ArticleJournal of structural biology: X2023
CryoEM reveals oligomeric isomers of a multienzyme complex and assembly mechanics.
Article in Journal of structural biology: X, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Conserved and divergent mitochondrial assemblies in kinetoplastid parasites.Molecular cell · 2026Article
- Oligomeric assemblies of plant biotin carboxylase revealed by cryo-EM and cross-linking.The Biochemical journal · 2026Article
- Structural basis for substrate specificity and MSMEG_0435-0436 binding by the mycobacterial long-chain acyl-CoA carboxylase complex.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Filament structures unveil the dynamic organization of human acetyl-CoA carboxylase.Science advances · 2024Article
- The cryo-EM structure of trypanosome 3-methylcrotonyl-CoA carboxylase provides mechanistic and dynamic insights into its enzymatic function.Structure (London, England : 1993) · 2024Article
- Sample optimizations to enable the structure determination of biotin-dependent carboxylases.Methods in enzymology · 2024Article
- Discovery, structure, and function of filamentous 3-methylcrotonyl-CoA carboxylase.Structure (London, England : 1993) · 2023Article
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6 authors.
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Abstract
Propionyl-CoA carboxylase (PCC) is a multienzyme complex consisting of up to six α-subunits and six β-subunits. Belonging to a metabolic pathway converging on the citric acid cycle, it is present in most forms of life and irregularities in its assembly lead to serious illness in humans, known as propionic acidemia. Here, we report the cryogenic electron microscopy (cryoEM) structures and assembly of different oligomeric isomers of endogenous PCC from the parasitic protozoan
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