Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-193 |
Sentence |
denotes |
Addition of beta1-6 GlcNAc branching to the oligosaccharide attached to Asn 772 in the serine protease domain of matriptase plays a pivotal role in its stability and resistance against trypsin. |
T1 |
0-193 |
Sentence |
denotes |
Addition of beta1-6 GlcNAc branching to the oligosaccharide attached to Asn 772 in the serine protease domain of matriptase plays a pivotal role in its stability and resistance against trypsin. |
T1 |
0-193 |
Sentence |
denotes |
Addition of beta1-6 GlcNAc branching to the oligosaccharide attached to Asn 772 in the serine protease domain of matriptase plays a pivotal role in its stability and resistance against trypsin. |
TextSentencer_T2 |
194-367 |
Sentence |
denotes |
beta1-6 GlcNAc branching, a product of N-acetylglucosaminyltransferase V (GnT-V), is a key structure that is associated with malignant transformations and cancer metastasis. |
T2 |
194-367 |
Sentence |
denotes |
beta1-6 GlcNAc branching, a product of N-acetylglucosaminyltransferase V (GnT-V), is a key structure that is associated with malignant transformations and cancer metastasis. |
T2 |
194-367 |
Sentence |
denotes |
beta1-6 GlcNAc branching, a product of N-acetylglucosaminyltransferase V (GnT-V), is a key structure that is associated with malignant transformations and cancer metastasis. |
TextSentencer_T3 |
368-591 |
Sentence |
denotes |
Although a number of reports concerning tumor metastasis-related glycoproteins that contain beta1-6 GlcNAc branching have appeared, the precise function of beta1-6 GlcNAc branching on glycoproteins remains to be elucidated. |
T3 |
368-591 |
Sentence |
denotes |
Although a number of reports concerning tumor metastasis-related glycoproteins that contain beta1-6 GlcNAc branching have appeared, the precise function of beta1-6 GlcNAc branching on glycoproteins remains to be elucidated. |
T3 |
368-591 |
Sentence |
denotes |
Although a number of reports concerning tumor metastasis-related glycoproteins that contain beta1-6 GlcNAc branching have appeared, the precise function of beta1-6 GlcNAc branching on glycoproteins remains to be elucidated. |
TextSentencer_T4 |
592-731 |
Sentence |
denotes |
We previously reported on the importance of beta1-6 GlcNAc branching on matriptase in terms of proteolytic degradation in tumor metastasis. |
T4 |
592-731 |
Sentence |
denotes |
We previously reported on the importance of beta1-6 GlcNAc branching on matriptase in terms of proteolytic degradation in tumor metastasis. |
T4 |
592-731 |
Sentence |
denotes |
We previously reported on the importance of beta1-6 GlcNAc branching on matriptase in terms of proteolytic degradation in tumor metastasis. |
TextSentencer_T5 |
732-1020 |
Sentence |
denotes |
We report here that matriptase purified from GnT-V transfectant (beta1-6 GlcNAc matriptase) binds strongly to L4-PHA, which preferentially recognizes beta1-6 GlcNAc branches of tri- or tetraantennary sugar chains, indicating that the isolated matriptase contains beta1-6 GlcNAc branching. |
T5 |
732-1020 |
Sentence |
denotes |
We report here that matriptase purified from GnT-V transfectant (beta1-6 GlcNAc matriptase) binds strongly to L4-PHA, which preferentially recognizes beta1-6 GlcNAc branches of tri- or tetraantennary sugar chains, indicating that the isolated matriptase contains beta1-6 GlcNAc branching. |
T5 |
732-1020 |
Sentence |
denotes |
We report here that matriptase purified from GnT-V transfectant (beta1-6 GlcNAc matriptase) binds strongly to L4-PHA, which preferentially recognizes beta1-6 GlcNAc branches of tri- or tetraantennary sugar chains, indicating that the isolated matriptase contains beta1-6 GlcNAc branching. |
TextSentencer_T6 |
1021-1177 |
Sentence |
denotes |
The beta1-6 GlcNAc matriptase was resistant to autodegradation, as well as trypsin digestion, compared with matriptase purified from mock-transfected cells. |
T6 |
1021-1177 |
Sentence |
denotes |
The beta1-6 GlcNAc matriptase was resistant to autodegradation, as well as trypsin digestion, compared with matriptase purified from mock-transfected cells. |
T6 |
1021-1177 |
Sentence |
denotes |
The beta1-6 GlcNAc matriptase was resistant to autodegradation, as well as trypsin digestion, compared with matriptase purified from mock-transfected cells. |
TextSentencer_T7 |
1178-1292 |
Sentence |
denotes |
Furthermore, N-glycosidase-F treatment of beta1-6 GlcNAc matriptase greatly reduced its resistance to degradation. |
T7 |
1178-1292 |
Sentence |
denotes |
Furthermore, N-glycosidase-F treatment of beta1-6 GlcNAc matriptase greatly reduced its resistance to degradation. |
T7 |
1178-1292 |
Sentence |
denotes |
Furthermore, N-glycosidase-F treatment of beta1-6 GlcNAc matriptase greatly reduced its resistance to degradation. |
TextSentencer_T8 |
1293-1531 |
Sentence |
denotes |
An analysis of matriptase mutants that do not contain potential N-glycosylation sites clearly shows that the beta1-6 GlcNAc branching on N-glycans attached to Asn 772 in the serine protease domain plays a major role in trypsin resistance. |
T8 |
1293-1531 |
Sentence |
denotes |
An analysis of matriptase mutants that do not contain potential N-glycosylation sites clearly shows that the beta1-6 GlcNAc branching on N-glycans attached to Asn 772 in the serine protease domain plays a major role in trypsin resistance. |
T8 |
1293-1531 |
Sentence |
denotes |
An analysis of matriptase mutants that do not contain potential N-glycosylation sites clearly shows that the beta1-6 GlcNAc branching on N-glycans attached to Asn 772 in the serine protease domain plays a major role in trypsin resistance. |
TextSentencer_T9 |
1532-1682 |
Sentence |
denotes |
This is the first example of a demonstration of a direct relationship between beta1-6 GlcNAc branching and a biological function at the protein level. |
T9 |
1532-1682 |
Sentence |
denotes |
This is the first example of a demonstration of a direct relationship between beta1-6 GlcNAc branching and a biological function at the protein level. |
T9 |
1532-1682 |
Sentence |
denotes |
This is the first example of a demonstration of a direct relationship between beta1-6 GlcNAc branching and a biological function at the protein level. |