Fosforylácia (Slovak Wikipedia)

Analysis of information sources in references of the Wikipedia article "Fosforylácia" in Slovak language version.

refsWebsite

Global rank Slovak rank

23nih.gov

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17doi.org

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4web.archive.org

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3jbc.org

4,455^th place

4,034^th place

1biologists.com

low place

1exactantigen.com

low place

1worldcat.org

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1^st place

biologists.com

journals.biologists.com

Eukaryotic signal transduction via histidine-aspartate phosphorelay. J. Cell. Sci., September 2000, s. 3141–50. Dostupné online. PMID 10954413.

doi.org

dx.doi.org

Cozzone AJ. Protein phosphorylation in prokaryotes. Annu. Rev. Microbiol., 1988, s. 97–125. DOI: 10.1146/annurev.mi.42.100188.000525. PMID 2849375.
The Two-Component System . Regulation of Diverse Signaling Pathways in Prokaryotes and Eukaryotes. Plant Physiol., July 1998, s. 723–31. DOI: 10.1104/PPSOE.117.3.723. PMID 9662515.
The structure and mechanism of protein phosphatases: insights into catalysis and regulation. Annu Rev Biophys Biomol Struct, 1998, s. 133–64. DOI: 10.1146/annurev.biophys.27.1.133. PMID 9646865.
Ser/Thr/Tyr protein phosphorylation in bacteria - for long time neglected, now well established. J Mol Microbiol Biotechnol, 2005, s. 125–31. DOI: 10.1159/000089641. PMID 16415586.
p53 in signaling checkpoint arrest or apoptosis. Curr. Opin. Genet. Dev., February 1996, s. 12–8. DOI: 10.1016/S0959-437X(96)90004-0. PMID 8791489.
Essential role for protein kinase B (PKB) in insulin-induced glycogen synthase kinase 3 inactivation. Characterization of dominant-negative mutant of PKB. J. Biol. Chem., May 1998, s. 13150–6. DOI: 10.1074/jbc.273.21.13150. PMID 9582355.
Protein tyrosine kinases Src and Csk: a tail's tale. Curr Opin Chem Biol, October 2003, s. 580–5. DOI: 10.1016/j.cbpa.2003.08.009. PMID 14580561.
Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell, November 2006, s. 635–48. DOI: 10.1016/j.cell.2006.09.026. PMID 17081983.
Phosphoproteomics for the discovery of kinases as cancer biomarkers and drug targets. Proteomics - Clinical Applications, 2007, s. 1042–1057. DOI: 10.1002/prca.200700102. PMID 21136756.
Functional Organization of the S. cerevisiae Phosphorylation Network. Cell, 2009, s. 952–963. DOI: 10.1016/j.cell.2008.12.039. PMID 19269370.
KOVACS KA, Steinmann M, Magistretti PJ, Halfon O, Cardinaux JR CCAAT/enhancer-binding protein family members recruit the coactivator CREB-binding protein and trigger its phosphorylation. J Biol. Chem. (UNITED STATES), Sept. 2003, s. 36959–65. ISSN 0021-9258. DOI: 10.1074/jbc.M303147200. PMID 12857754.
Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations. Mol. Cell Proteomics, February 2007, s. 283–93. DOI: 10.1074/mcp.M600046-MCP200. PMID 17114649.
Quantitative analysis of synaptic phosphorylation and protein expression. Mol. Cell Proteomics, April 2008, s. 684–96. DOI: 10.1074/mcp.M700170-MCP200. PMID 18056256.
Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS. Proc. Natl. Acad. Sci. U.S.A., June 2003, s. 6940–5. DOI: 10.1073/pnas.0832254100. PMID 12771378.
Proteome analysis of low-abundance proteins using multidimensional chromatography and isotope-coded affinity tags. J. Proteome Res., 2002, s. 47–54. DOI: 10.1021/pr015509n. PMID 12643526.
Olive DM. Quantitative methods for the analysis of protein phosphorylation in drug development. Expert Rev Proteomics, October 2004, s. 327–41. DOI: 10.1586/14789450.1.3.327. PMID 15966829.
A cell-based immunocytockemical assay for monitoring kinase signaling pathways and drug efficacy. Anal. Biochem., March 2005, s. 136–42. DOI: 10.1016/j.ab.2004.11.015. PMID 15707944.

exactantigen.com

phospho antibody [online]. [Cit. 2009-01-22]. Dostupné online. Archivované 2009-12-07 z originálu.

jbc.org

The cleavage products of vitellin. J. Biol. Chem., 1906, s. 127–133. Dostupné online. Archivované 2020-06-09 na Wayback Machine
Serinephosphoric acid obtained on hydrolysis of vitellinic acid. J. Biol. Chem., October 1932, s. 109–114. Dostupné online. Archivované 2020-06-09 na Wayback Machine
The enzymatic phosphorylation of proteins. J. Biol. Chem., December 1954, s. 969–80. Dostupné online. PMID 13221602. Archivované 2020-06-09 na Wayback Machine

nih.gov

ncbi.nlm.nih.gov

The enzymatic phosphorylation of proteins. J. Biol. Chem., December 1954, s. 969–80. Dostupné online. PMID 13221602. Archivované 2020-06-09 na Wayback Machine
Cozzone AJ. Protein phosphorylation in prokaryotes. Annu. Rev. Microbiol., 1988, s. 97–125. DOI: 10.1146/annurev.mi.42.100188.000525. PMID 2849375.
Protein phosphorylation and regulation of adaptive responses in bacteria. Microbiol. Rev., December 1989, s. 450–90. PMID 2556636.
The Two-Component System . Regulation of Diverse Signaling Pathways in Prokaryotes and Eukaryotes. Plant Physiol., July 1998, s. 723–31. DOI: 10.1104/PPSOE.117.3.723. PMID 9662515.
The structure and mechanism of protein phosphatases: insights into catalysis and regulation. Annu Rev Biophys Biomol Struct, 1998, s. 133–64. DOI: 10.1146/annurev.biophys.27.1.133. PMID 9646865.
Phosphorylation of basic amino acid residues in proteins: important but easily missed. Acta Biochim Pol, 2011, s. 137–47. PMID 21623415.
Ser/Thr/Tyr protein phosphorylation in bacteria - for long time neglected, now well established. J Mol Microbiol Biotechnol, 2005, s. 125–31. DOI: 10.1159/000089641. PMID 16415586.
Regulation of p53 Function and Stability by Phosphorylation. Mol. Cell. Biol., March 1999, s. 1751–8. PMID 10022862.
p53 in signaling checkpoint arrest or apoptosis. Curr. Opin. Genet. Dev., February 1996, s. 12–8. DOI: 10.1016/S0959-437X(96)90004-0. PMID 8791489.
Essential role for protein kinase B (PKB) in insulin-induced glycogen synthase kinase 3 inactivation. Characterization of dominant-negative mutant of PKB. J. Biol. Chem., May 1998, s. 13150–6. DOI: 10.1074/jbc.273.21.13150. PMID 9582355.
Protein tyrosine kinases Src and Csk: a tail's tale. Curr Opin Chem Biol, October 2003, s. 580–5. DOI: 10.1016/j.cbpa.2003.08.009. PMID 14580561.
Babior BM. NADPH oxidase: an update. Blood, March 1999, s. 1464–76. PMID 10029572.
Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell, November 2006, s. 635–48. DOI: 10.1016/j.cell.2006.09.026. PMID 17081983.
Phosphoproteomics for the discovery of kinases as cancer biomarkers and drug targets. Proteomics - Clinical Applications, 2007, s. 1042–1057. DOI: 10.1002/prca.200700102. PMID 21136756.
Functional Organization of the S. cerevisiae Phosphorylation Network. Cell, 2009, s. 952–963. DOI: 10.1016/j.cell.2008.12.039. PMID 19269370.
Eukaryotic signal transduction via histidine-aspartate phosphorelay. J. Cell. Sci., September 2000, s. 3141–50. Dostupné online. PMID 10954413.
KOVACS KA, Steinmann M, Magistretti PJ, Halfon O, Cardinaux JR CCAAT/enhancer-binding protein family members recruit the coactivator CREB-binding protein and trigger its phosphorylation. J Biol. Chem. (UNITED STATES), Sept. 2003, s. 36959–65. ISSN 0021-9258. DOI: 10.1074/jbc.M303147200. PMID 12857754.
Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations. Mol. Cell Proteomics, February 2007, s. 283–93. DOI: 10.1074/mcp.M600046-MCP200. PMID 17114649.
Quantitative analysis of synaptic phosphorylation and protein expression. Mol. Cell Proteomics, April 2008, s. 684–96. DOI: 10.1074/mcp.M700170-MCP200. PMID 18056256.
Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS. Proc. Natl. Acad. Sci. U.S.A., June 2003, s. 6940–5. DOI: 10.1073/pnas.0832254100. PMID 12771378.
Proteome analysis of low-abundance proteins using multidimensional chromatography and isotope-coded affinity tags. J. Proteome Res., 2002, s. 47–54. DOI: 10.1021/pr015509n. PMID 12643526.
Olive DM. Quantitative methods for the analysis of protein phosphorylation in drug development. Expert Rev Proteomics, October 2004, s. 327–41. DOI: 10.1586/14789450.1.3.327. PMID 15966829.
A cell-based immunocytockemical assay for monitoring kinase signaling pathways and drug efficacy. Anal. Biochem., March 2005, s. 136–42. DOI: 10.1016/j.ab.2004.11.015. PMID 15707944.

web.archive.org

The cleavage products of vitellin. J. Biol. Chem., 1906, s. 127–133. Dostupné online. Archivované 2020-06-09 na Wayback Machine
Serinephosphoric acid obtained on hydrolysis of vitellinic acid. J. Biol. Chem., October 1932, s. 109–114. Dostupné online. Archivované 2020-06-09 na Wayback Machine
The enzymatic phosphorylation of proteins. J. Biol. Chem., December 1954, s. 969–80. Dostupné online. PMID 13221602. Archivované 2020-06-09 na Wayback Machine
phospho antibody [online]. [Cit. 2009-01-22]. Dostupné online. Archivované 2009-12-07 z originálu.

worldcat.org

KOVACS KA, Steinmann M, Magistretti PJ, Halfon O, Cardinaux JR CCAAT/enhancer-binding protein family members recruit the coactivator CREB-binding protein and trigger its phosphorylation. J Biol. Chem. (UNITED STATES), Sept. 2003, s. 36959–65. ISSN 0021-9258. DOI: 10.1074/jbc.M303147200. PMID 12857754.