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The [NiFe]-hydrogenase accessory chaperones HypC and HybG of Escherichia coli are iron- and carbon dioxide-binding proteins.
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- FEBS Letters, 2013, v. 587, n. 16, p. 2512, doi. 10.1016/j.febslet.2013.06.055
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- Article
The N‐terminal domains of the paralogous HycE and NuoCD govern assembly of the respective formate hydrogenlyase and NADH dehydrogenase complexes.
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- FEBS Open Bio, 2020, v. 10, n. 3, p. 371, doi. 10.1002/2211-5463.12787
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- Article
The dual-function chaperone HycH improves assembly of the formate hydrogenlyase complex.
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- Biochemical Journal, 2017, v. 474, n. 17, p. 2937, doi. 10.1042/BCJ20170431
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- Article
[NiFe]-hydrogenase maturation in vitro: analysis of the roles of the HybG and HypD accessory proteins.
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- Biochemical Journal, 2014, v. 464, n. 2, p. 169, doi. 10.1042/BJ20140485
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- Article
The Influence of Oxygen on [NiFe]–Hydrogenase Cofactor Biosynthesis and How Ligation of Carbon Monoxide Precedes Cyanation.
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- PLoS ONE, 2014, v. 9, n. 9, p. 1, doi. 10.1371/journal.pone.0107488
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- Article
Metabolic Deficiences Revealed in the Biotechnologically Important Model Bacterium Escherichia coli BL21(DE3).
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- PLoS ONE, 2011, v. 6, n. 8, p. 1, doi. 10.1371/journal.pone.0022830
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- Article
Identification of an Isothiocyanate on the HypEF Complex Suggests a Route for Efficient Cyanyl–Group Channeling during [NiFe]–Hydrogenase Cofactor Generation.
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- PLoS ONE, 2015, v. 10, n. 7, p. 1, doi. 10.1371/journal.pone.0133118
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- Article
Malfolded recombinant Tat substrates are Tat-independently degraded in Escherichia coli
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- FEBS Letters, 2010, v. 584, n. 16, p. 3644, doi. 10.1016/j.febslet.2010.07.039
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- Article
The TatBC complex formation suppresses a modular TatB-multimerization in Escherichia coli
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- FEBS Letters, 2007, v. 581, n. 21, p. 4085, doi. 10.1016/j.febslet.2007.07.045
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- Article
Structural studies on a twin-arginine signal sequence
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- FEBS Letters, 2003, v. 550, n. 1-3, p. 18, doi. 10.1016/S0014-5793(03)00804-4
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- Article