| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-181 |
Sentence |
denotes |
Spectrin cagliari. an Ala-->Gly substitution in helix 1 of beta spectrin repeat 17 that severely disrupts the structure and self-association of the erythrocyte spectrin heterodimer. |
| T2 |
182-352 |
Sentence |
denotes |
The spectrin tetramer, the principal structural element of the red cell membrane skeleton, is formed by stable head-to-head self-association of two spectrin heterodimers. |
| T3 |
353-595 |
Sentence |
denotes |
The self-association site appears to be formed by interactions between helices 1 and 2 of beta spectrin repeat 17 of one dimer with helix 3 of alpha spectrin repeat 1 of the other dimer to form two combined alpha-beta triple-helical segments. |
| T4 |
596-675 |
Sentence |
denotes |
The head of the heterodimer appears to involve similar intradimer interactions. |
| T5 |
676-871 |
Sentence |
denotes |
We describe the first example of an amino acid substitution in helix 1 of this combined alpha-beta triple-helical segment, which, although relatively minor, profoundly impairs tetramer formation. |
| T6 |
872-1059 |
Sentence |
denotes |
Strikingly, low angle rotary shadowing electron microscopy of isolated spectrin dimers reveals that this mutation also severely disrupts the head of the heterodimer causing it to be open. |
| T7 |
1060-1293 |
Sentence |
denotes |
Following linkage studies which were most consistent with a beta spectrin gene mutation, a nucleotide change was identified in codon 2018, resulting in an Ala-->Gly substitution in the first helical domain of beta spectrin repeat 17. |
| T8 |
1294-1413 |
Sentence |
denotes |
Because glycine is a strong helix breaker, this change is predicted to disrupt the conformation of this helical domain. |
| T9 |
1414-1654 |
Sentence |
denotes |
Our results indicate that this helical domain must play direct roles in the alpha-beta interdimer interactions that form the self-association site of the tetramer and in the alpha-beta intradimer interactions at the head of the heterodimer. |
| T1 |
0-181 |
Sentence |
denotes |
Spectrin cagliari. an Ala-->Gly substitution in helix 1 of beta spectrin repeat 17 that severely disrupts the structure and self-association of the erythrocyte spectrin heterodimer. |
| T2 |
182-352 |
Sentence |
denotes |
The spectrin tetramer, the principal structural element of the red cell membrane skeleton, is formed by stable head-to-head self-association of two spectrin heterodimers. |
| T3 |
353-595 |
Sentence |
denotes |
The self-association site appears to be formed by interactions between helices 1 and 2 of beta spectrin repeat 17 of one dimer with helix 3 of alpha spectrin repeat 1 of the other dimer to form two combined alpha-beta triple-helical segments. |
| T4 |
596-675 |
Sentence |
denotes |
The head of the heterodimer appears to involve similar intradimer interactions. |
| T5 |
676-871 |
Sentence |
denotes |
We describe the first example of an amino acid substitution in helix 1 of this combined alpha-beta triple-helical segment, which, although relatively minor, profoundly impairs tetramer formation. |
| T6 |
872-1059 |
Sentence |
denotes |
Strikingly, low angle rotary shadowing electron microscopy of isolated spectrin dimers reveals that this mutation also severely disrupts the head of the heterodimer causing it to be open. |
| T7 |
1060-1293 |
Sentence |
denotes |
Following linkage studies which were most consistent with a beta spectrin gene mutation, a nucleotide change was identified in codon 2018, resulting in an Ala-->Gly substitution in the first helical domain of beta spectrin repeat 17. |
| T8 |
1294-1413 |
Sentence |
denotes |
Because glycine is a strong helix breaker, this change is predicted to disrupt the conformation of this helical domain. |
| T9 |
1414-1654 |
Sentence |
denotes |
Our results indicate that this helical domain must play direct roles in the alpha-beta interdimer interactions that form the self-association site of the tetramer and in the alpha-beta intradimer interactions at the head of the heterodimer. |