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The peroxisomal zebrafish SCP2-thiolase (type-1) is a weak transient dimer as revealed by crystal structures and native mass spectrometry.
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- Biochemical Journal, 2019, v. 476, n. 2, p. 307, doi. 10.1042/BCJ20180788
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- Article
Crystal structures of two monomeric triosephosphate isomerase variants identified via a directed-evolution protocol selecting for l-arabinose isomerase activity.
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- Acta Crystallographica: Section F, Structural Biology Communications, 2016, v. 72, n. 6, p. 490, doi. 10.1107/S2053230X16007548
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- Article
Structures of lactaldehyde reductase, FucO, link enzyme activity to hydrogen bond networks and conformational dynamics.
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- FEBS Journal, 2023, v. 290, n. 2, p. 465, doi. 10.1111/febs.16603
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- Article
De novo biosynthesis of sterols and fatty acids in the Trypanosoma brucei procyclic form: Carbon source preferences and metabolic flux redistributions.
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- PLoS Pathogens, 2018, v. 14, n. 5, p. 1, doi. 10.1371/journal.ppat.1007116
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- Article
Expression of the naturally occurring truncated trkB neurotrophin receptor induces outgrowth of filopodia and processes in neuroblastoma cells.
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- Oncogene, 1999, v. 18, n. 6, p. 1285, doi. 10.1038/sj.onc.1202401
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- Article
IceBear: an intuitive and versatile web application for research‐data tracking from crystallization experiment to PDB deposition.
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- Acta Crystallographica: Section D, Structural Biology, 2021, v. 77, n. 2, p. 151, doi. 10.1107/S2059798320015223
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Crystallographic binding studies of rat peroxisomal multifunctional enzyme type 1 with 3‐ketodecanoyl‐CoA: capturing active and inactive states of its hydratase and dehydrogenase catalytic sites.
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- Acta Crystallographica: Section D, Structural Biology, 2020, v. 76, n. 12, p. 1256, doi. 10.1107/S2059798320013819
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- Article
Crystallographic substrate binding studies of Leishmania mexicana SCP2-thiolase (type-2): unique features of oxyanion hole-1.
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- PEDS: Protein Engineering, Design & Selection, 2017, v. 30, n. 3, p. 225, doi. 10.1093/protein/gzw080
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Structural enzymology studies with the substrate 3S‐hydroxybutanoyl‐CoA: bifunctional MFE1 is a less efficient dehydrogenase than monofunctional HAD.
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- FEBS Open Bio, 2024, v. 14, n. 4, p. 655, doi. 10.1002/2211-5463.13786
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Structural enzymology comparisons of multifunctional enzyme, type-1 ( MFE1): the flexibility of its dehydrogenase part.
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- FEBS Open Bio, 2017, v. 7, n. 12, p. 1830, doi. 10.1002/2211-5463.12337
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- Article