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succinyl-coenzyme a and Genetic Diseases, X-Chromosome Linked

succinyl-coenzyme a has been researched along with Genetic Diseases, X-Chromosome Linked in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	1 (50.00)	2.80

Authors

Authors	Studies
Bailey, HJ; Bezerra, GA; Bishop, DF; Bulusu, G; Dailey, HA; Desnick, RJ; Foster, WR; Marcero, JR; Padhi, S; Rembeza, E; Roy, A; Yue, WW	1
Astner, I; Heinz, DW; Jahn, D; Schubert, WD; Schulze, JO; van den Heuvel, J	1

Other Studies

2 other study(ies) available for succinyl-coenzyme a and Genetic Diseases, X-Chromosome Linked

Article	Year
Human aminolevulinate synthase structure reveals a eukaryotic-specific autoinhibitory loop regulating substrate binding and product release. Nature communications, 2020, 06-04, Volume: 11, Issue:1 Topics: 5-Aminolevulinate Synthetase; Acyl Coenzyme A; Catalysis; Catalytic Domain; Crystallography, X-Ray; Gene Expression Regulation, Enzymologic; Genetic Diseases, X-Linked; Heme; Humans; Kinetics; Molecular Dynamics Simulation; Protein Binding; Protein Conformation; Protein Domains; Protoporphyria, Erythropoietic; Substrate Specificity	2020
Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans. The EMBO journal, 2005, Sep-21, Volume: 24, Issue:18 Topics: 5-Aminolevulinate Synthetase; Acyl Coenzyme A; Amino Acid Sequence; Anemia, Sideroblastic; Binding Sites; Crystallography, X-Ray; Dimerization; Genetic Diseases, X-Linked; Glycine; Heme; Humans; Models, Molecular; Molecular Sequence Data; Mutation; Protein Structure, Quaternary; Pyridoxal Phosphate; Rhodobacter capsulatus; Sequence Alignment; Substrate Specificity	2005

Article

Year

Human aminolevulinate synthase structure reveals a eukaryotic-specific autoinhibitory loop regulating substrate binding and product release.

Nature communications, 2020, 06-04, Volume: 11, Issue:1

Topics: 5-Aminolevulinate Synthetase; Acyl Coenzyme A; Catalysis; Catalytic Domain; Crystallography, X-Ray; Gene Expression Regulation, Enzymologic; Genetic Diseases, X-Linked; Heme; Humans; Kinetics; Molecular Dynamics Simulation; Protein Binding; Protein Conformation; Protein Domains; Protoporphyria, Erythropoietic; Substrate Specificity

2020

Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans.

The EMBO journal, 2005, Sep-21, Volume: 24, Issue:18

Topics: 5-Aminolevulinate Synthetase; Acyl Coenzyme A; Amino Acid Sequence; Anemia, Sideroblastic; Binding Sites; Crystallography, X-Ray; Dimerization; Genetic Diseases, X-Linked; Glycine; Heme; Humans; Models, Molecular; Molecular Sequence Data; Mutation; Protein Structure, Quaternary; Pyridoxal Phosphate; Rhodobacter capsulatus; Sequence Alignment; Substrate Specificity

2005