. Among authors: weijland a. J Mol Biol. 1997 Dec 19;274(5):757-75. doi: 10.1006/jmbi.1997.1426. J Mol Biol. 1997. PMID: 9405157
Src regulated by C-terminal phosphorylation is monomeric.
Weijland A, Williams JC, Neubauer G, Courtneidge SA, Wierenga RK, Superti-Furga G. Weijland A, et al. Proc Natl Acad Sci U S A. 1997 Apr 15;94(8):3590-5. doi: 10.1073/pnas.94.8.3590. Proc Natl Acad Sci U S A. 1997. PMID: 9108021 Free PMC article.
Elongation factor Tu D138N, a mutant with modified substrate specificity, as a tool to study energy consumption in protein biosynthesis.
Weijland A, Parlato G, Parmeggiani A. Weijland A, et al. Biochemistry. 1994 Sep 6;33(35):10711-7. doi: 10.1021/bi00201a019. Biochemistry. 1994. PMID: 8075071
Toward a model for the interaction between elongation factor Tu and the ribosome.
Weijland A, Parmeggiani A. Weijland A, et al. Science. 1993 Feb 26;259(5099):1311-4. doi: 10.1126/science.8446899. Science. 1993. PMID: 8446899
Asparagine-135 of elongation factor Tu is a crucial residue for the folding of the guanine nucleotide binding pocket.
Weijland A, Sarfati R, Bârzu O, Parmeggiani A. Weijland A, et al. FEBS Lett. 1993 Sep 20;330(3):334-8. doi: 10.1016/0014-5793(93)80899-6. FEBS Lett. 1993. PMID: 8375504 Free article.
Why do two EF-Tu molecules act in the elongation cycle of protein biosynthesis?
Weijland A, Parmeggiani A. Weijland A, et al. Trends Biochem Sci. 1994 May;19(5):188-93. doi: 10.1016/0968-0004(94)90018-3. Trends Biochem Sci. 1994. PMID: 8048158 Review.
Mutagenesis of the NH2-terminal domain of elongation factor Tu.
Gümüşel F, Cool RH, Weijland A, Anborgh PH, Parmeggiani A. Gümüşel F, et al. Among authors: weijland a. Biochim Biophys Acta. 1990 Aug 27;1050(1-3):215-21. doi: 10.1016/0167-4781(90)90169-3. Biochim Biophys Acta. 1990. PMID: 2119812
The double substitution Val88----Asp and Leu121----Lys, two residues situated on two vicinal alpha-helices, influences the basic activities of the truncated factor to a limited extent, probably via long-range interactions, and induces a destabilisation of the G doma …
The double substitution Val88----Asp and Leu121----Lys, two residues situated on two vicinal alpha-helices, influences the basic activities …
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