DOI: 10.1016/j.bbapap.2007.10.008. 3D structure of Syk kinase determined by single-particle electron microscopy

3D structure of Syk kinase determined by single-particle electron microscopy

10.1016/j.bbapap.2007.10.008

Crossref journal-article

Elsevier BV

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics (78)

Bibliography

Arias-Palomo, E., Recuero-Checa, M. A., Bustelo, X. R., & Llorca, O. (2007). 3D structure of Syk kinase determined by single-particle electron microscopy. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 1774(12), 1493â1499.

Authors 4

Ernesto Arias-Palomo (first)
María A. Recuero-Checa (additional)
Xosé R. Bustelo (additional)
Oscar Llorca (additional)

References 33 Referenced 20

10.1016/S0952-7915(00)00219-3 / Curr. Opin. Immunol. / Proximal protein tyrosine kinases in immunoreceptor signaling by Latour (2001)
10.1093/oxfordjournals.jbchem.a002970 / J. Biochem. (Tokyo) / Structure and function of Syk protein–tyrosine kinase by Sada (2001)
10.1016/j.bbrc.2004.09.171 / Biochem. Biophys. Res. Commun. / Src protein–tyrosine kinase structure and regulation by Roskoski (2004)
10.1006/jmbi.1998.1964 / J. Mol. Biol. / Structural basis for Syk tyrosine kinase ubiquity in signal transduction pathways revealed by the crystal structure of its regulatory SH2 domains bound to a dually phosphorylated ITAM peptide by Futterer (1998)
10.1093/emboj/17.9.2584 / Embo J. / A unique insert in the linker domain of Syk is necessary for its function in immunoreceptor signalling by Latour (1998)
10.1016/j.jasms.2005.02.011 / J. Am. Soc. Mass Spectrom. / Binding of a diphosphorylated-ITAM peptide to spleen tyrosine kinase (Syk) induces distal conformational changes: a hydrogen exchange mass spectrometry study by Catalina (2005)
10.1128/MCB.16.4.1471 / Mol. Cell Biol. / Conformational changes induced in the protein tyrosine kinase p72syk by tyrosine phosphorylation or by binding of phosphorylated immunoreceptor tyrosine-based activation motif peptides by Kimura (1996)
10.1021/bi991840x / Biochemistry / Activation of Zap-70 tyrosine kinase due to a structural rearrangement induced by tyrosine phosphorylation and/or ITAM binding by Visco (2000)
10.1038/35021086 / Nature / The Syk tyrosine kinase suppresses malignant growth of human breast cancer cells by Coopman (2000)
10.1016/j.canlet.2005.11.004 / Cancer Lett. / The Syk tyrosine kinase: a new negative regulator in tumor growth and progression by Coopman (2006)
10.1128/MCB.25.12.4924-4933.2005 / Mol. Cell Biol. / Intramolecular regulatory switch in ZAP-70: analogy with receptor tyrosine kinases by Brdicka (2005)
10.1016/S1074-7613(00)80273-3 / Immunity / Functional and physical interactions of Syk family kinases with the Vav proto-oncogene product by Deckert (1996)
10.1016/j.jmb.2005.11.095 / J. Mol. Biol. / Structural basis for the requirement of two phosphotyrosine residues in signaling mediated by Syk tyrosine kinase by Groesch (2006)
10.1021/bi026465e / Biochemistry / Crystal structure and NMR studies of the apo SH2 domains of ZAP-70: two bikes rather than a tandem by Folmer (2002)
10.1016/j.cell.2007.03.039 / Cell / Structural basis for the inhibition of tyrosine kinase activity of ZAP-70 by Deindl (2007)
10.1074/jbc.M409792200 / J. Biol. Chem. / A novel mode of Gleevec binding is revealed by the structure of spleen tyrosine kinase by Atwell (2004)
10.1111/j.1745-7254.2005.00203.x / Acta Pharmacol. Sin. / Introduction to 3D reconstruction of macromolecules using single particle electron microscopy by Llorca (2005)
10.1006/prep.1993.1051 / Protein Expr. Purif. / Analysis of the tyrosine protein kinase p56lck expressed as a glutathione S-transferase fusion protein in Spodoptera frugiperda cells by Spana (1993)
10.1074/jbc.270.21.12659 / J. Biol. Chem. / Molecular cloning of rodent p72Syk. Evidence of alternative mRNA splicing by Rowley (1995)
10.1038/385169a0 / Nature / Phosphotyrosine-dependent activation of Rac-1 GDP/GTP exchange by the vav proto-oncogene product by Crespo (1997)
10.1128/MCB.20.5.1678-1691.2000 / Mol. Cell Biol. / Tyrosine phosphorylation mediates both activation and downmodulation of the biological activity of Vav by Lopez-Lago (2000)
10.1038/sj.onc.1201430 / Oncogene / Cbl-b, a member of the Sli-1/c-Cbl protein family, inhibits Vav-mediated c-Jun N-terminal kinase activation by Bustelo (1997)
10.1006/jsbi.1999.4174 / J. Struct. Biol. / EMAN: semiautomated software for high-resolution single-particle reconstructions by Ludtke (1999)
10.1016/j.jsb.2004.06.006 / J. Struct. Biol. / XMIPP: a new generation of an open-source image processing package for electron microscopy by Sorzano (2004)
10.1038/sj.embor.7400847 / EMBO Rep. / Structural model of full-length human Ku70-Ku80 heterodimer and its recognition of DNA and DNA-PKcs by Rivera-Calzada (2007)
10.1016/j.molcel.2006.04.013 / Mol. Cell / Three-dimensional structure of the human DNA–PKcs/Ku70/Ku80 complex assembled on DNA and its implications for DNA DSB repair by Spagnolo (2006)
10.1002/jcc.20084 / J. Comput. Chem. / UCSF Chimera—a visualization system for exploratory research and analysis by Pettersen (2004)
10.1002/jemt.1060090405 / J. Electron. Microsc. Tech. / Three-dimensional reconstruction of single particles from random and nonrandom tilt series by Radermacher (1988)
10.1006/jmbi.2002.5438 / J. Mol. Biol. / Multi-resolution contour-based fitting of macromolecular structures by Chacon (2002)
10.1006/jsbi.1998.4080 / J. Struct. Biol. / Situs: a package for docking crystal structures into low-resolution maps from electron microscopy by Wriggers (1999)
{'key': '10.1016/j.bbapap.2007.10.008_bib31', 'article-title': 'ADP_EM: fast exhaustive multi-resolution docking for high-throughput coverage', 'author': 'Garzon', 'year': '2006', 'journal-title': 'Bioinformatics'} / Bioinformatics / ADP_EM: fast exhaustive multi-resolution docking for high-throughput coverage by Garzon (2006)
10.1016/S0167-4889(96)00131-0 / Biochim. Biophys. Acta / Identification of the major sites of autophosphorylation of the murine protein–tyrosine kinase Syk by Furlong (1997)
10.1016/S0003-2697(03)00026-5 / Anal. Biochem. / Development of a high-throughput fluoroimmunoassay for Syk kinase and Syk kinase inhibitors by Yamamoto (2003)

Dates

Type	When
Created	17 years, 9 months ago (Oct. 29, 2007, 8:47 a.m.)
Deposited	3 years, 1 month ago (July 14, 2022, 11:09 p.m.)
Indexed	1 year, 2 months ago (May 25, 2024, 2:32 a.m.)
Issued	17 years, 8 months ago (Dec. 1, 2007)
Published	17 years, 8 months ago (Dec. 1, 2007)
Published Print	17 years, 8 months ago (Dec. 1, 2007)

Funders 0

None

BibTeX

@article{Arias_Palomo_2007, title={3D structure of Syk kinase determined by single-particle electron microscopy}, volume={1774}, ISSN={1570-9639}, url={http://dx.doi.org/10.1016/j.bbapap.2007.10.008}, DOI={10.1016/j.bbapap.2007.10.008}, number={12}, journal={Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics}, publisher={Elsevier BV}, author={Arias-Palomo, Ernesto and Recuero-Checa, María A. and Bustelo, Xosé R. and Llorca, Oscar}, year={2007}, month=dec, pages={1493–1499} }

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