The hidden (degron) truth behind the degradation of DHFR disease-associated variants
In this issue of Structure, Kampmeyer et al. provide detailed mechanistic insights into how structural changes in disease-associated dihydrofolate reductase (DHFR) missense variants affect their cellular protein abundance and discuss implications for hereditary megaloblastic anemia disease. In this...
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Veröffentlicht in: | Structure (London) 2022-09, Vol.30 (9), p.1219-1221 |
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Format: | Artikel |
Sprache: | eng |
Online-Zugang: | Volltext |
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Zusammenfassung: | In this issue of Structure, Kampmeyer et al. provide detailed mechanistic insights into how structural changes in disease-associated dihydrofolate reductase (DHFR) missense variants affect their cellular protein abundance and discuss implications for hereditary megaloblastic anemia disease.
In this issue of Structure, Kampmeyer et al. provide detailed mechanistic insights into how structural changes in disease-associated dihydrofolate reductase (DHFR) missense variants affect their cellular protein abundance and discuss implications for hereditary megaloblastic anemia disease. |
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ISSN: | 0969-2126 1878-4186 |
DOI: | 10.1016/j.str.2022.08.003 |