Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-199 |
Sentence |
denotes |
Oligosaccharide analysis and molecular modeling of soluble forms of glycoproteins belonging to the Ly-6, scavenger receptor, and immunoglobulin superfamilies expressed in Chinese hamster ovary cells. |
T1 |
0-199 |
Sentence |
denotes |
Oligosaccharide analysis and molecular modeling of soluble forms of glycoproteins belonging to the Ly-6, scavenger receptor, and immunoglobulin superfamilies expressed in Chinese hamster ovary cells. |
T1 |
0-199 |
Sentence |
denotes |
Oligosaccharide analysis and molecular modeling of soluble forms of glycoproteins belonging to the Ly-6, scavenger receptor, and immunoglobulin superfamilies expressed in Chinese hamster ovary cells. |
TextSentencer_T2 |
200-385 |
Sentence |
denotes |
Most cell surface molecules are glycoproteins consisting of linear arrays of globular domains containing stretches of amino acid sequence with similarities to regions in other proteins. |
T2 |
200-385 |
Sentence |
denotes |
Most cell surface molecules are glycoproteins consisting of linear arrays of globular domains containing stretches of amino acid sequence with similarities to regions in other proteins. |
T2 |
200-385 |
Sentence |
denotes |
Most cell surface molecules are glycoproteins consisting of linear arrays of globular domains containing stretches of amino acid sequence with similarities to regions in other proteins. |
TextSentencer_T3 |
386-479 |
Sentence |
denotes |
These conserved regions form the basis for the classification of proteins into superfamilies. |
T3 |
386-479 |
Sentence |
denotes |
These conserved regions form the basis for the classification of proteins into superfamilies. |
T3 |
386-479 |
Sentence |
denotes |
These conserved regions form the basis for the classification of proteins into superfamilies. |
TextSentencer_T4 |
480-889 |
Sentence |
denotes |
Recombinant soluble forms of six leukocyte antigens belonging to the Ly-6 (CD59), scavenger receptor (CD5), and immunoglobulin (CD2, CD48, CD4, and Thy-1) superfamilies were expressed in the same Chinese hamster ovary cell line, thus providing an opportunity to examine the extent to which N-linked oligosaccharide processing might vary in a superfamily-, domain-, or protein-dependent manner in a given cell. |
T4 |
480-889 |
Sentence |
denotes |
Recombinant soluble forms of six leukocyte antigens belonging to the Ly-6 (CD59), scavenger receptor (CD5), and immunoglobulin (CD2, CD48, CD4, and Thy-1) superfamilies were expressed in the same Chinese hamster ovary cell line, thus providing an opportunity to examine the extent to which N-linked oligosaccharide processing might vary in a superfamily-, domain-, or protein-dependent manner in a given cell. |
T4 |
480-889 |
Sentence |
denotes |
Recombinant soluble forms of six leukocyte antigens belonging to the Ly-6 (CD59), scavenger receptor (CD5), and immunoglobulin (CD2, CD48, CD4, and Thy-1) superfamilies were expressed in the same Chinese hamster ovary cell line, thus providing an opportunity to examine the extent to which N-linked oligosaccharide processing might vary in a superfamily-, domain-, or protein-dependent manner in a given cell. |
TextSentencer_T5 |
890-1093 |
Sentence |
denotes |
While we found no evidence for superfamily-specific modifications of the glycans, marked differences were seen in the types of oligosaccharides attached to individual proteins within a given superfamily. |
T5 |
890-1093 |
Sentence |
denotes |
While we found no evidence for superfamily-specific modifications of the glycans, marked differences were seen in the types of oligosaccharides attached to individual proteins within a given superfamily. |
T5 |
890-1093 |
Sentence |
denotes |
While we found no evidence for superfamily-specific modifications of the glycans, marked differences were seen in the types of oligosaccharides attached to individual proteins within a given superfamily. |
TextSentencer_T6 |
1094-1302 |
Sentence |
denotes |
The relative importance of local protein surface properties versus the overall tertiary structure of the molecules in directing this protein-specific variation was examined in the context of molecular models. |
T6 |
1094-1302 |
Sentence |
denotes |
The relative importance of local protein surface properties versus the overall tertiary structure of the molecules in directing this protein-specific variation was examined in the context of molecular models. |
T6 |
1094-1302 |
Sentence |
denotes |
The relative importance of local protein surface properties versus the overall tertiary structure of the molecules in directing this protein-specific variation was examined in the context of molecular models. |
TextSentencer_T7 |
1303-1439 |
Sentence |
denotes |
These were constructed using the 3D structures of the proteins, glycan data from this study, and an oligosaccharide structural database. |
T7 |
1303-1439 |
Sentence |
denotes |
These were constructed using the 3D structures of the proteins, glycan data from this study, and an oligosaccharide structural database. |
T7 |
1303-1439 |
Sentence |
denotes |
These were constructed using the 3D structures of the proteins, glycan data from this study, and an oligosaccharide structural database. |
TextSentencer_T8 |
1440-1625 |
Sentence |
denotes |
The results indicated that both the overall organization of the domains and the local protein structure can have a large bearing on site-specific glycan modification of cells in stasis. |
T8 |
1440-1625 |
Sentence |
denotes |
The results indicated that both the overall organization of the domains and the local protein structure can have a large bearing on site-specific glycan modification of cells in stasis. |
T8 |
1440-1625 |
Sentence |
denotes |
The results indicated that both the overall organization of the domains and the local protein structure can have a large bearing on site-specific glycan modification of cells in stasis. |
TextSentencer_T9 |
1626-1833 |
Sentence |
denotes |
This level of control ensures that the surface of a single cell will display a diverse repertoire of glycans and precludes the presentation of multiple copies of a single oligosaccharide on the cell surface. |
T9 |
1626-1833 |
Sentence |
denotes |
This level of control ensures that the surface of a single cell will display a diverse repertoire of glycans and precludes the presentation of multiple copies of a single oligosaccharide on the cell surface. |
T9 |
1626-1833 |
Sentence |
denotes |
This level of control ensures that the surface of a single cell will display a diverse repertoire of glycans and precludes the presentation of multiple copies of a single oligosaccharide on the cell surface. |
TextSentencer_T10 |
1834-2010 |
Sentence |
denotes |
The glycans invariably shield large regions of the protein surfaces although, for the glycoproteins examined here, these did not hinder the known active sites of the molecules. |
T10 |
1834-2010 |
Sentence |
denotes |
The glycans invariably shield large regions of the protein surfaces although, for the glycoproteins examined here, these did not hinder the known active sites of the molecules. |
T10 |
1834-2010 |
Sentence |
denotes |
The glycans invariably shield large regions of the protein surfaces although, for the glycoproteins examined here, these did not hinder the known active sites of the molecules. |
TextSentencer_T11 |
2011-2185 |
Sentence |
denotes |
The models also indicated that sugars are likely to play a role in the packing of the native cell surface glycoproteins and to limit nonspecific protein-protein interactions. |
T11 |
2011-2185 |
Sentence |
denotes |
The models also indicated that sugars are likely to play a role in the packing of the native cell surface glycoproteins and to limit nonspecific protein-protein interactions. |
T11 |
2011-2185 |
Sentence |
denotes |
The models also indicated that sugars are likely to play a role in the packing of the native cell surface glycoproteins and to limit nonspecific protein-protein interactions. |
TextSentencer_T12 |
2186-2337 |
Sentence |
denotes |
In addition, glycans located close to the cell membrane are likely to affect crucially the orientation of the glycoproteins to which they are attached. |
T12 |
2186-2337 |
Sentence |
denotes |
In addition, glycans located close to the cell membrane are likely to affect crucially the orientation of the glycoproteins to which they are attached. |
T12 |
2186-2337 |
Sentence |
denotes |
In addition, glycans located close to the cell membrane are likely to affect crucially the orientation of the glycoproteins to which they are attached. |