PubMed:24942733
Annnotations
test-210614
Id | Subject | Object | Predicate | Lexical cue | proteinmutation |
---|---|---|---|---|---|
24942733_0 | 934-940 | ProteinMutation | denotes | G2019S | rs34637584 |
PubTator4TogoVar
Id | Subject | Object | Predicate | Lexical cue | proteinmutation |
---|---|---|---|---|---|
24942733_0 | 934-940 | ProteinMutation | denotes | G2019S | rs34637584 |
sentences
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 0-162 | Sentence | denotes | Arsenite stress down-regulates phosphorylation and 14-3-3 binding of leucine-rich repeat kinase 2 (LRRK2), promoting self-association and cellular redistribution. |
T2 | 163-338 | Sentence | denotes | Mutations in the gene encoding leucine-rich repeat kinase 2 (LRRK2) are a common genetic cause of Parkinson disease, but the mechanisms whereby LRRK2 is regulated are unknown. |
T3 | 339-418 | Sentence | denotes | Phosphorylation of LRRK2 at Ser(910)/Ser(935) mediates interaction with 14-3-3. |
T4 | 419-590 | Sentence | denotes | Pharmacological inhibition of its kinase activity abolishes Ser(910)/Ser(935) phosphorylation and 14-3-3 binding, and this effect is also mimicked by pathogenic mutations. |
T5 | 591-678 | Sentence | denotes | However, physiological situations where dephosphorylation occurs have not been defined. |
T6 | 679-827 | Sentence | denotes | Here, we show that arsenite or H2O2-induced stresses promote loss of Ser(910)/Ser(935) phosphorylation, which is reversed by phosphatase inhibition. |
T7 | 828-971 | Sentence | denotes | Arsenite-induced dephosphorylation is accompanied by loss of 14-3-3 binding and is observed in wild type, G2019S, and kinase-dead D2017A LRRK2. |
T8 | 972-1169 | Sentence | denotes | Arsenite stress stimulates LRRK2 self-association and association with protein phosphatase 1α, decreases kinase activity and GTP binding in vitro, and induces translocation of LRRK2 to centrosomes. |
T9 | 1170-1279 | Sentence | denotes | Our data indicate that signaling events induced by arsenite and oxidative stress may regulate LRRK2 function. |
PubmedHPO
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 261-270 | HP_0001300 | denotes | Parkinson |
T2 | 953-957 | HP_0000365 | denotes | dead |
Allie
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
SS1_24942733_0_0 | 69-97 | expanded | denotes | leucine-rich repeat kinase 2 |
SS2_24942733_0_0 | 99-104 | abbr | denotes | LRRK2 |
SS1_24942733_1_0 | 194-222 | expanded | denotes | leucine-rich repeat kinase 2 |
SS2_24942733_1_0 | 224-229 | abbr | denotes | LRRK2 |
AE1_24942733_0_0 | SS1_24942733_0_0 | SS2_24942733_0_0 | abbreviatedTo | leucine-rich repeat kinase 2,LRRK2 |
AE1_24942733_1_0 | SS1_24942733_1_0 | SS2_24942733_1_0 | abbreviatedTo | leucine-rich repeat kinase 2,LRRK2 |
PubMed_ArguminSci
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 163-338 | DRI_Approach | denotes | Mutations in the gene encoding leucine-rich repeat kinase 2 (LRRK2) are a common genetic cause of Parkinson disease, but the mechanisms whereby LRRK2 is regulated are unknown. |
T2 | 339-418 | DRI_Background | denotes | Phosphorylation of LRRK2 at Ser(910)/Ser(935) mediates interaction with 14-3-3. |
T3 | 419-590 | DRI_Background | denotes | Pharmacological inhibition of its kinase activity abolishes Ser(910)/Ser(935) phosphorylation and 14-3-3 binding, and this effect is also mimicked by pathogenic mutations. |
T4 | 591-678 | DRI_Background | denotes | However, physiological situations where dephosphorylation occurs have not been defined. |
T5 | 679-827 | DRI_Outcome | denotes | Here, we show that arsenite or H2O2-induced stresses promote loss of Ser(910)/Ser(935) phosphorylation, which is reversed by phosphatase inhibition. |
T6 | 828-945 | DRI_Background | denotes | Arsenite-induced dephosphorylation is accompanied by loss of 14-3-3 binding and is observed in wild type, G2019S, and |
T7 | 970-971 | DRI_Background | denotes | . |
T8 | 972-998 | DRI_Background | denotes | Arsenite stress stimulates |
T9 | 1022-1169 | DRI_Background | denotes | and association with protein phosphatase 1α, decreases kinase activity and GTP binding in vitro, and induces translocation of LRRK2 to centrosomes. |
T10 | 1170-1279 | DRI_Approach | denotes | Our data indicate that signaling events induced by arsenite and oxidative stress may regulate LRRK2 function. |
mondo_disease
Id | Subject | Object | Predicate | Lexical cue | mondo_id |
---|---|---|---|---|---|
T1 | 261-278 | Disease | denotes | Parkinson disease | http://purl.obolibrary.org/obo/MONDO_0005180 |
HP-phenotype
Id | Subject | Object | Predicate | Lexical cue | hp_id |
---|---|---|---|---|---|
T1 | 261-270 | Phenotype | denotes | Parkinson | HP:0001300 |
T2 | 1234-1250 | Phenotype | denotes | oxidative stress | HP:0025464 |