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Thermal Shift Assay (German Wikipedia)

Analysis of information sources in references of the Wikipedia article "Thermal Shift Assay" in German language version.

refsWebsite
Global rank German rank
12zdb-katalog.de
123rd place
6th place
12doi.org
2nd place
3rd place
12nih.gov
4th place
7th place

doi.org (Global: 2nd place; German: 3rd place)

  • F. H. Niesen, H. Berglund, M. Vedadi: The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability. In: Nature protocols. Band 2, Nummer 9, 2007, ISSN 1750-2799, S. 2212–2221, doi:10.1038/nprot.2007.321, PMID 17853878.
  • K. R. Rupesh, A. Smith, P. E. Boehmer: Ligand induced stabilization of the melting temperature of the HSV-1 single-strand DNA binding protein using the thermal shift assay. In: Biochemical and biophysical research communications. [elektronische Veröffentlichung vor dem Druck] Nummer 4, November 2014, ISSN 1090-2104, doi:10.1016/j.bbrc.2014.10.145, PMID 25449284, PMC 4254511 (freier Volltext).
  • K. Huynh, C. L. Partch: Analysis of protein stability and ligand interactions by thermal shift assay. In: Current protocols in protein science / editorial board, John E. Coligan.. [et al.]. Band 79, 2015, ISSN 1934-3663, S. 28.9.1–28.9.14, doi:10.1002/0471140864.ps2809s79, PMID 25640896.
  • S. N. Krishna, C. H. Luan, R. K. Mishra, L. Xu, K. A. Scheidt, W. F. Anderson, R. C. Bergan: A fluorescence-based thermal shift assay identifies inhibitors of mitogen activated protein kinase kinase 4. In: PloS one. Band 8, Nummer 12, 2013, ISSN 1932-6203, S. e81504, doi:10.1371/journal.pone.0081504, PMID 24339940, PMC 3855329 (freier Volltext).
  • J. J. Lavinder, S. B. Hari, B. J. Sullivan, T. J. Magliery: High-throughput thermal scanning: a general, rapid dye-binding thermal shift screen for protein engineering. In: Journal of the American Chemical Society. Band 131, Nummer 11, März 2009, ISSN 1520-5126, S. 3794–3795, doi:10.1021/ja8049063, PMID 19292479, PMC 2701314 (freier Volltext).
  • Anders O. Magnusson, Anna Szekrenyi, Henk-Jan Joosten, James Finnigan, Simon Charnock: nanoDSF as screening tool for enzyme libraries and biotechnology development. In: The FEBS Journal. Band 286, Nr. 1, 2019, ISSN 1742-4658, S. 184–204, doi:10.1111/febs.14696.
  • D. Martinez Molina, R. Jafari, M. Ignatushchenko, T. Seki, E. A. Larsson, C. Dan, L. Sreekumar, Y. Cao, P. Nordlund: Monitoring drug target engagement in cells and tissues using the cellular thermal shift assay. In: Science. Band 341, Nummer 6141, Juli 2013, ISSN 1095-9203, S. 84–87, doi:10.1126/science.1233606, PMID 23828940.
  • R. Jafari, H. Almqvist, H. Axelsson, M. Ignatushchenko, T. Lundbäck, P. Nordlund, D. Martinez Molina: The cellular thermal shift assay for evaluating drug target interactions in cells. In: Nature protocols. Band 9, Nummer 9, September 2014, ISSN 1750-2799, S. 2100–2122, doi:10.1038/nprot.2014.138, PMID 25101824.
  • L. Reinhard, H. Mayerhofer, A. Geerlof, J. Mueller-Dieckmann, M. S. Weiss: Optimization of protein buffer cocktails using Thermofluor. In: Acta crystallographica. Section F, Structural biology and crystallization communications. Band 69, Pt 2, Februar 2013, ISSN 1744-3091, S. 209–214, doi:10.1107/S1744309112051858, PMID 23385769, PMC 3564630 (freier Volltext).
  • A. Ciulli, C. Abell: Fragment-based approaches to enzyme inhibition. In: Current Opinion in Biotechnology. Band 18, Nummer 6, Dezember 2007, ISSN 0958-1669, S. 489–496, doi:10.1016/j.copbio.2007.09.003, PMID 17959370.
  • J. K. Kranz, C. Schalk-Hihi: Protein thermal shifts to identify low molecular weight fragments. In: Methods in enzymology. Band 493, 2011, ISSN 1557-7988, S. 277–298, doi:10.1016/B978-0-12-381274-2.00011-X, PMID 21371595.
  • Reinhard L., Mayerhofer H., Geerlof A., Mueller-Dieckmann J., Weiss M.S.: Optimization of protein buffer cocktails using Thermofluor. In: Acta Crystallogr Sect F Struct Biol Cryst Commun. 69. Jahrgang, Nr. 2, Januar 2013, S. 209–214, doi:10.1107/S1744309112051858, PMID 23385769.

nih.gov (Global: 4th place; German: 7th place)

ncbi.nlm.nih.gov

zdb-katalog.de (Global: 123rd place; German: 6th place)

  • F. H. Niesen, H. Berglund, M. Vedadi: The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability. In: Nature protocols. Band 2, Nummer 9, 2007, ISSN 1750-2799, S. 2212–2221, doi:10.1038/nprot.2007.321, PMID 17853878.
  • K. R. Rupesh, A. Smith, P. E. Boehmer: Ligand induced stabilization of the melting temperature of the HSV-1 single-strand DNA binding protein using the thermal shift assay. In: Biochemical and biophysical research communications. [elektronische Veröffentlichung vor dem Druck] Nummer 4, November 2014, ISSN 1090-2104, doi:10.1016/j.bbrc.2014.10.145, PMID 25449284, PMC 4254511 (freier Volltext).
  • K. Huynh, C. L. Partch: Analysis of protein stability and ligand interactions by thermal shift assay. In: Current protocols in protein science / editorial board, John E. Coligan.. [et al.]. Band 79, 2015, ISSN 1934-3663, S. 28.9.1–28.9.14, doi:10.1002/0471140864.ps2809s79, PMID 25640896.
  • S. N. Krishna, C. H. Luan, R. K. Mishra, L. Xu, K. A. Scheidt, W. F. Anderson, R. C. Bergan: A fluorescence-based thermal shift assay identifies inhibitors of mitogen activated protein kinase kinase 4. In: PloS one. Band 8, Nummer 12, 2013, ISSN 1932-6203, S. e81504, doi:10.1371/journal.pone.0081504, PMID 24339940, PMC 3855329 (freier Volltext).
  • Daniel E. Koshland: Application of a Theory of Enzyme Specificity to Protein Synthesis. In: Proceedings of the National Academy of Sciences. Band 44, Nummer 2, Februar 1958, ISSN 0027-8424, S. 98–104, PMID 16590179, PMC 335371 (freier Volltext).
  • J. J. Lavinder, S. B. Hari, B. J. Sullivan, T. J. Magliery: High-throughput thermal scanning: a general, rapid dye-binding thermal shift screen for protein engineering. In: Journal of the American Chemical Society. Band 131, Nummer 11, März 2009, ISSN 1520-5126, S. 3794–3795, doi:10.1021/ja8049063, PMID 19292479, PMC 2701314 (freier Volltext).
  • Anders O. Magnusson, Anna Szekrenyi, Henk-Jan Joosten, James Finnigan, Simon Charnock: nanoDSF as screening tool for enzyme libraries and biotechnology development. In: The FEBS Journal. Band 286, Nr. 1, 2019, ISSN 1742-4658, S. 184–204, doi:10.1111/febs.14696.
  • D. Martinez Molina, R. Jafari, M. Ignatushchenko, T. Seki, E. A. Larsson, C. Dan, L. Sreekumar, Y. Cao, P. Nordlund: Monitoring drug target engagement in cells and tissues using the cellular thermal shift assay. In: Science. Band 341, Nummer 6141, Juli 2013, ISSN 1095-9203, S. 84–87, doi:10.1126/science.1233606, PMID 23828940.
  • R. Jafari, H. Almqvist, H. Axelsson, M. Ignatushchenko, T. Lundbäck, P. Nordlund, D. Martinez Molina: The cellular thermal shift assay for evaluating drug target interactions in cells. In: Nature protocols. Band 9, Nummer 9, September 2014, ISSN 1750-2799, S. 2100–2122, doi:10.1038/nprot.2014.138, PMID 25101824.
  • L. Reinhard, H. Mayerhofer, A. Geerlof, J. Mueller-Dieckmann, M. S. Weiss: Optimization of protein buffer cocktails using Thermofluor. In: Acta crystallographica. Section F, Structural biology and crystallization communications. Band 69, Pt 2, Februar 2013, ISSN 1744-3091, S. 209–214, doi:10.1107/S1744309112051858, PMID 23385769, PMC 3564630 (freier Volltext).
  • A. Ciulli, C. Abell: Fragment-based approaches to enzyme inhibition. In: Current Opinion in Biotechnology. Band 18, Nummer 6, Dezember 2007, ISSN 0958-1669, S. 489–496, doi:10.1016/j.copbio.2007.09.003, PMID 17959370.
  • J. K. Kranz, C. Schalk-Hihi: Protein thermal shifts to identify low molecular weight fragments. In: Methods in enzymology. Band 493, 2011, ISSN 1557-7988, S. 277–298, doi:10.1016/B978-0-12-381274-2.00011-X, PMID 21371595.