^Deed RW, Jasiok M, Norton JD. Lymphoid-specific expression of the Id3 gene in hematopoietic cells. Selective antagonism of E2A basic helix-loop-helix protein associated with Id3-induced differentiation of erythroleukemia cells. J. Biol. Chem. Apr 1998, 273 (14): 8278–86. PMID 9525934. doi:10.1074/jbc.273.14.8278.
^Langlands K, Yin X, Anand G, Prochownik EV. Differential interactions of Id proteins with basic-helix-loop-helix transcription factors. J. Biol. Chem. Aug 1997, 272 (32): 19785–93. PMID 9242638. doi:10.1074/jbc.272.32.19785.
Wibley J, Deed R, Jasiok M, Douglas K, Norton J. A homology model of the Id-3 helix-loop-helix domain as a basis for structure-function predictions. Biochim. Biophys. Acta. 1996, 1294 (2): 138–46. PMID 8645731. doi:10.1016/0167-4838(96)00008-8.
Deed RW, Armitage S, Norton JD. Nuclear localization and regulation of Id protein through an E protein-mediated chaperone mechanism. J. Biol. Chem. 1996, 271 (39): 23603–6. PMID 8798572. doi:10.1074/jbc.271.39.23603.
Deed RW, Jasiok M, Norton JD. Lymphoid-specific expression of the Id3 gene in hematopoietic cells. Selective antagonism of E2A basic helix-loop-helix protein associated with Id3-induced differentiation of erythroleukemia cells. J. Biol. Chem. 1998, 273 (14): 8278–86. PMID 9525934. doi:10.1074/jbc.273.14.8278.
Asp J, Thornemo M, Inerot S, Lindahl A. The helix-loop-helix transcription factors Id1 and Id3 have a functional role in control of cell division in human normal and neoplastic chondrocytes. FEBS Lett. 1998, 438 (1-2): 85–90. PMID 9821964. doi:10.1016/S0014-5793(98)01268-X.
Jögi A, Persson P, Grynfeld A, Påhlman S, Axelson H. Modulation of basic helix-loop-helix transcription complex formation by Id proteins during neuronal differentiation. J. Biol. Chem. 2002, 277 (11): 9118–26. PMID 11756408. doi:10.1074/jbc.M107713200.