N- and C-terminal domains in human holocarboxylase synthetase participate in substrate recognition
- 30 April 2009
- journal article
- research article
- Published by Elsevier BV in Molecular Genetics and Metabolism
- Vol. 96 (4), 183-188
- https://doi.org/10.1016/j.ymgme.2008.12.006
Abstract
No abstract availableKeywords
This publication has 44 references indexed in Scilit:
- Biotinylation of Histones Represses Transposable Elements in Human and Mouse Cells and Cell Lines and in Drosophila melanogaster3Journal of Nutrition, 2008
- Epigenetic regulation of chromatin structure and gene function by biotin: are biotin requirements being met?Nutrition Reviews, 2008
- Holocarboxylase synthetase regulates expression of biotin transporters by chromatin remodeling events at the SMVT locusThe Journal of Nutritional Biochemistry, 2008
- K12-biotinylated histone H4 marks heterochromatin in human lymphoblastoma cellsThe Journal of Nutritional Biochemistry, 2007
- K4, K9 and K18 in human histone H3 are targets for biotinylation by biotinidaseThe FEBS Journal, 2005
- K8 and K12 are biotinylated in human histone H4European Journal of Biochemistry, 2004
- The Pfam protein families databaseNucleic Acids Research, 2004
- Reduced histone biotinylation in multiple carboxylase deficiency patients: a nuclear role for holocarboxylase synthetaseHuman Molecular Genetics, 2003
- SWISS‐MODEL and the Swiss‐Pdb Viewer: An environment for comparative protein modelingElectrophoresis, 1997
- A novel genetic system to detect protein–protein interactionsNature, 1989