Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-148 |
Sentence |
denotes |
An insulin receptor mutant (Asp707 --> Ala), involved in leprechaunism, is processed and transported to the cell surface but unable to bind insulin. |
TextSentencer_T2 |
149-312 |
Sentence |
denotes |
We have identified a homozygous mutation near the carboxyl terminus of the insulin receptor (IR) alpha subunit from a leprechaun patient, changing Asp707 into Ala. |
TextSentencer_T3 |
313-386 |
Sentence |
denotes |
Fibroblasts from this patient had no high affinity insulin binding sites. |
TextSentencer_T4 |
387-509 |
Sentence |
denotes |
To examine the effect of the mutation on IR properties, the mutant IR was stably expressed in Chinese hamster ovary cells. |
TextSentencer_T5 |
510-632 |
Sentence |
denotes |
Western blot analysis and metabolic labeling showed a normal processing of the mutant receptor to alpha and beta subunits. |
TextSentencer_T6 |
633-900 |
Sentence |
denotes |
No increase in high affinity insulin binding sites was observed on Chinese hamster ovary cells expressing the mutant receptor, and also, affinity cross-linking of 125I-labeled insulin by disuccinimidyl suberate to these cells failed to label the mutant alpha subunit. |
TextSentencer_T7 |
901-1088 |
Sentence |
denotes |
Biotinylation of cell surface proteins by biotin succinimidyl ester resulted in efficient biotinylation of the mutant IR alpha and beta subunits, showing its presence on the cell surface. |
TextSentencer_T8 |
1089-1273 |
Sentence |
denotes |
On solubilization of the mutant insulin receptor in Triton X-100-containing buffers, 125I-insulin was efficiently cross-linked to the receptor alpha subunit by disuccinimidyl suberate. |
TextSentencer_T9 |
1274-1429 |
Sentence |
denotes |
These studies demonstrate that Ala707 IR is normally processed and transported to the cell surface and that the mutation distorts the insulin binding site. |
TextSentencer_T10 |
1430-1459 |
Sentence |
denotes |
Detergent restores this site. |
TextSentencer_T11 |
1460-1618 |
Sentence |
denotes |
This is an example of a naturally occurring mutation in the insulin receptor that affects insulin binding without affecting receptor transport and processing. |
TextSentencer_T12 |
1619-1722 |
Sentence |
denotes |
This mutation points to a major contribution of the alpha subunit carboxyl terminus to insulin binding. |
T1 |
0-148 |
Sentence |
denotes |
An insulin receptor mutant (Asp707 --> Ala), involved in leprechaunism, is processed and transported to the cell surface but unable to bind insulin. |
T2 |
149-312 |
Sentence |
denotes |
We have identified a homozygous mutation near the carboxyl terminus of the insulin receptor (IR) alpha subunit from a leprechaun patient, changing Asp707 into Ala. |
T3 |
313-386 |
Sentence |
denotes |
Fibroblasts from this patient had no high affinity insulin binding sites. |
T4 |
387-509 |
Sentence |
denotes |
To examine the effect of the mutation on IR properties, the mutant IR was stably expressed in Chinese hamster ovary cells. |
T5 |
510-632 |
Sentence |
denotes |
Western blot analysis and metabolic labeling showed a normal processing of the mutant receptor to alpha and beta subunits. |
T6 |
633-900 |
Sentence |
denotes |
No increase in high affinity insulin binding sites was observed on Chinese hamster ovary cells expressing the mutant receptor, and also, affinity cross-linking of 125I-labeled insulin by disuccinimidyl suberate to these cells failed to label the mutant alpha subunit. |
T7 |
901-1088 |
Sentence |
denotes |
Biotinylation of cell surface proteins by biotin succinimidyl ester resulted in efficient biotinylation of the mutant IR alpha and beta subunits, showing its presence on the cell surface. |
T8 |
1089-1273 |
Sentence |
denotes |
On solubilization of the mutant insulin receptor in Triton X-100-containing buffers, 125I-insulin was efficiently cross-linked to the receptor alpha subunit by disuccinimidyl suberate. |
T9 |
1274-1429 |
Sentence |
denotes |
These studies demonstrate that Ala707 IR is normally processed and transported to the cell surface and that the mutation distorts the insulin binding site. |
T10 |
1430-1459 |
Sentence |
denotes |
Detergent restores this site. |
T11 |
1460-1618 |
Sentence |
denotes |
This is an example of a naturally occurring mutation in the insulin receptor that affects insulin binding without affecting receptor transport and processing. |
T12 |
1619-1722 |
Sentence |
denotes |
This mutation points to a major contribution of the alpha subunit carboxyl terminus to insulin binding. |