Structural changes in glycogen phosphorylase induced by phosphorylation
Sprang, S. R. ; Acharya, K. R. ; Goldsmith, E. J. ; Stuart, D. I. ; Varvill, K. ; Fletterick, R. J. ; Madsen, N. B. ; Johnson, L. N.
[s.l.] : Nature Publishing Group
Published 1988
[s.l.] : Nature Publishing Group
Published 1988
ISSN: |
1476-4687
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Source: |
Nature Archives 1869 - 2009
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Topics: |
Biology
Chemistry and Pharmacology
Medicine
Natural Sciences in General
Physics
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Notes: |
[Auszug] A comparison of the refined crystal structures of dimeric glycogen phosphorylase b and a reveals structural changes that represent the first step in the activation of the enzyme. On phosphorylation of serine-14, the N-terminus of each subunit assumes an ordered helical conformation and binds to the ...
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Type of Medium: |
Electronic Resource
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URL: |
_version_ | 1798293086741200898 |
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autor | Sprang, S. R. Acharya, K. R. Goldsmith, E. J. Stuart, D. I. Varvill, K. Fletterick, R. J. Madsen, N. B. Johnson, L. N. |
autorsonst | Stuart, D. I. Varvill, K. Fletterick, R. J. Madsen, N. B. Johnson, L. N. |
book_url | http://dx.doi.org/10.1038/336215a0 |
datenlieferant | nat_lic_papers |
hauptsatz | hsatz_simple |
identnr | NLZ235290688 |
insertion_date | 1911-02-25 |
issn | 1476-4687 |
journal_name | Nature |
materialart | 1 |
notes | [Auszug] A comparison of the refined crystal structures of dimeric glycogen phosphorylase b and a reveals structural changes that represent the first step in the activation of the enzyme. On phosphorylation of serine-14, the N-terminus of each subunit assumes an ordered helical conformation and binds to the ... |
package_name | Nature Publishing Group |
publikationsjahr_anzeige | 1988 |
publikationsjahr_facette | 1988 |
publikationsjahr_intervall | 8014:1985-1989 |
publikationsjahr_sort | 1988 |
publikationsort | [s.l.] |
publisher | Nature Publishing Group |
reference | 336 (1988), S. 215-221 |
search_space | articles |
shingle_author_1 | Sprang, S. R. Acharya, K. R. Goldsmith, E. J. Stuart, D. I. Varvill, K. Fletterick, R. J. Madsen, N. B. Johnson, L. N. |
shingle_author_2 | Sprang, S. R. Acharya, K. R. Goldsmith, E. J. Stuart, D. I. Varvill, K. Fletterick, R. J. Madsen, N. B. Johnson, L. N. |
shingle_author_3 | Sprang, S. R. Acharya, K. R. Goldsmith, E. J. Stuart, D. I. Varvill, K. Fletterick, R. J. Madsen, N. B. Johnson, L. N. |
shingle_author_4 | Sprang, S. R. Acharya, K. R. Goldsmith, E. J. Stuart, D. I. Varvill, K. Fletterick, R. J. Madsen, N. B. Johnson, L. N. |
shingle_catch_all_1 | Sprang, S. R. Acharya, K. R. Goldsmith, E. J. Stuart, D. I. Varvill, K. Fletterick, R. J. Madsen, N. B. Johnson, L. N. Structural changes in glycogen phosphorylase induced by phosphorylation Nature Publishing Group [Auszug] A comparison of the refined crystal structures of dimeric glycogen phosphorylase b and a reveals structural changes that represent the first step in the activation of the enzyme. On phosphorylation of serine-14, the N-terminus of each subunit assumes an ordered helical conformation and binds to the ... 1476-4687 14764687 |
shingle_catch_all_2 | Sprang, S. R. Acharya, K. R. Goldsmith, E. J. Stuart, D. I. Varvill, K. Fletterick, R. J. Madsen, N. B. Johnson, L. N. Structural changes in glycogen phosphorylase induced by phosphorylation Nature Publishing Group [Auszug] A comparison of the refined crystal structures of dimeric glycogen phosphorylase b and a reveals structural changes that represent the first step in the activation of the enzyme. On phosphorylation of serine-14, the N-terminus of each subunit assumes an ordered helical conformation and binds to the ... 1476-4687 14764687 |
shingle_catch_all_3 | Sprang, S. R. Acharya, K. R. Goldsmith, E. J. Stuart, D. I. Varvill, K. Fletterick, R. J. Madsen, N. B. Johnson, L. N. Structural changes in glycogen phosphorylase induced by phosphorylation Nature Publishing Group [Auszug] A comparison of the refined crystal structures of dimeric glycogen phosphorylase b and a reveals structural changes that represent the first step in the activation of the enzyme. On phosphorylation of serine-14, the N-terminus of each subunit assumes an ordered helical conformation and binds to the ... 1476-4687 14764687 |
shingle_catch_all_4 | Sprang, S. R. Acharya, K. R. Goldsmith, E. J. Stuart, D. I. Varvill, K. Fletterick, R. J. Madsen, N. B. Johnson, L. N. Structural changes in glycogen phosphorylase induced by phosphorylation Nature Publishing Group [Auszug] A comparison of the refined crystal structures of dimeric glycogen phosphorylase b and a reveals structural changes that represent the first step in the activation of the enzyme. On phosphorylation of serine-14, the N-terminus of each subunit assumes an ordered helical conformation and binds to the ... 1476-4687 14764687 |
shingle_title_1 | Structural changes in glycogen phosphorylase induced by phosphorylation |
shingle_title_2 | Structural changes in glycogen phosphorylase induced by phosphorylation |
shingle_title_3 | Structural changes in glycogen phosphorylase induced by phosphorylation |
shingle_title_4 | Structural changes in glycogen phosphorylase induced by phosphorylation |
sigel_instance_filter | dkfz geomar wilbert ipn albert |
source_archive | Nature Archives 1869 - 2009 |
timestamp | 2024-05-06T08:58:50.071Z |
titel | Structural changes in glycogen phosphorylase induced by phosphorylation |
titel_suche | Structural changes in glycogen phosphorylase induced by phosphorylation |
topic | W V WW-YZ TA-TD U |
uid | nat_lic_papers_NLZ235290688 |