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2.
Eur J Surg Oncol ; 2007 Jan 09.
Article in English | MEDLINE | ID: mdl-17218077

ABSTRACT

This article has been withdrawn consistent with Elsevier Policy on Article Withdrawal (http://www.elsevier.com/locate/withdrawalpolicy). The Publisher apologizes for any inconvenience this may cause.

3.
Gene ; 197(1-2): 115-20, 1997 Sep 15.
Article in English | MEDLINE | ID: mdl-9332356

ABSTRACT

Pinin is a cell junction-associated protein involved in the stabilization of the desmosome-intermediate filament complex in various epithelial tissues. Utilizing a cDNA probe derived from canine pinin, we isolated overlapping cDNA clones encoding murine full-length pinin. The total cDNA contained an open reading frame of 2175 nucleotides coding for 725 amino acids as well as a 3'- and a 5'-untranslated regions of 620 and 18 nucleotides, respectively. The overall predicted amino acid sequence of mouse pinin displayed strong identities to those of canine and human pinin, with the exception of a stretch of 38 amino acids which were found to be deleted in mouse pinin. There were several discernible domains found within mouse pinin. These included three coiled-coil domains, a small stretch of glycine loops, a short glutamine-proline-rich domain and a polyserine domain.


Subject(s)
Cell Adhesion Molecules/genetics , DNA, Complementary/genetics , Nuclear Proteins , Amino Acid Sequence , Animals , Base Sequence , Cell Adhesion Molecules/chemistry , Cloning, Molecular , DNA-Binding Proteins , Dogs , Mice , Molecular Sequence Data , Open Reading Frames/genetics , Protein Structure, Secondary , Sequence Analysis, DNA , Sequence Homology, Amino Acid
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