PubMed:16267041
Annnotations
sentences
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 0-69 | Sentence | denotes | The role of the epsilon subunit in the Escherichia coli ATP synthase. |
T2 | 70-134 | Sentence | denotes | The C-terminal domain is required for efficient energy coupling. |
T3 | 135-387 | Sentence | denotes | The role of the C-domain of the epsilon subunit of ATP synthase was investigated by fusing either the 20-kDa flavodoxin (Fd) or the 5-kDa chitin binding domain (CBD) to the N termini of both full-length epsilon and a truncation mutant epsilon(88-stop). |
T4 | 388-465 | Sentence | denotes | All mutant epsilon proteins were stable in cells and supported F1F0 assembly. |
T5 | 466-681 | Sentence | denotes | Cells expressing the Fd-epsilon or Fd-epsilon(88-stop) mutants were unable to grow on acetate minimal medium, indicating their inability to carry out oxidative phosphorylation because of steric blockage of rotation. |
T6 | 682-737 | Sentence | denotes | The other forms of epsilon supported growth on acetate. |
T7 | 738-915 | Sentence | denotes | Membrane vesicles containing Fd-epsilon showed 23% of the wild type ATPase activity but no proton pumping, suggesting that the ATP synthase is intrinsically partially uncoupled. |
T8 | 916-1100 | Sentence | denotes | Vesicles containing CBD-epsilon were indistinguishable from the wild type in ATPase activity and proton pumping, indicating that the N-terminal fusions alone do not promote uncoupling. |
T9 | 1101-1320 | Sentence | denotes | Fd-epsilon(88-stop) caused higher rates of uncoupled ATP hydrolysis than Fd-epsilon, and epsilon(88-stop) showed an increased rate of membrane-bound ATP hydrolysis but decreased proton pumping relative to the wild type. |
T10 | 1321-1383 | Sentence | denotes | Both results demonstrate the role of the C-domain in coupling. |
T11 | 1384-1611 | Sentence | denotes | Analysis of the wild type and epsilon(88-stop) mutant membrane ATPase activities at concentrations of ATP from 50 mum to 8 mm showed no significant dependence of the ratio of bound/released ATPase activity on ATP concentration. |
T12 | 1612-1809 | Sentence | denotes | These results support the hypothesis that the main function of the C-domain in the Escherichia coli epsilon subunit is to reduce uncoupled ATPase activity, rather than to regulate coupled activity. |
mondo_disease
Id | Subject | Object | Predicate | Lexical cue | mondo_id |
---|---|---|---|---|---|
T1 | 296-299 | Disease | denotes | CBD | http://purl.obolibrary.org/obo/MONDO_0010564 |
T2 | 936-939 | Disease | denotes | CBD | http://purl.obolibrary.org/obo/MONDO_0010564 |
Glycan-GlyCosmos
Id | Subject | Object | Predicate | Lexical cue | image |
---|---|---|---|---|---|
T1 | 273-279 | Glycan | denotes | chitin | https://api.glycosmos.org/wurcs2image/latest/png/binary/G97099AY |
GlyCosmos15-MONDO
Id | Subject | Object | Predicate | Lexical cue | mondo_id |
---|---|---|---|---|---|
T1 | 296-299 | Disease | denotes | CBD | http://purl.obolibrary.org/obo/MONDO_0010564 |
T2 | 936-939 | Disease | denotes | CBD | http://purl.obolibrary.org/obo/MONDO_0010564 |
GlyCosmos15-NCBITAXON
Id | Subject | Object | Predicate | Lexical cue | db_id |
---|---|---|---|---|---|
T1 | 39-55 | OrganismTaxon | denotes | Escherichia coli | 562 |
T2 | 1498-1501 | OrganismTaxon | denotes | mum | 41568 |
T3 | 1695-1711 | OrganismTaxon | denotes | Escherichia coli | 562 |
GlyCosmos15-CL
Id | Subject | Object | Predicate | Lexical cue | cl_id |
---|---|---|---|---|---|
T1 | 16-23 | Cell | denotes | epsilon | http://purl.obolibrary.org/obo/CL:0003025 |
T2 | 167-174 | Cell | denotes | epsilon | http://purl.obolibrary.org/obo/CL:0003025 |
T3 | 338-345 | Cell | denotes | epsilon | http://purl.obolibrary.org/obo/CL:0003025 |
T4 | 370-377 | Cell | denotes | epsilon | http://purl.obolibrary.org/obo/CL:0003025 |
T5 | 399-406 | Cell | denotes | epsilon | http://purl.obolibrary.org/obo/CL:0003025 |
T6 | 490-497 | Cell | denotes | epsilon | http://purl.obolibrary.org/obo/CL:0003025 |
T7 | 504-511 | Cell | denotes | epsilon | http://purl.obolibrary.org/obo/CL:0003025 |
T8 | 701-708 | Cell | denotes | epsilon | http://purl.obolibrary.org/obo/CL:0003025 |
T9 | 770-777 | Cell | denotes | epsilon | http://purl.obolibrary.org/obo/CL:0003025 |
T10 | 940-947 | Cell | denotes | epsilon | http://purl.obolibrary.org/obo/CL:0003025 |
T11 | 1104-1111 | Cell | denotes | epsilon | http://purl.obolibrary.org/obo/CL:0003025 |
T12 | 1177-1184 | Cell | denotes | epsilon | http://purl.obolibrary.org/obo/CL:0003025 |
T13 | 1190-1197 | Cell | denotes | epsilon | http://purl.obolibrary.org/obo/CL:0003025 |
T14 | 1414-1421 | Cell | denotes | epsilon | http://purl.obolibrary.org/obo/CL:0003025 |
T15 | 1712-1719 | Cell | denotes | epsilon | http://purl.obolibrary.org/obo/CL:0003025 |
GlyCosmos15-UBERON
Id | Subject | Object | Predicate | Lexical cue | uberon_id |
---|---|---|---|---|---|
T1 | 738-746 | Body_part | denotes | Membrane | http://purl.obolibrary.org/obo/GO_0016020|http://purl.obolibrary.org/obo/UBERON_0000094|http://purl.obolibrary.org/obo/UBERON_0000158 |
T4 | 1235-1243 | Body_part | denotes | membrane | http://purl.obolibrary.org/obo/GO_0016020|http://purl.obolibrary.org/obo/UBERON_0000094|http://purl.obolibrary.org/obo/UBERON_0000158 |
T7 | 1438-1446 | Body_part | denotes | membrane | http://purl.obolibrary.org/obo/GO_0016020|http://purl.obolibrary.org/obo/UBERON_0000094|http://purl.obolibrary.org/obo/UBERON_0000158 |
sentences
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 0-69 | Sentence | denotes | The role of the epsilon subunit in the Escherichia coli ATP synthase. |
T2 | 70-134 | Sentence | denotes | The C-terminal domain is required for efficient energy coupling. |
T3 | 135-387 | Sentence | denotes | The role of the C-domain of the epsilon subunit of ATP synthase was investigated by fusing either the 20-kDa flavodoxin (Fd) or the 5-kDa chitin binding domain (CBD) to the N termini of both full-length epsilon and a truncation mutant epsilon(88-stop). |
T4 | 388-465 | Sentence | denotes | All mutant epsilon proteins were stable in cells and supported F1F0 assembly. |
T5 | 466-681 | Sentence | denotes | Cells expressing the Fd-epsilon or Fd-epsilon(88-stop) mutants were unable to grow on acetate minimal medium, indicating their inability to carry out oxidative phosphorylation because of steric blockage of rotation. |
T6 | 682-737 | Sentence | denotes | The other forms of epsilon supported growth on acetate. |
T7 | 738-915 | Sentence | denotes | Membrane vesicles containing Fd-epsilon showed 23% of the wild type ATPase activity but no proton pumping, suggesting that the ATP synthase is intrinsically partially uncoupled. |
T8 | 916-1100 | Sentence | denotes | Vesicles containing CBD-epsilon were indistinguishable from the wild type in ATPase activity and proton pumping, indicating that the N-terminal fusions alone do not promote uncoupling. |
T9 | 1101-1320 | Sentence | denotes | Fd-epsilon(88-stop) caused higher rates of uncoupled ATP hydrolysis than Fd-epsilon, and epsilon(88-stop) showed an increased rate of membrane-bound ATP hydrolysis but decreased proton pumping relative to the wild type. |
T10 | 1321-1383 | Sentence | denotes | Both results demonstrate the role of the C-domain in coupling. |
T11 | 1384-1611 | Sentence | denotes | Analysis of the wild type and epsilon(88-stop) mutant membrane ATPase activities at concentrations of ATP from 50 mum to 8 mm showed no significant dependence of the ratio of bound/released ATPase activity on ATP concentration. |
T12 | 1612-1809 | Sentence | denotes | These results support the hypothesis that the main function of the C-domain in the Escherichia coli epsilon subunit is to reduce uncoupled ATPase activity, rather than to regulate coupled activity. |
GlyCosmos15-Sentences
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 0-69 | Sentence | denotes | The role of the epsilon subunit in the Escherichia coli ATP synthase. |
T2 | 70-134 | Sentence | denotes | The C-terminal domain is required for efficient energy coupling. |
T3 | 135-387 | Sentence | denotes | The role of the C-domain of the epsilon subunit of ATP synthase was investigated by fusing either the 20-kDa flavodoxin (Fd) or the 5-kDa chitin binding domain (CBD) to the N termini of both full-length epsilon and a truncation mutant epsilon(88-stop). |
T4 | 388-465 | Sentence | denotes | All mutant epsilon proteins were stable in cells and supported F1F0 assembly. |
T5 | 466-681 | Sentence | denotes | Cells expressing the Fd-epsilon or Fd-epsilon(88-stop) mutants were unable to grow on acetate minimal medium, indicating their inability to carry out oxidative phosphorylation because of steric blockage of rotation. |
T6 | 682-737 | Sentence | denotes | The other forms of epsilon supported growth on acetate. |
T7 | 738-915 | Sentence | denotes | Membrane vesicles containing Fd-epsilon showed 23% of the wild type ATPase activity but no proton pumping, suggesting that the ATP synthase is intrinsically partially uncoupled. |
T8 | 916-1100 | Sentence | denotes | Vesicles containing CBD-epsilon were indistinguishable from the wild type in ATPase activity and proton pumping, indicating that the N-terminal fusions alone do not promote uncoupling. |
T9 | 1101-1320 | Sentence | denotes | Fd-epsilon(88-stop) caused higher rates of uncoupled ATP hydrolysis than Fd-epsilon, and epsilon(88-stop) showed an increased rate of membrane-bound ATP hydrolysis but decreased proton pumping relative to the wild type. |
T10 | 1321-1383 | Sentence | denotes | Both results demonstrate the role of the C-domain in coupling. |
T11 | 1384-1611 | Sentence | denotes | Analysis of the wild type and epsilon(88-stop) mutant membrane ATPase activities at concentrations of ATP from 50 mum to 8 mm showed no significant dependence of the ratio of bound/released ATPase activity on ATP concentration. |
T12 | 1612-1809 | Sentence | denotes | These results support the hypothesis that the main function of the C-domain in the Escherichia coli epsilon subunit is to reduce uncoupled ATPase activity, rather than to regulate coupled activity. |
GlyCosmos15-Glycan
Id | Subject | Object | Predicate | Lexical cue | image |
---|---|---|---|---|---|
T1 | 273-279 | Glycan | denotes | chitin | https://api.glycosmos.org/wurcs2image/latest/png/binary/G97099AY |
NCBITAXON
Id | Subject | Object | Predicate | Lexical cue | db_id |
---|---|---|---|---|---|
T1 | 39-55 | OrganismTaxon | denotes | Escherichia coli | 562 |
T2 | 1498-1501 | OrganismTaxon | denotes | mum | 41568 |
T3 | 1695-1711 | OrganismTaxon | denotes | Escherichia coli | 562 |
Anatomy-UBERON
Id | Subject | Object | Predicate | Lexical cue | uberon_id |
---|---|---|---|---|---|
T1 | 738-746 | Body_part | denotes | Membrane | http://purl.obolibrary.org/obo/GO_0016020|http://purl.obolibrary.org/obo/UBERON_0000094|http://purl.obolibrary.org/obo/UBERON_0000158 |
T4 | 1235-1243 | Body_part | denotes | membrane | http://purl.obolibrary.org/obo/GO_0016020|http://purl.obolibrary.org/obo/UBERON_0000094|http://purl.obolibrary.org/obo/UBERON_0000158 |
T7 | 1438-1446 | Body_part | denotes | membrane | http://purl.obolibrary.org/obo/GO_0016020|http://purl.obolibrary.org/obo/UBERON_0000094|http://purl.obolibrary.org/obo/UBERON_0000158 |
CL-cell
Id | Subject | Object | Predicate | Lexical cue | cl_id |
---|---|---|---|---|---|
T1 | 16-23 | Cell | denotes | epsilon | http://purl.obolibrary.org/obo/CL:0003025 |
T2 | 167-174 | Cell | denotes | epsilon | http://purl.obolibrary.org/obo/CL:0003025 |
T3 | 338-345 | Cell | denotes | epsilon | http://purl.obolibrary.org/obo/CL:0003025 |
T4 | 370-377 | Cell | denotes | epsilon | http://purl.obolibrary.org/obo/CL:0003025 |
T5 | 399-406 | Cell | denotes | epsilon | http://purl.obolibrary.org/obo/CL:0003025 |
T6 | 490-497 | Cell | denotes | epsilon | http://purl.obolibrary.org/obo/CL:0003025 |
T7 | 504-511 | Cell | denotes | epsilon | http://purl.obolibrary.org/obo/CL:0003025 |
T8 | 701-708 | Cell | denotes | epsilon | http://purl.obolibrary.org/obo/CL:0003025 |
T9 | 770-777 | Cell | denotes | epsilon | http://purl.obolibrary.org/obo/CL:0003025 |
T10 | 940-947 | Cell | denotes | epsilon | http://purl.obolibrary.org/obo/CL:0003025 |
T11 | 1104-1111 | Cell | denotes | epsilon | http://purl.obolibrary.org/obo/CL:0003025 |
T12 | 1177-1184 | Cell | denotes | epsilon | http://purl.obolibrary.org/obo/CL:0003025 |
T13 | 1190-1197 | Cell | denotes | epsilon | http://purl.obolibrary.org/obo/CL:0003025 |
T14 | 1414-1421 | Cell | denotes | epsilon | http://purl.obolibrary.org/obo/CL:0003025 |
T15 | 1712-1719 | Cell | denotes | epsilon | http://purl.obolibrary.org/obo/CL:0003025 |