The hidden (degron) truth behind the degradation of DHFR disease-associated variants

Research output: Contribution to journalComment/debate

Abstract

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.

Original languageEnglish
Pages (from-to)1219-1221
Number of pages3
JournalStructure
Volume30
Issue number9
DOIs
StatePublished - 1 Sep 2022

Bibliographical note

Publisher Copyright:
© 2022

Funding

The work in my laboratory on PQC is supported by European Research Council ( ERC-2020-STG 947709 ) and Israel Science Foundation (ISF) ( 2380/21 , 3096/21 ). Figure 1 was created with BioRender.com .

FundersFunder number
European CommissionERC-2020-STG 947709
Israel Science Foundation3096/21, 2380/21

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