Einzeldomänenantikörper (German Wikipedia)

Analysis of information sources in references of the Wikipedia article "Einzeldomänenantikörper" in German language version.

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doi.org

  • Harmsen MM, van Solt CB, Hoogendoorn A, van Zijderveld FG, Niewold TA, van der Meulen J: Escherichia coli F4 fimbriae specific llama single-domain antibody fragments effectively inhibit bacterial adhesion in vitro but poorly protect against diarrhoea. In: Vet. Microbiol. 111. Jahrgang, Nr. 1–2, November 2005, S. 89–98, doi:10.1016/j.vetmic.2005.09.005, PMID 16221532 (elsevier.com).
  • Harmsen MM, van Solt CB, van Zijderveld-van Bemmel AM, Niewold TA, van Zijderveld FG: Selection and optimization of proteolytically stable llama single-domain antibody fragments for oral immunotherapy. In: Appl. Microbiol. Biotechnol. 72. Jahrgang, Nr. 3, September 2006, S. 544–51, doi:10.1007/s00253-005-0300-7, PMID 16450109.
  • Dolk E, van der Vaart M, Lutje Hulsik D, et al.: Isolation of llama antibody fragments for prevention of dandruff by phage display in shampoo. In: Appl. Environ. Microbiol. 71. Jahrgang, Nr. 1, Januar 2005, S. 442–50, doi:10.1128/AEM.71.1.442-450.2005, PMID 15640220, PMC 544197 (freier Volltext).
  • Harmsen MM, De Haard HJ: Properties, production, and applications of camelid single-domain antibody fragments. In: Appl. Microbiol. Biotechnol. 77. Jahrgang, Nr. 1, November 2007, S. 13–22, doi:10.1007/s00253-007-1142-2, PMID 17704915, PMC 2039825 (freier Volltext).
  • Jähnichen S, Blanchetot C, Maussang D, et al.: CXCR4 nanobodies (VHH-based single variable domains) potently inhibit chemotaxis and HIV-1 replication and mobilize stem cells. In: Proc. Natl. Acad. Sci. USA. 107. Jahrgang, Nr. 47, November 2010, S. 20565–70, doi:10.1073/pnas.1012865107, PMID 21059953, PMC 2996674 (freier Volltext).
  • Saerens D, Ghassabeh GH, Muyldermans S: Single-domain antibodies as building blocks for novel therapeutics. In: Curr Opin Pharmacol. 8. Jahrgang, Nr. 5, Oktober 2008, S. 600–8, doi:10.1016/j.coph.2008.07.006, PMID 18691671 (elsevier.com).
  • Borrebaeck CA, Ohlin M: Antibody evolution beyond Nature. In: Nat. Biotechnol. 20. Jahrgang, Nr. 12, Dezember 2002, S. 1189–90, doi:10.1038/nbt1202-1189, PMID 12454662.
  • Hamers-Casterman C, Atarhouch T, Muyldermans S, et al.: Naturally occurring antibodies devoid of light chains. In: Nature. 363. Jahrgang, Nr. 6428, Juni 1993, S. 446–8, doi:10.1038/363446a0, PMID 8502296.
  • Greenberg AS, Avila D, Hughes M, Hughes A, McKinney EC, Flajnik MF: A new antigen receptor gene family that undergoes rearrangement and extensive somatic diversification in sharks. In: Nature. 374. Jahrgang, Nr. 6518, März 1995, S. 168–73, doi:10.1038/374168a0, PMID 7877689.

elsevier.com

linkinghub.elsevier.com

  • van der Linden RH, Frenken LG, de Geus B, et al.: Comparison of physical chemical properties of llama VHH antibody fragments and mouse monoclonal antibodies. In: Biochim. Biophys. Acta. 1431. Jahrgang, Nr. 1, April 1999, S. 37–46, PMID 10209277 (elsevier.com).
  • Harmsen MM, van Solt CB, Hoogendoorn A, van Zijderveld FG, Niewold TA, van der Meulen J: Escherichia coli F4 fimbriae specific llama single-domain antibody fragments effectively inhibit bacterial adhesion in vitro but poorly protect against diarrhoea. In: Vet. Microbiol. 111. Jahrgang, Nr. 1–2, November 2005, S. 89–98, doi:10.1016/j.vetmic.2005.09.005, PMID 16221532 (elsevier.com).
  • Ghahroudi MA, Desmyter A, Wyns L, Hamers R, Muyldermans S: Selection and identification of single domain antibody fragments from camel heavy-chain antibodies. In: FEBS Lett. 414. Jahrgang, Nr. 3, September 1997, S. 521–6, PMID 9323027 (elsevier.com).
  • Saerens D, Ghassabeh GH, Muyldermans S: Single-domain antibodies as building blocks for novel therapeutics. In: Curr Opin Pharmacol. 8. Jahrgang, Nr. 5, Oktober 2008, S. 600–8, doi:10.1016/j.coph.2008.07.006, PMID 18691671 (elsevier.com).
  • Holt LJ, Herring C, Jespers LS, Woolven BP, Tomlinson IM: Domain antibodies: proteins for therapy. In: Trends Biotechnol. 21. Jahrgang, Nr. 11, November 2003, S. 484–90, PMID 14573361 (elsevier.com).

nih.gov

ncbi.nlm.nih.gov

  • van der Linden RH, Frenken LG, de Geus B, et al.: Comparison of physical chemical properties of llama VHH antibody fragments and mouse monoclonal antibodies. In: Biochim. Biophys. Acta. 1431. Jahrgang, Nr. 1, April 1999, S. 37–46, PMID 10209277 (elsevier.com).
  • Harmsen MM, van Solt CB, Hoogendoorn A, van Zijderveld FG, Niewold TA, van der Meulen J: Escherichia coli F4 fimbriae specific llama single-domain antibody fragments effectively inhibit bacterial adhesion in vitro but poorly protect against diarrhoea. In: Vet. Microbiol. 111. Jahrgang, Nr. 1–2, November 2005, S. 89–98, doi:10.1016/j.vetmic.2005.09.005, PMID 16221532 (elsevier.com).
  • Harmsen MM, van Solt CB, van Zijderveld-van Bemmel AM, Niewold TA, van Zijderveld FG: Selection and optimization of proteolytically stable llama single-domain antibody fragments for oral immunotherapy. In: Appl. Microbiol. Biotechnol. 72. Jahrgang, Nr. 3, September 2006, S. 544–51, doi:10.1007/s00253-005-0300-7, PMID 16450109.
  • Dolk E, van der Vaart M, Lutje Hulsik D, et al.: Isolation of llama antibody fragments for prevention of dandruff by phage display in shampoo. In: Appl. Environ. Microbiol. 71. Jahrgang, Nr. 1, Januar 2005, S. 442–50, doi:10.1128/AEM.71.1.442-450.2005, PMID 15640220, PMC 544197 (freier Volltext).
  • Harmsen MM, De Haard HJ: Properties, production, and applications of camelid single-domain antibody fragments. In: Appl. Microbiol. Biotechnol. 77. Jahrgang, Nr. 1, November 2007, S. 13–22, doi:10.1007/s00253-007-1142-2, PMID 17704915, PMC 2039825 (freier Volltext).
  • Jähnichen S, Blanchetot C, Maussang D, et al.: CXCR4 nanobodies (VHH-based single variable domains) potently inhibit chemotaxis and HIV-1 replication and mobilize stem cells. In: Proc. Natl. Acad. Sci. USA. 107. Jahrgang, Nr. 47, November 2010, S. 20565–70, doi:10.1073/pnas.1012865107, PMID 21059953, PMC 2996674 (freier Volltext).
  • Ghahroudi MA, Desmyter A, Wyns L, Hamers R, Muyldermans S: Selection and identification of single domain antibody fragments from camel heavy-chain antibodies. In: FEBS Lett. 414. Jahrgang, Nr. 3, September 1997, S. 521–6, PMID 9323027 (elsevier.com).
  • Saerens D, Ghassabeh GH, Muyldermans S: Single-domain antibodies as building blocks for novel therapeutics. In: Curr Opin Pharmacol. 8. Jahrgang, Nr. 5, Oktober 2008, S. 600–8, doi:10.1016/j.coph.2008.07.006, PMID 18691671 (elsevier.com).
  • Holt LJ, Herring C, Jespers LS, Woolven BP, Tomlinson IM: Domain antibodies: proteins for therapy. In: Trends Biotechnol. 21. Jahrgang, Nr. 11, November 2003, S. 484–90, PMID 14573361 (elsevier.com).
  • Borrebaeck CA, Ohlin M: Antibody evolution beyond Nature. In: Nat. Biotechnol. 20. Jahrgang, Nr. 12, Dezember 2002, S. 1189–90, doi:10.1038/nbt1202-1189, PMID 12454662.
  • Hamers-Casterman C, Atarhouch T, Muyldermans S, et al.: Naturally occurring antibodies devoid of light chains. In: Nature. 363. Jahrgang, Nr. 6428, Juni 1993, S. 446–8, doi:10.1038/363446a0, PMID 8502296.
  • Greenberg AS, Avila D, Hughes M, Hughes A, McKinney EC, Flajnik MF: A new antigen receptor gene family that undergoes rearrangement and extensive somatic diversification in sharks. In: Nature. 374. Jahrgang, Nr. 6518, März 1995, S. 168–73, doi:10.1038/374168a0, PMID 7877689.
  • Muyldermans S, Atarhouch T, Saldanha J, Barbosa JA, Hamers R: Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chains. In: Protein Eng. 7. Jahrgang, Nr. 9, September 1994, S. 1129–35, PMID 7831284.

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