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Memo Is a Copper-Dependent Redox Protein with an Essential Role in Migration and Metastasis.
- Published in:
- Science Signaling, 2014, v. 7, n. 329, p. 1, doi. 10.1126/scisignal.2004870
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- Article
The Sir4 H‐BRCT domain interacts with phospho‐proteins to sequester and repress yeast heterochromatin.
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- EMBO Journal, 2020, v. 39, n. 1, p. N.PAG, doi. 10.15252/embj.2019103976
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- Article
The Sir4 H‐BRCT domain interacts with phospho‐proteins to sequester and repress yeast heterochromatin.
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- EMBO Journal, 2019, v. 38, n. 20, p. 1, doi. 10.15252/embj.2019101744
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- Article
Dimerization of Sir3 via its C-terminal winged helix domain is essential for yeast heterochromatin formation.
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- EMBO Journal, 2013, v. 32, n. 3, p. 437, doi. 10.1038/emboj.2012.343
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- Article
Structure of human POFUT2: insights into thrombospondin type 1 repeat fold and O-fucosylation.
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- EMBO Journal, 2012, v. 31, n. 14, p. 3183, doi. 10.1038/emboj.2012.143
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- Article
Evolutionary plasticity of the NHL domain underlies distinct solutions to RNA recognition.
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- Nature Communications, 2018, v. 9, n. 1, p. 1, doi. 10.1038/s41467-018-03920-7
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- Article
The TRIM-NHL Protein LIN-41 Controls the Onset of Developmental Plasticity in <i>Caenorhabditis elegans</i>.
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- PLoS Genetics, 2014, v. 10, n. 8, p. 1, doi. 10.1371/journal.pgen.1004533
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- Article