| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-85 |
Sentence |
denotes |
Enzymatic large-scale synthesis of MUC6-Tn glycoconjugates for antitumor vaccination. |
| T1 |
0-85 |
Sentence |
denotes |
Enzymatic large-scale synthesis of MUC6-Tn glycoconjugates for antitumor vaccination. |
| T1 |
0-85 |
Sentence |
denotes |
Enzymatic large-scale synthesis of MUC6-Tn glycoconjugates for antitumor vaccination. |
| TextSentencer_T2 |
86-244 |
Sentence |
denotes |
In cancer, mucins are aberrantly O-glycosylated, and consequently, they express tumor-associated antigens such as the Tn determinant (alpha-GalNAc-O-Ser/Thr). |
| T2 |
86-244 |
Sentence |
denotes |
In cancer, mucins are aberrantly O-glycosylated, and consequently, they express tumor-associated antigens such as the Tn determinant (alpha-GalNAc-O-Ser/Thr). |
| T2 |
86-244 |
Sentence |
denotes |
In cancer, mucins are aberrantly O-glycosylated, and consequently, they express tumor-associated antigens such as the Tn determinant (alpha-GalNAc-O-Ser/Thr). |
| TextSentencer_T3 |
245-330 |
Sentence |
denotes |
As compared with normal tissues, they also exhibit a different pattern of expression. |
| T3 |
245-330 |
Sentence |
denotes |
As compared with normal tissues, they also exhibit a different pattern of expression. |
| T3 |
245-330 |
Sentence |
denotes |
As compared with normal tissues, they also exhibit a different pattern of expression. |
| TextSentencer_T4 |
331-483 |
Sentence |
denotes |
In particular, MUC6, which is normally expressed only in gastric tissues, has been detected in intestinal, pulmonary, colorectal, and breast carcinomas. |
| T4 |
331-483 |
Sentence |
denotes |
In particular, MUC6, which is normally expressed only in gastric tissues, has been detected in intestinal, pulmonary, colorectal, and breast carcinomas. |
| T4 |
331-483 |
Sentence |
denotes |
In particular, MUC6, which is normally expressed only in gastric tissues, has been detected in intestinal, pulmonary, colorectal, and breast carcinomas. |
| TextSentencer_T5 |
484-586 |
Sentence |
denotes |
Recently, we have shown that the MCF7 breast cancer cell line expresses MUC6-Tn glycoproteins in vivo. |
| T5 |
484-586 |
Sentence |
denotes |
Recently, we have shown that the MCF7 breast cancer cell line expresses MUC6-Tn glycoproteins in vivo. |
| T5 |
484-586 |
Sentence |
denotes |
Recently, we have shown that the MCF7 breast cancer cell line expresses MUC6-Tn glycoproteins in vivo. |
| TextSentencer_T6 |
587-728 |
Sentence |
denotes |
Cancer-associated mucins show antigenic differences from normal mucins, and as such, they may be used as potential targets for immunotherapy. |
| T6 |
587-728 |
Sentence |
denotes |
Cancer-associated mucins show antigenic differences from normal mucins, and as such, they may be used as potential targets for immunotherapy. |
| T6 |
587-728 |
Sentence |
denotes |
Cancer-associated mucins show antigenic differences from normal mucins, and as such, they may be used as potential targets for immunotherapy. |
| TextSentencer_T7 |
729-829 |
Sentence |
denotes |
To develop anticancer vaccines based on the Tn antigen, we prepared several MUC6-Tn glycoconjugates. |
| T7 |
729-829 |
Sentence |
denotes |
To develop anticancer vaccines based on the Tn antigen, we prepared several MUC6-Tn glycoconjugates. |
| T7 |
729-829 |
Sentence |
denotes |
To develop anticancer vaccines based on the Tn antigen, we prepared several MUC6-Tn glycoconjugates. |
| TextSentencer_T8 |
830-1093 |
Sentence |
denotes |
To this end, we performed the GalNAc enzymatic transfer to two recombinant MUC6 proteins expressed in Escherichia coli, using UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferases (ppGalNAc-Ts), which catalyze in vivo the Tn antigen synthesis. |
| T8 |
830-1093 |
Sentence |
denotes |
To this end, we performed the GalNAc enzymatic transfer to two recombinant MUC6 proteins expressed in Escherichia coli, using UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferases (ppGalNAc-Ts), which catalyze in vivo the Tn antigen synthesis. |
| T8 |
830-1093 |
Sentence |
denotes |
To this end, we performed the GalNAc enzymatic transfer to two recombinant MUC6 proteins expressed in Escherichia coli, using UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferases (ppGalNAc-Ts), which catalyze in vivo the Tn antigen synthesis. |
| TextSentencer_T9 |
1094-1201 |
Sentence |
denotes |
We used either a mixture of ppGalNAc-Ts from MCF7 breast cancer cell extracts or a recombinant ppGalNAc-T1. |
| T9 |
1094-1201 |
Sentence |
denotes |
We used either a mixture of ppGalNAc-Ts from MCF7 breast cancer cell extracts or a recombinant ppGalNAc-T1. |
| T9 |
1094-1201 |
Sentence |
denotes |
We used either a mixture of ppGalNAc-Ts from MCF7 breast cancer cell extracts or a recombinant ppGalNAc-T1. |
| TextSentencer_T10 |
1202-1311 |
Sentence |
denotes |
In both cases, we achieved the synthesis of MUC6-Tn glycoconjugates at a semi-preparative scale (mg amounts). |
| T10 |
1202-1311 |
Sentence |
denotes |
In both cases, we achieved the synthesis of MUC6-Tn glycoconjugates at a semi-preparative scale (mg amounts). |
| T10 |
1202-1311 |
Sentence |
denotes |
In both cases, we achieved the synthesis of MUC6-Tn glycoconjugates at a semi-preparative scale (mg amounts). |
| TextSentencer_T11 |
1312-1451 |
Sentence |
denotes |
These glycoproteins displayed a high level of Tn antigens, although the overall density depends on both enzyme source and protein acceptor. |
| T11 |
1312-1451 |
Sentence |
denotes |
These glycoproteins displayed a high level of Tn antigens, although the overall density depends on both enzyme source and protein acceptor. |
| T11 |
1312-1451 |
Sentence |
denotes |
These glycoproteins displayed a high level of Tn antigens, although the overall density depends on both enzyme source and protein acceptor. |
| TextSentencer_T12 |
1452-1575 |
Sentence |
denotes |
These MUC6-Tn glycoconjugates were recognized by two anti-Tn monoclonal antibodies that are specific to human cancer cells. |
| T12 |
1452-1575 |
Sentence |
denotes |
These MUC6-Tn glycoconjugates were recognized by two anti-Tn monoclonal antibodies that are specific to human cancer cells. |
| T12 |
1452-1575 |
Sentence |
denotes |
These MUC6-Tn glycoconjugates were recognized by two anti-Tn monoclonal antibodies that are specific to human cancer cells. |
| TextSentencer_T13 |
1576-1764 |
Sentence |
denotes |
Moreover, the MUC6-Tn glycoconjugate glycosylated using MCF7 extracts as the ppGalNAc-T source was able to induce immunoglobulin G (IgG) antibodies that recognized a human tumor cell line. |
| T13 |
1576-1764 |
Sentence |
denotes |
Moreover, the MUC6-Tn glycoconjugate glycosylated using MCF7 extracts as the ppGalNAc-T source was able to induce immunoglobulin G (IgG) antibodies that recognized a human tumor cell line. |
| T13 |
1576-1764 |
Sentence |
denotes |
Moreover, the MUC6-Tn glycoconjugate glycosylated using MCF7 extracts as the ppGalNAc-T source was able to induce immunoglobulin G (IgG) antibodies that recognized a human tumor cell line. |
| TextSentencer_T14 |
1765-1988 |
Sentence |
denotes |
In conclusion, the large-scaled production of MUC6 with tumor-relevant glycoforms holds considerable promise for developing effective anticancer vaccines, and further studies of their immunological properties are warranted. |
| T14 |
1765-1988 |
Sentence |
denotes |
In conclusion, the large-scaled production of MUC6 with tumor-relevant glycoforms holds considerable promise for developing effective anticancer vaccines, and further studies of their immunological properties are warranted. |
| T14 |
1765-1988 |
Sentence |
denotes |
In conclusion, the large-scaled production of MUC6 with tumor-relevant glycoforms holds considerable promise for developing effective anticancer vaccines, and further studies of their immunological properties are warranted. |