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Insights Into the Allosteric Inhibition of the SUMO E2 Enzyme Ubc9.
- Published in:
- Angewandte Chemie, 2016, v. 128, n. 19, p. 5797, doi. 10.1002/ange.201511351
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- Article
Insights Into the Allosteric Inhibition of the SUMO E2 Enzyme Ubc9.
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- Angewandte Chemie International Edition, 2016, v. 55, n. 19, p. 5703, doi. 10.1002/anie.201511351
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- Article
Biomolecular Interactions of Small-molecule Inhibitors Affecting the YopH Protein Tyrosine Phosphatase.
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- Chemical Biology & Drug Design, 2013, v. 81, n. 3, p. 323, doi. 10.1111/cbdd.12097
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- Article
Unique Structural Fold of LonBA Protease from Bacillus subtilis, a Member of a Newly Identified Subfamily of Lon Proteases.
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- International Journal of Molecular Sciences, 2022, v. 23, n. 19, p. 11425, doi. 10.3390/ijms231911425
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- Article
The Convergence of the Hedgehog/Intein Fold in Different Protein Splicing Mechanisms.
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- International Journal of Molecular Sciences, 2020, v. 21, n. 21, p. 8367, doi. 10.3390/ijms21218367
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- Article
Crystal structure of UDP‐glucose pyrophosphorylase from Yersinia pestis, a potential therapeutic target against plague.
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- Acta Crystallographica: Section F, Structural Biology Communications, 2019, v. 75, n. 9, p. 608, doi. 10.1107/S2053230X19011154
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- Article
MBP‐binding DARPins facilitate the crystallization of an MBP fusion protein.
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- Acta Crystallographica: Section F, Structural Biology Communications, 2018, v. 74, n. 9, p. 549, doi. 10.1107/S2053230X18009901
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- Article
Structure of human dual-specificity phosphatase 7, a potential cancer drug target.
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- Acta Crystallographica: Section F, Structural Biology Communications, 2015, v. 71, n. 6, p. 650, doi. 10.1107/S2053230X1500504X
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- Article
Structural analysis of human dual-specificity phosphatase 22 complexed with a phosphotyrosine-like substrate.
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- Acta Crystallographica: Section F, Structural Biology Communications, 2015, v. 71, n. 2, p. 199, doi. 10.1107/S2053230X15000217
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- Article
Targeted sulfur(VI) fluoride exchange-mediated covalent modification of a tyrosine residue in the catalytic pocket of tyrosyl-DNA phosphodiesterase 1.
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- Communications Chemistry, 2024, v. 7, n. 1, p. 1, doi. 10.1038/s42004-024-01298-w
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- Article
Phosphotyrosine Substrate Sequence Motifs for Dual Specificity Phosphatases.
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- PLoS ONE, 2015, v. 10, n. 8, p. 1, doi. 10.1371/journal.pone.0134984
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- Article
Characterization of a broadly specific cadaverine N-hydroxylase involved in desferrioxamine B biosynthesis in Streptomyces sviceus.
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- PLoS ONE, 2021, v. 16, n. 3, p. 1, doi. 10.1371/journal.pone.0248385
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- Article
High‐resolution crystal structures of the D1 and D2 domains of protein tyrosine phosphatase epsilon for structure‐based drug design.
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- Acta Crystallographica: Section D, Structural Biology, 2018, v. 74, n. 10, p. 1015, doi. 10.1107/S2059798318011919
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- Article
Identification of a ligand binding hot spot and structural motifs replicating aspects of tyrosyl-DNA phosphodiesterase I (TDP1) phosphoryl recognition by crystallographic fragment cocktail screening.
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- Nucleic Acids Research, 2019, v. 47, n. 19, p. 10134, doi. 10.1093/nar/gkz515
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- Article
X-ray structures of checkpoint kinase 2 in complex with inhibitors that target its gatekeeper-dependent hydrophobic pocket
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- FEBS Letters, 2011, v. 585, n. 20, p. 3245, doi. 10.1016/j.febslet.2011.08.050
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- Article
Atomic resolution structure of the cytoplasmic domain of Yersinia pestis YscU, a regulatory switch involved in type III secretion.
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- Protein Science: A Publication of the Protein Society, 2009, v. 18, n. 2, p. 467, doi. 10.1002/pro.56
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- Article
Crystal structure of checkpoint kinase 2 in complex with NSC 109555, a potent and selective inhibitor.
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- Protein Science: A Publication of the Protein Society, 2009, v. 18, n. 1, p. 92, doi. 10.1002/pro.16
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- Article
P1′ specificity of the S219V/R203G mutant tobacco etch virus protease.
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- Proteins, 2024, v. 92, n. 9, p. 1085, doi. 10.1002/prot.26693
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- Article
Crystal structure of the human dual specificity phosphatase 1 catalytic domain.
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- Protein Science: A Publication of the Protein Society, 2018, v. 27, n. 2, p. 561, doi. 10.1002/pro.3328
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- Article