Macro domain-like
Short name | Macro_dom-like |
Overlapping entries |
Description
References
1.Structural and functional basis for ADP-ribose and poly(ADP-ribose) binding by viral macro domains. Egloff MP, Malet H, Putics A, Heinonen M, Dutartre H, Frangeul A, Gruez A, Campanacci V, Cambillau C, Ziebuhr J, Ahola T, Canard B. J. Virol. 80, 8493-502, (2006). View articlePMID: 16912299
2.Differential activities of cellular and viral macro domain proteins in binding of ADP-ribose metabolites. Neuvonen M, Ahola T. J. Mol. Biol. 385, 212-25, (2009). View articlePMID: 18983849
3.The WWE domain: a common interaction module in protein ubiquitination and ADP ribosylation. Aravind L. Trends Biochem. Sci. 26, 273-5, (2001). View articlePMID: 11343911
4.Nuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going? Hassa PO, Haenni SS, Elser M, Hottiger MO. Microbiol. Mol. Biol. Rev. 70, 789-829, (2006). View articlePMID: 16959969
5.Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins. Ahel I, Ahel D, Matsusaka T, Clark AJ, Pines J, Boulton SJ, West SC. Nature 451, 81-5, (2008). View articlePMID: 18172500
6.The macro domain is an ADP-ribose binding module. Karras GI, Kustatscher G, Buhecha HR, Allen MD, Pugieux C, Sait F, Bycroft M, Ladurner AG. EMBO J. 24, 1911-20, (2005). View articlePMID: 15902274
7.Splicing regulates NAD metabolite binding to histone macroH2A. Kustatscher G, Hothorn M, Pugieux C, Scheffzek K, Ladurner AG. Nat. Struct. Mol. Biol. 12, 624-5, (2005). View articlePMID: 15965484
8.The crystal structure of AF1521 a protein from Archaeoglobus fulgidus with homology to the non-histone domain of macroH2A. Allen MD, Buckle AM, Cordell SC, Lowe J, Bycroft M. J. Mol. Biol. 330, 503-11, (2003). View articlePMID: 12842467
9.A biochemical genomics approach for identifying genes by the activity of their products. Martzen MR, McCraith SM, Spinelli SL, Torres FM, Fields S, Grayhack EJ, Phizicky EM. Science 286, 1153-5, (1999). View articlePMID: 10550052
10.X-ray structure of aminopeptidase A from Escherichia coli and a model for the nucleoprotein complex in Xer site-specific recombination. Strater N, Sherratt DJ, Colloms SD. EMBO J. 18, 4513-22, (1999). View articlePMID: 10449417
11.Bacterial aminopeptidases: properties and functions. Gonzales T, Robert-Baudouy J. FEMS Microbiol. Rev. 18, 319-44, (1996). View articlePMID: 8703509
12.Structural and immunological evidence for the identity of prolyl aminopeptidase with leucyl aminopeptidase. Matsushima M, Takahashi T, Ichinose M, Miki K, Kurokawa K, Takahashi K. Biochem. Biophys. Res. Commun. 178, 1459-64, (1991). View articlePMID: 1908238
13.Leucine aminopeptidase from Arabidopsis thaliana. Molecular evidence for a phylogenetically conserved enzyme of protein turnover in higher plants. Bartling D, Weiler EW. Eur. J. Biochem. 205, 425-31, (1992). View articlePMID: 1555602
14.Molecular structure of leucine aminopeptidase at 2.7-A resolution. Burley SK, David PR, Taylor A, Lipscomb WN. Proc. Natl. Acad. Sci. U.S.A. 87, 6878-82, (1990). View articlePMID: 2395881
15.Mutational analysis of Escherichia coli PepA, a multifunctional DNA-binding aminopeptidase. Charlier D, Kholti A, Huysveld N, Gigot D, Maes D, Thia-Toong TL, Glansdorff N. J. Mol. Biol. 302, 411-26, (2000). View articlePMID: 10970742
16.The ADP-ribose-1''-monophosphatase domains of severe acute respiratory syndrome coronavirus and human coronavirus 229E mediate resistance to antiviral interferon responses. Kuri T, Eriksson KK, Putics A, Zust R, Snijder EJ, Davidson AD, Siddell SG, Thiel V, Ziebuhr J, Weber F. J. Gen. Virol. 92, 1899-1905, (2011). PMID: 21525212
Cross References
Contributing Member Database Entries
- CATH-Gene3D:G3DSA:3.40.220.10
- SUPERFAMILY:SSF52949