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
1. Verfasser: Koren, Itay
Format: Artikel
Sprache:eng
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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.
ISSN:0969-2126
1878-4186
DOI:10.1016/j.str.2022.08.003