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Scientific Reports|April 7, 2016
Structural basis for ligand-dependent dimerization of phenylalanine hydroxylase regulatory domainDipali Patel, Jolanta Kopec, Fiona Fitzpatrick, et al.
Human Mutation|August 16, 2014
Functional characterization and categorization of missense mutations that cause methylmalonyl-CoA mutase (MUT) deficiencyPatrick Forny, D Sean Froese, Terttu Suormala, et al.
Journal of Molecular Biology|April 7, 2009
Structural snapshots for the conformation-dependent catalysis by human medium-chain acyl-coenzyme A synthetase ACSM2AGrazyna Kochan, Ewa S Pilka, Frank von Delft, et al.
The EMBO Journal|September 21, 2007
Insights into histone code syntax from structural and biochemical studies of CARM1 methyltransferaseWyatt W Yue, Markus Hassler, S Mark Roe, et al.
Human Mutation|May 13, 2017
Protein destabilization and loss of protein-protein interaction are fundamental mechanisms in cblA-type methylmalonic aciduriaTanja Plessl, Céline Bürer, Seraina Lutz, et al.
Biochimie|August 16, 2024
Luminescence-based complementation assay to assess target engagement and cell permeability of glycolate oxidase (HAO1) inhibitorsSabrina R Mackinnon, Tryfon Zarganes-Tzitzikas, Cassandra J Adams, et al.
Biochemistry|February 27, 2026
5,10-Methylenetetrahydrofolate Reductase─the Key Allosteric Regulator in One-Carbon MetabolismLinnea K M Blomgren, Shuning Guo, D Sean Froese, et al.
Proceedings of the National Academy of Sciences of the United States of America|December 14, 2011
Conformational plasticity of glycogenin and its maltosaccharide substrate during glycogen biogenesisApirat Chaikuad, D Sean Froese, Georgina Berridge, et al.
European Journal of Human Genetics : EJHG|June 19, 2014
Linking genotypes database with locus-specific database and genotype-phenotype correlation in phenylketonuriaSarah Wettstein, Jarl Underhaug, Belen Perez, et al.
Biochimie|July 23, 2018
Zinc(II) binding on human wild-type ISCU and Met140 variants modulates NFS1 desulfurase activityNicholas G Fox, Alain Martelli, Joseph F Nabhan, et al.
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