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JAMC-Journal of Ayub Medical College-Abbotabad-Pakistan. 2008; 20 (4): 130-133
in English | IMEMR | ID: emr-101913

ABSTRACT

Vaccine development is one of the most promising fields in cancer research. After autologous transplantation, due to low tumour burden, patients are more likely to respond immunologically to a cancer vaccine[7]. MUC1 with its adhesive and antiadhesive functions, immunostimulatory and immunosuppressive activities, is therefore a good candidate for breast cancer vaccine. A structure-based insight into the immunogenicity of natural MUC1 glycoforms, of its sub-domains, motifs and post translational modification like glycosylation and myriostoylation may aid the design of tumour vaccines. Primary sequences of human MUC1 were retrieved from the SWISSPROT data bank. Protein pattern search: The primary sequence of Human MUC1 was searched at PROSITE [a dictionary of protein sites and patterns] database. Our study observes that post-translational modifications play an important role in presenting MUC1 as a candidate for breast cancer vaccine. It is found that the phosphrylation and glycosylation of important functional motifs of MUC1 may take part in the production of cytokines that may provide immunization


Subject(s)
Humans , Mucin-1 , Vaccines , Protein Processing, Post-Translational , Phosphorylation , Glycosylation , Tandem Repeat Sequences , Cytokines
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