The Immunomodulatory Activity of Peptides Related to the DNA Contacting Loop of p53 Protein
Taking into account the sequence homology existing between thymopoietin II and the DNA-binding domain of p53 protein, a series of octapeptides was synthesized, related to the wild p53 type protein as well as to its mutated forms, appearing in some human tumours. The wild type octapeptide has immunos...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
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| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
1996 |
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| Umfang: |
1 Ill. ; 5 Tab. 7 |
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| Reproduktion: |
Wiley InterScience Backfile Collection 1832-2000 |
|---|---|
| Übergeordnetes Werk: |
in: Journal of Peptide Science - New York, NY [u.a.] : Wiley, 2(1996) vom: Mai, Seite 318-324 |
| Übergeordnetes Werk: |
volume:2 ; year:1996 ; month:05 ; pages:318-324 ; extent:7 |
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NLEJ159433290 |
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| 520 | |a Taking into account the sequence homology existing between thymopoietin II and the DNA-binding domain of p53 protein, a series of octapeptides was synthesized, related to the wild p53 type protein as well as to its mutated forms, appearing in some human tumours. The wild type octapeptide has immunostimulative activity with regard to the humoral immune response, but is inactive in the cellular immune response. The mutated peptides of p53 differ in their immunomodulatory activity from the wild type octapeptide. The Ser5 analogue of the wild type peptide is a strong stimulant of the humoral immune response and enhances TNF-α production, while at the same time suppressing the cellular immune response. The data suggest that the mutations of p53, which favour tumour development and growth, may also change the immune activity of respective p53 fragments. | ||
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(DE-627)NLEJ159433290 DE-627 ger DE-627 rakwb eng The Immunomodulatory Activity of Peptides Related to the DNA Contacting Loop of p53 Protein 1996 1 Ill. 5 Tab. 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Taking into account the sequence homology existing between thymopoietin II and the DNA-binding domain of p53 protein, a series of octapeptides was synthesized, related to the wild p53 type protein as well as to its mutated forms, appearing in some human tumours. The wild type octapeptide has immunostimulative activity with regard to the humoral immune response, but is inactive in the cellular immune response. The mutated peptides of p53 differ in their immunomodulatory activity from the wild type octapeptide. The Ser5 analogue of the wild type peptide is a strong stimulant of the humoral immune response and enhances TNF-α production, while at the same time suppressing the cellular immune response. The data suggest that the mutations of p53, which favour tumour development and growth, may also change the immune activity of respective p53 fragments. Wiley InterScience Backfile Collection 1832-2000 Bolewska-Pedyczak, Eleonora oth Siemion, Ignacy Z. oth Wieczorek, Zbigniew oth in Journal of Peptide Science New York, NY [u.a.] : Wiley 2(1996) vom: Mai, Seite 318-324 (DE-627)NLEJ159070635 (DE-600)1491819-5 1075-2617 nnns volume:2 year:1996 month:05 pages:318-324 extent:7 http://dx.doi.org/10.1002/psc.68 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 2 1996 5 318-324 7 |
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(DE-627)NLEJ159433290 DE-627 ger DE-627 rakwb eng The Immunomodulatory Activity of Peptides Related to the DNA Contacting Loop of p53 Protein 1996 1 Ill. 5 Tab. 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Taking into account the sequence homology existing between thymopoietin II and the DNA-binding domain of p53 protein, a series of octapeptides was synthesized, related to the wild p53 type protein as well as to its mutated forms, appearing in some human tumours. The wild type octapeptide has immunostimulative activity with regard to the humoral immune response, but is inactive in the cellular immune response. The mutated peptides of p53 differ in their immunomodulatory activity from the wild type octapeptide. The Ser5 analogue of the wild type peptide is a strong stimulant of the humoral immune response and enhances TNF-α production, while at the same time suppressing the cellular immune response. The data suggest that the mutations of p53, which favour tumour development and growth, may also change the immune activity of respective p53 fragments. Wiley InterScience Backfile Collection 1832-2000 Bolewska-Pedyczak, Eleonora oth Siemion, Ignacy Z. oth Wieczorek, Zbigniew oth in Journal of Peptide Science New York, NY [u.a.] : Wiley 2(1996) vom: Mai, Seite 318-324 (DE-627)NLEJ159070635 (DE-600)1491819-5 1075-2617 nnns volume:2 year:1996 month:05 pages:318-324 extent:7 http://dx.doi.org/10.1002/psc.68 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 2 1996 5 318-324 7 |
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(DE-627)NLEJ159433290 DE-627 ger DE-627 rakwb eng The Immunomodulatory Activity of Peptides Related to the DNA Contacting Loop of p53 Protein 1996 1 Ill. 5 Tab. 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Taking into account the sequence homology existing between thymopoietin II and the DNA-binding domain of p53 protein, a series of octapeptides was synthesized, related to the wild p53 type protein as well as to its mutated forms, appearing in some human tumours. The wild type octapeptide has immunostimulative activity with regard to the humoral immune response, but is inactive in the cellular immune response. The mutated peptides of p53 differ in their immunomodulatory activity from the wild type octapeptide. The Ser5 analogue of the wild type peptide is a strong stimulant of the humoral immune response and enhances TNF-α production, while at the same time suppressing the cellular immune response. The data suggest that the mutations of p53, which favour tumour development and growth, may also change the immune activity of respective p53 fragments. Wiley InterScience Backfile Collection 1832-2000 Bolewska-Pedyczak, Eleonora oth Siemion, Ignacy Z. oth Wieczorek, Zbigniew oth in Journal of Peptide Science New York, NY [u.a.] : Wiley 2(1996) vom: Mai, Seite 318-324 (DE-627)NLEJ159070635 (DE-600)1491819-5 1075-2617 nnns volume:2 year:1996 month:05 pages:318-324 extent:7 http://dx.doi.org/10.1002/psc.68 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 2 1996 5 318-324 7 |
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(DE-627)NLEJ159433290 DE-627 ger DE-627 rakwb eng The Immunomodulatory Activity of Peptides Related to the DNA Contacting Loop of p53 Protein 1996 1 Ill. 5 Tab. 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Taking into account the sequence homology existing between thymopoietin II and the DNA-binding domain of p53 protein, a series of octapeptides was synthesized, related to the wild p53 type protein as well as to its mutated forms, appearing in some human tumours. The wild type octapeptide has immunostimulative activity with regard to the humoral immune response, but is inactive in the cellular immune response. The mutated peptides of p53 differ in their immunomodulatory activity from the wild type octapeptide. The Ser5 analogue of the wild type peptide is a strong stimulant of the humoral immune response and enhances TNF-α production, while at the same time suppressing the cellular immune response. The data suggest that the mutations of p53, which favour tumour development and growth, may also change the immune activity of respective p53 fragments. Wiley InterScience Backfile Collection 1832-2000 Bolewska-Pedyczak, Eleonora oth Siemion, Ignacy Z. oth Wieczorek, Zbigniew oth in Journal of Peptide Science New York, NY [u.a.] : Wiley 2(1996) vom: Mai, Seite 318-324 (DE-627)NLEJ159070635 (DE-600)1491819-5 1075-2617 nnns volume:2 year:1996 month:05 pages:318-324 extent:7 http://dx.doi.org/10.1002/psc.68 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 2 1996 5 318-324 7 |
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the immunomodulatory activity of peptides related to the dna contacting loop of p53 protein |
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The Immunomodulatory Activity of Peptides Related to the DNA Contacting Loop of p53 Protein |
| abstract |
Taking into account the sequence homology existing between thymopoietin II and the DNA-binding domain of p53 protein, a series of octapeptides was synthesized, related to the wild p53 type protein as well as to its mutated forms, appearing in some human tumours. The wild type octapeptide has immunostimulative activity with regard to the humoral immune response, but is inactive in the cellular immune response. The mutated peptides of p53 differ in their immunomodulatory activity from the wild type octapeptide. The Ser5 analogue of the wild type peptide is a strong stimulant of the humoral immune response and enhances TNF-α production, while at the same time suppressing the cellular immune response. The data suggest that the mutations of p53, which favour tumour development and growth, may also change the immune activity of respective p53 fragments. |
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Taking into account the sequence homology existing between thymopoietin II and the DNA-binding domain of p53 protein, a series of octapeptides was synthesized, related to the wild p53 type protein as well as to its mutated forms, appearing in some human tumours. The wild type octapeptide has immunostimulative activity with regard to the humoral immune response, but is inactive in the cellular immune response. The mutated peptides of p53 differ in their immunomodulatory activity from the wild type octapeptide. The Ser5 analogue of the wild type peptide is a strong stimulant of the humoral immune response and enhances TNF-α production, while at the same time suppressing the cellular immune response. The data suggest that the mutations of p53, which favour tumour development and growth, may also change the immune activity of respective p53 fragments. |
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Taking into account the sequence homology existing between thymopoietin II and the DNA-binding domain of p53 protein, a series of octapeptides was synthesized, related to the wild p53 type protein as well as to its mutated forms, appearing in some human tumours. The wild type octapeptide has immunostimulative activity with regard to the humoral immune response, but is inactive in the cellular immune response. The mutated peptides of p53 differ in their immunomodulatory activity from the wild type octapeptide. The Ser5 analogue of the wild type peptide is a strong stimulant of the humoral immune response and enhances TNF-α production, while at the same time suppressing the cellular immune response. The data suggest that the mutations of p53, which favour tumour development and growth, may also change the immune activity of respective p53 fragments. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ159433290</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707005946.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070201s1996 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ159433290</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">The Immunomodulatory Activity of Peptides Related to the DNA Contacting Loop of p53 Protein</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1996</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="b">1 Ill.</subfield><subfield code="b">5 Tab.</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">7</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Taking into account the sequence homology existing between thymopoietin II and the DNA-binding domain of p53 protein, a series of octapeptides was synthesized, related to the wild p53 type protein as well as to its mutated forms, appearing in some human tumours. The wild type octapeptide has immunostimulative activity with regard to the humoral immune response, but is inactive in the cellular immune response. The mutated peptides of p53 differ in their immunomodulatory activity from the wild type octapeptide. The Ser5 analogue of the wild type peptide is a strong stimulant of the humoral immune response and enhances TNF-α production, while at the same time suppressing the cellular immune response. The data suggest that the mutations of p53, which favour tumour development and growth, may also change the immune activity of respective p53 fragments.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Wiley InterScience Backfile Collection 1832-2000</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Bolewska-Pedyczak, Eleonora</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Siemion, Ignacy Z.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Wieczorek, Zbigniew</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Journal of Peptide Science</subfield><subfield code="d">New York, NY [u.a.] : Wiley</subfield><subfield code="g">2(1996) vom: Mai, Seite 318-324</subfield><subfield code="w">(DE-627)NLEJ159070635</subfield><subfield code="w">(DE-600)1491819-5</subfield><subfield code="x">1075-2617</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:2</subfield><subfield code="g">year:1996</subfield><subfield code="g">month:05</subfield><subfield code="g">pages:318-324</subfield><subfield code="g">extent:7</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1002/psc.68</subfield><subfield code="q">text/html</subfield><subfield code="z">Deutschlandweit zugänglich</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-WIS</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">2</subfield><subfield code="j">1996</subfield><subfield code="c">5</subfield><subfield code="h">318-324</subfield><subfield code="g">7</subfield></datafield></record></collection>
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7.40108 |