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Lactococcal phage p2 ORF35-Sak3 is an ATPase involved in DNA recombination and AbiK mechanism.
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- Molecular Microbiology, 2011, v. 80, n. 1, p. 102, doi. 10.1111/j.1365-2958.2011.07561.x
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- Article
Structure and function of phage p2 ORF34<sub>p2</sub>, a new type of single-stranded DNA binding protein.
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- Molecular Microbiology, 2009, v. 73, n. 6, p. 1156, doi. 10.1111/j.1365-2958.2009.06844.x
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- Article
Kinetics and interaction studies between cytochrome c<sub>3</sub> and Fe-only hydrogenase from Desulfovibrio vulgaris hildenborough.
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- Proteins, 1998, v. 33, n. 4, p. 590, doi. 10.1002/(SICI)1097-0134(19981201)33:4<590::AID-PROT11>3.0.CO;2-I
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- Article
A hypothetical complex between crystalline flavocytochrome b<sub>2</sub> and Cytochrome c.
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- Proteins, 1993, v. 16, n. 4, p. 408, doi. 10.1002/prot.340160409
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- Article
A novel type of catalytic copper cluster in nitrous oxide reductase.
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- Nature Structural Biology, 2000, v. 7, n. 3, p. 191
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- Article
The membrane bound bacterial lipocalin Blc is a functional dimer with binding preference for lysophospholipids
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- FEBS Letters, 2006, v. 580, n. 20, p. 4877, doi. 10.1016/j.febslet.2006.07.086
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- Article
Plant stress proteins of the thaumatin-like family discovered in animals
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- FEBS Letters, 2004, v. 572, n. 1-3, p. 3, doi. 10.1016/j.febslet.2004.07.003
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- Article
Crystal structure and reactivity of YbdL from Escherichia coli identify a methionine aminotransferase function
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- FEBS Letters, 2004, v. 571, n. 1-3, p. 141, doi. 10.1016/j.febslet.2004.06.075
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- Article
Domain swapping of a llama VHH domain builds a crystal-wide β-sheet structure
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- FEBS Letters, 2004, v. 564, n. 1/2, p. 35, doi. 10.1016/S0014-5793(04)00304-7
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- Article
The crystal structure of the Escherichia coli lipocalin Blc suggests a possible role in phospholipid binding
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- FEBS Letters, 2004, v. 562, n. 1-3, p. 183, doi. 10.1016/S0014-5793(04)00199-1
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- Article
Camelid nanobodies raised against an integral membrane enzyme, nitric oxide reductase.
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- Protein Science: A Publication of the Protein Society, 2009, v. 18, n. 3, p. 619, doi. 10.1002/pro.69
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- Article