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An active twenty-amino-acid-residue peptide derived from the inhibitor protein of the cyclic AMP-dependent protein kinase
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| Zeitschriftentitel: | Biochemical Journal |
|---|---|
| Personen und Körperschaften: | , , , |
| In: | Biochemical Journal, 231, 1985, 3, S. 655-661 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Portland Press Ltd.
|
| Schlagwörter: |
| author_facet |
Cheng, H C van Patten, S M Smith, A J Walsh, D A Cheng, H C van Patten, S M Smith, A J Walsh, D A |
|---|---|
| author |
Cheng, H C van Patten, S M Smith, A J Walsh, D A |
| spellingShingle |
Cheng, H C van Patten, S M Smith, A J Walsh, D A Biochemical Journal An active twenty-amino-acid-residue peptide derived from the inhibitor protein of the cyclic AMP-dependent protein kinase Cell Biology Molecular Biology Biochemistry |
| author_sort |
cheng, h c |
| spelling |
Cheng, H C van Patten, S M Smith, A J Walsh, D A 0264-6021 1470-8728 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1042/bj2310655 <jats:p>Digestion with Staphylococcus aureus V8 proteinase of the inhibitor protein of the cyclic AMP-dependent protein kinase results in the sequential formation of three active inhibitory peptides. The smallest active peptide has the sequence Thr-Thr-Tyr-Ala-Asp-Phe-Ile-Ala-Ser-Gly-Arg-Thr-Gly-Arg-Arg-Asn-Ala-Ile- His-Asp . This 20-amino-acid-residue peptide has 20-40% of the activity of the native molecule and a Ki of 0.2 nM. Inhibition, as a minimum, appears to be based upon the inhibitor protein containing the recognition sequences that dictate protein-substrate-specificity. This inhibitory peptide also has sequence homology with the phosphorylation site for a protein kinase other than the cyclic AMP-dependent enzyme.</jats:p> An active twenty-amino-acid-residue peptide derived from the inhibitor protein of the cyclic AMP-dependent protein kinase Biochemical Journal |
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10.1042/bj2310655 |
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Online Free |
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Biologie Chemie und Pharmazie |
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| imprint |
Portland Press Ltd., 1985 |
| imprint_str_mv |
Portland Press Ltd., 1985 |
| issn |
0264-6021 1470-8728 |
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0264-6021 1470-8728 |
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English |
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Portland Press Ltd. (CrossRef) |
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cheng1985anactivetwentyaminoacidresiduepeptidederivedfromtheinhibitorproteinofthecyclicampdependentproteinkinase |
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1985 |
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Portland Press Ltd. |
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ai |
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ai |
| series |
Biochemical Journal |
| source_id |
49 |
| title |
An active twenty-amino-acid-residue peptide derived from the inhibitor protein of the cyclic AMP-dependent protein kinase |
| title_unstemmed |
An active twenty-amino-acid-residue peptide derived from the inhibitor protein of the cyclic AMP-dependent protein kinase |
| title_full |
An active twenty-amino-acid-residue peptide derived from the inhibitor protein of the cyclic AMP-dependent protein kinase |
| title_fullStr |
An active twenty-amino-acid-residue peptide derived from the inhibitor protein of the cyclic AMP-dependent protein kinase |
| title_full_unstemmed |
An active twenty-amino-acid-residue peptide derived from the inhibitor protein of the cyclic AMP-dependent protein kinase |
| title_short |
An active twenty-amino-acid-residue peptide derived from the inhibitor protein of the cyclic AMP-dependent protein kinase |
| title_sort |
an active twenty-amino-acid-residue peptide derived from the inhibitor protein of the cyclic amp-dependent protein kinase |
| topic |
Cell Biology Molecular Biology Biochemistry |
| url |
http://dx.doi.org/10.1042/bj2310655 |
| publishDate |
1985 |
| physical |
655-661 |
| description |
<jats:p>Digestion with Staphylococcus aureus V8 proteinase of the inhibitor protein of the cyclic AMP-dependent protein kinase results in the sequential formation of three active inhibitory peptides. The smallest active peptide has the sequence Thr-Thr-Tyr-Ala-Asp-Phe-Ile-Ala-Ser-Gly-Arg-Thr-Gly-Arg-Arg-Asn-Ala-Ile- His-Asp . This 20-amino-acid-residue peptide has 20-40% of the activity of the native molecule and a Ki of 0.2 nM. Inhibition, as a minimum, appears to be based upon the inhibitor protein containing the recognition sequences that dictate protein-substrate-specificity. This inhibitory peptide also has sequence homology with the phosphorylation site for a protein kinase other than the cyclic AMP-dependent enzyme.</jats:p> |
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Biochemical Journal |
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| _version_ | 1792343170580742152 |
| author | Cheng, H C, van Patten, S M, Smith, A J, Walsh, D A |
| author_facet | Cheng, H C, van Patten, S M, Smith, A J, Walsh, D A, Cheng, H C, van Patten, S M, Smith, A J, Walsh, D A |
| author_sort | cheng, h c |
| container_issue | 3 |
| container_start_page | 655 |
| container_title | Biochemical Journal |
| container_volume | 231 |
| description | <jats:p>Digestion with Staphylococcus aureus V8 proteinase of the inhibitor protein of the cyclic AMP-dependent protein kinase results in the sequential formation of three active inhibitory peptides. The smallest active peptide has the sequence Thr-Thr-Tyr-Ala-Asp-Phe-Ile-Ala-Ser-Gly-Arg-Thr-Gly-Arg-Arg-Asn-Ala-Ile- His-Asp . This 20-amino-acid-residue peptide has 20-40% of the activity of the native molecule and a Ki of 0.2 nM. Inhibition, as a minimum, appears to be based upon the inhibitor protein containing the recognition sequences that dictate protein-substrate-specificity. This inhibitory peptide also has sequence homology with the phosphorylation site for a protein kinase other than the cyclic AMP-dependent enzyme.</jats:p> |
| doi_str_mv | 10.1042/bj2310655 |
| facet_avail | Online, Free |
| finc_class_facet | Biologie, Chemie und Pharmazie |
| format | ElectronicArticle |
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| format_dezwi2 | Article, E-Article |
| format_finc | Article, E-Article |
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| geogr_code_person | not assigned |
| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTA0Mi9iajIzMTA2NTU |
| imprint | Portland Press Ltd., 1985 |
| imprint_str_mv | Portland Press Ltd., 1985 |
| institution | DE-Brt1, DE-Zwi2, DE-D161, DE-Zi4, DE-Gla1, DE-15, DE-Pl11, DE-Rs1, DE-14, DE-105, DE-Ch1, DE-L229, DE-D275, DE-Bn3 |
| issn | 0264-6021, 1470-8728 |
| issn_str_mv | 0264-6021, 1470-8728 |
| language | English |
| last_indexed | 2024-03-01T16:46:48.941Z |
| match_str | cheng1985anactivetwentyaminoacidresiduepeptidederivedfromtheinhibitorproteinofthecyclicampdependentproteinkinase |
| mega_collection | Portland Press Ltd. (CrossRef) |
| physical | 655-661 |
| publishDate | 1985 |
| publishDateSort | 1985 |
| publisher | Portland Press Ltd. |
| record_format | ai |
| recordtype | ai |
| series | Biochemical Journal |
| source_id | 49 |
| spelling | Cheng, H C van Patten, S M Smith, A J Walsh, D A 0264-6021 1470-8728 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1042/bj2310655 <jats:p>Digestion with Staphylococcus aureus V8 proteinase of the inhibitor protein of the cyclic AMP-dependent protein kinase results in the sequential formation of three active inhibitory peptides. The smallest active peptide has the sequence Thr-Thr-Tyr-Ala-Asp-Phe-Ile-Ala-Ser-Gly-Arg-Thr-Gly-Arg-Arg-Asn-Ala-Ile- His-Asp . This 20-amino-acid-residue peptide has 20-40% of the activity of the native molecule and a Ki of 0.2 nM. Inhibition, as a minimum, appears to be based upon the inhibitor protein containing the recognition sequences that dictate protein-substrate-specificity. This inhibitory peptide also has sequence homology with the phosphorylation site for a protein kinase other than the cyclic AMP-dependent enzyme.</jats:p> An active twenty-amino-acid-residue peptide derived from the inhibitor protein of the cyclic AMP-dependent protein kinase Biochemical Journal |
| spellingShingle | Cheng, H C, van Patten, S M, Smith, A J, Walsh, D A, Biochemical Journal, An active twenty-amino-acid-residue peptide derived from the inhibitor protein of the cyclic AMP-dependent protein kinase, Cell Biology, Molecular Biology, Biochemistry |
| title | An active twenty-amino-acid-residue peptide derived from the inhibitor protein of the cyclic AMP-dependent protein kinase |
| title_full | An active twenty-amino-acid-residue peptide derived from the inhibitor protein of the cyclic AMP-dependent protein kinase |
| title_fullStr | An active twenty-amino-acid-residue peptide derived from the inhibitor protein of the cyclic AMP-dependent protein kinase |
| title_full_unstemmed | An active twenty-amino-acid-residue peptide derived from the inhibitor protein of the cyclic AMP-dependent protein kinase |
| title_short | An active twenty-amino-acid-residue peptide derived from the inhibitor protein of the cyclic AMP-dependent protein kinase |
| title_sort | an active twenty-amino-acid-residue peptide derived from the inhibitor protein of the cyclic amp-dependent protein kinase |
| title_unstemmed | An active twenty-amino-acid-residue peptide derived from the inhibitor protein of the cyclic AMP-dependent protein kinase |
| topic | Cell Biology, Molecular Biology, Biochemistry |
| url | http://dx.doi.org/10.1042/bj2310655 |