| First Author | Sol-Church K | Year | 2000 |
| Journal | Biochim Biophys Acta | Volume | 1492 |
| Issue | 2-3 | Pages | 488-92 |
| PubMed ID | 11004518 | Mgi Jnum | J:63600 |
| Mgi Id | MGI:1861279 | Doi | 10.1016/s0167-4781(00)00114-7 |
| Citation | Sol-Church K, et al. (2000) Characterization of mouse cathepsin R, a new member of a family of placentally expressed cysteine proteases. Biochim Biophys Acta 1492(2-3):488-92 |
| abstractText | A new mouse cysteine protease, termed cathepsin R, has been identified. The complete nucleotide sequence of this gene was derived from a set of cDNAs generated from 15.5-day mouse placenta. Sequence analysis revealed an open reading frame encoding a 334 amino acid long polypeptide closely related to placentally expressed cathepsins P, Q, and M. RT-PCR analysis indicated that cathepsin R is only expressed in placenta and thus is a new member of the emerging family of cathepsins whose expression is regulated during mouse embryonic development. Modeling and structural analysis suggests that cathepsin R will have a restricted substrate specificity when compared to that of cathepsin L. |
