自己リン酸化 (Japanese Wikipedia)

Analysis of information sources in references of the Wikipedia article "自己リン酸化" in Japanese language version.

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1copewithcytokines.de

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copewithcytokines.de

C O P E , Cytokines & Cells Online Pathfinder Encyclopedia, April 2012

doi.org

“Phosphorylation: the molecular switch of double-strand break repair”. International Journal of Proteomics 2011: 373816. (2011). doi:10.1155/2011/373816. PMC 3200257. PMID 22084686.
“Autophosphorylation: a salient feature of protein kinases”. Molecular and Cellular Biochemistry 127–128: 51–70. (Nov 1993). doi:10.1007/BF01076757. PMID 7935362.
“Identifying three-dimensional structures of autophosphorylation complexes in crystals of protein kinases”. Science Signaling 8 (405): rs13. (Dec 2015). doi:10.1126/scisignal.aaa6711. PMC 4766099. PMID 26628682.
“Structure of a c-kit product complex reveals the basis for kinase transactivation”. The Journal of Biological Chemistry 278 (34): 31461–4. (Aug 2003). doi:10.1074/jbc.C300186200. PMID 12824176.
“Structure-based drug design enables conversion of a DFG-in binding CSF-1R kinase inhibitor to a DFG-out binding mode”. Bioorganic & Medicinal Chemistry Letters 20 (5): 1543–7. (Mar 2010). doi:10.1016/j.bmcl.2010.01.078. PMID 20137931.
“The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site”. Cell 138 (3): 514–24. (Aug 2009). doi:10.1016/j.cell.2009.05.028. PMC 4764080. PMID 19665973.
“Structural mimicry of a-loop tyrosine phosphorylation by a pathogenic FGF receptor 3 mutation”. Structure 21 (10): 1889–96. (Oct 2013). doi:10.1016/j.str.2013.07.017. PMC 3839590. PMID 23972473.
“Small-molecule inhibition and activation-loop trans-phosphorylation of the IGF1 receptor”. The EMBO Journal 27 (14): 1985–94. (Jul 2008). doi:10.1038/emboj.2008.116. PMC 2486273. PMID 18566589.
“Design of potent IGF1-R inhibitors related to bis-azaindoles”. Chemical Biology & Drug Design 76 (2): 100–6. (Aug 2010). doi:10.1111/j.1747-0285.2010.00991.x. PMID 20545947.
“Classifying protein kinase structures guides use of ligand-selectivity profiles to predict inactive conformations: structure of lck/imatinib complex”. Proteins 70 (4): 1451–60. (Mar 2008). doi:10.1002/prot.21633. PMID 17910071.
“Structural insights into the autoactivation mechanism of p21-activated protein kinase”. Structure 19 (12): 1752–61. (Dec 2011). doi:10.1016/j.str.2011.10.013. PMID 22153498.
“Back pocket flexibility provides group II p21-activated kinase (PAK) selectivity for type I 1/2 kinase inhibitors”. Journal of Medicinal Chemistry 57 (3): 1033–45. (Feb 2014). doi:10.1021/jm401768t. PMID 24432870.
“Structure-Guided Design of Group I Selective p21-Activated Kinase Inhibitors”. Journal of Medicinal Chemistry 58 (12): 5121–36. (Jun 2015). doi:10.1021/acs.jmedchem.5b00572. PMID 26030457.
“Design of Selective PAK1 Inhibitor G-5555: Improving Properties by Employing an Unorthodox Low-pK a Polar Moiety”. ACS Medicinal Chemistry Letters 6 (12): 1241–6. (Dec 2015). doi:10.1021/acsmedchemlett.5b00398. PMC 4677365. PMID 26713112.
“IRAK4 dimerization and trans-autophosphorylation are induced by Myddosome assembly”. Molecular Cell 55 (6): 891–903. (Sep 2014). doi:10.1016/j.molcel.2014.08.006. PMC 4169746. PMID 25201411.
“Intersubunit capture of regulatory segments is a component of cooperative CaMKII activation”. Nature Structural & Molecular Biology 17 (3): 264–72. (Mar 2010). doi:10.1038/nsmb.1751. PMC 2855215. PMID 20139983.
“Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation”. PLOS Biology 8 (7): e1000426. (2010). doi:10.1371/journal.pbio.1000426. PMC 2910593. PMID 20668654.
“Asymmetric tyrosine kinase arrangements in activation or autophosphorylation of receptor tyrosine kinases”. Molecules and Cells 29 (5): 443–8. (May 2010). doi:10.1007/s10059-010-0080-5. PMID 20432069.
“Src in cancer: deregulation and consequences for cell behaviour”. Biochimica et Biophysica Acta (BBA) - Reviews on Cancer 1602 (2): 114–30. (Jun 2002). doi:10.1016/s0304-419x(02)00040-9. PMID 12020799.
“DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation”. Nature 421 (6922): 499–506. (Jan 2003). Bibcode: 2003Natur.421..499B. doi:10.1038/nature01368. PMID 12556884.

harvard.edu

ui.adsabs.harvard.edu

“DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation”. Nature 421 (6922): 499–506. (Jan 2003). Bibcode: 2003Natur.421..499B. doi:10.1038/nature01368. PMID 12556884.

nih.gov

pubmed.ncbi.nlm.nih.gov

“Phosphorylation: the molecular switch of double-strand break repair”. International Journal of Proteomics 2011: 373816. (2011). doi:10.1155/2011/373816. PMC 3200257. PMID 22084686.
“Autophosphorylation: a salient feature of protein kinases”. Molecular and Cellular Biochemistry 127–128: 51–70. (Nov 1993). doi:10.1007/BF01076757. PMID 7935362.
“Identifying three-dimensional structures of autophosphorylation complexes in crystals of protein kinases”. Science Signaling 8 (405): rs13. (Dec 2015). doi:10.1126/scisignal.aaa6711. PMC 4766099. PMID 26628682.
“Structure of a c-kit product complex reveals the basis for kinase transactivation”. The Journal of Biological Chemistry 278 (34): 31461–4. (Aug 2003). doi:10.1074/jbc.C300186200. PMID 12824176.
“Structure-based drug design enables conversion of a DFG-in binding CSF-1R kinase inhibitor to a DFG-out binding mode”. Bioorganic & Medicinal Chemistry Letters 20 (5): 1543–7. (Mar 2010). doi:10.1016/j.bmcl.2010.01.078. PMID 20137931.
“The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site”. Cell 138 (3): 514–24. (Aug 2009). doi:10.1016/j.cell.2009.05.028. PMC 4764080. PMID 19665973.
“Structural mimicry of a-loop tyrosine phosphorylation by a pathogenic FGF receptor 3 mutation”. Structure 21 (10): 1889–96. (Oct 2013). doi:10.1016/j.str.2013.07.017. PMC 3839590. PMID 23972473.
“Small-molecule inhibition and activation-loop trans-phosphorylation of the IGF1 receptor”. The EMBO Journal 27 (14): 1985–94. (Jul 2008). doi:10.1038/emboj.2008.116. PMC 2486273. PMID 18566589.
“Design of potent IGF1-R inhibitors related to bis-azaindoles”. Chemical Biology & Drug Design 76 (2): 100–6. (Aug 2010). doi:10.1111/j.1747-0285.2010.00991.x. PMID 20545947.
“Classifying protein kinase structures guides use of ligand-selectivity profiles to predict inactive conformations: structure of lck/imatinib complex”. Proteins 70 (4): 1451–60. (Mar 2008). doi:10.1002/prot.21633. PMID 17910071.
“Structural insights into the autoactivation mechanism of p21-activated protein kinase”. Structure 19 (12): 1752–61. (Dec 2011). doi:10.1016/j.str.2011.10.013. PMID 22153498.
“Back pocket flexibility provides group II p21-activated kinase (PAK) selectivity for type I 1/2 kinase inhibitors”. Journal of Medicinal Chemistry 57 (3): 1033–45. (Feb 2014). doi:10.1021/jm401768t. PMID 24432870.
“Structure-Guided Design of Group I Selective p21-Activated Kinase Inhibitors”. Journal of Medicinal Chemistry 58 (12): 5121–36. (Jun 2015). doi:10.1021/acs.jmedchem.5b00572. PMID 26030457.
“Design of Selective PAK1 Inhibitor G-5555: Improving Properties by Employing an Unorthodox Low-pK a Polar Moiety”. ACS Medicinal Chemistry Letters 6 (12): 1241–6. (Dec 2015). doi:10.1021/acsmedchemlett.5b00398. PMC 4677365. PMID 26713112.
“IRAK4 dimerization and trans-autophosphorylation are induced by Myddosome assembly”. Molecular Cell 55 (6): 891–903. (Sep 2014). doi:10.1016/j.molcel.2014.08.006. PMC 4169746. PMID 25201411.
“Intersubunit capture of regulatory segments is a component of cooperative CaMKII activation”. Nature Structural & Molecular Biology 17 (3): 264–72. (Mar 2010). doi:10.1038/nsmb.1751. PMC 2855215. PMID 20139983.
“Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation”. PLOS Biology 8 (7): e1000426. (2010). doi:10.1371/journal.pbio.1000426. PMC 2910593. PMID 20668654.
“Asymmetric tyrosine kinase arrangements in activation or autophosphorylation of receptor tyrosine kinases”. Molecules and Cells 29 (5): 443–8. (May 2010). doi:10.1007/s10059-010-0080-5. PMID 20432069.
“Src in cancer: deregulation and consequences for cell behaviour”. Biochimica et Biophysica Acta (BBA) - Reviews on Cancer 1602 (2): 114–30. (Jun 2002). doi:10.1016/s0304-419x(02)00040-9. PMID 12020799.
“DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation”. Nature 421 (6922): 499–506. (Jan 2003). Bibcode: 2003Natur.421..499B. doi:10.1038/nature01368. PMID 12556884.

ncbi.nlm.nih.gov

worldcat.org

Petsko, Gregory A. (2004). Protein structure and function. Dagmar Ringe. London: New Science Press. ISBN 0-87893-663-7. OCLC 53181467