1 r the self-assembly nature of amelogenin and tuftelin.

2 etween ameloblastin and either amelogenin or tuftelin.

3        To identify proteins interacting with tuftelin, a potential nucleator of enamel crystallites,

4 nd porcine cDNAs supports the revised bovine tuftelin amino acid sequence and suggests that the bovin

5 s revealed a significant interaction between tuftelin and S. mutans, with 26.8% of the variation in d

6                   These are the amelogenins, tuftelin, and ameloblastin, with recent data implicating

7 uctures of three enamel proteins-amelogenin, tuftelin, and sheathlin (ameloblastin/amelin)-have been

8 ected the derived amino acid sequence of the tuftelin carboxyl-terminus.

9               Published sequences for bovine tuftelin cDNA and genomic clones proposed different read

10                                    The mouse tuftelin clone is 2572 nucleotides in length, exclusive

11 Within the developing tooth organ, TIP39 and tuftelin immunolocalized to the apical pole of secretory

12              Immunolocalization of TIP39 and tuftelin in cultured ameloblast-like cells showed that t

13 mplification product confirmed expression of tuftelin in kidney, and identified an alternatively spli

14 ed to a mouse tooth expression library and a tuftelin-interacting protein (TIP) was isolated for furt

15                                              Tuftelin is a protein that has been suggested to functio

16          Northern blot analysis reveals that tuftelin is not ameloblast-specific but is expressed in

17 ultiple organs, a pattern similar to that of tuftelin messenger RNA.

18 nd identified an alternatively spliced mouse tuftelin mRNA lacking exon 2.

19 e translation initiation codon lengthens the tuftelin protein by 52 amino acids, 51 of which are iden

20                                          Two tuftelin RNA messages, of 2.6 and 3.2 kb, were detected.

21 o acid sequence and suggests that the bovine tuftelin translation initiation codon be re-assigned to