PubMed:28747658 JSONTXT

{"project":"LitCoin-entities-OrganismTaxon-PD","denotations":[{"id":"T1","span":{"begin":75,"end":80},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":140,"end":145},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"NCBItxid:11676"},{"id":"A2","pred":"db_id","subj":"T2","obj":"NCBItxid:11676"}],"text":"A single amino acid substitution confers B-cell clonogenic activity to the HIV-1 matrix protein p17.\nRecent data highlight the presence, in HIV-1-seropositive patients with lymphoma, of p17 variants (vp17s) endowed with B-cell clonogenicity, suggesting a role of vp17s in lymphomagenesis. We investigated the mechanisms responsible for the functional disparity on B cells between a wild-type p17 (refp17) and a vp17 named S75X. Here, we show that a single Arginine (R) to Glycine (G) mutation at position 76 in the refp17 backbone (p17R76G), as in the S75X variant, is per se sufficient to confer a B-cell clonogenic potential to the viral protein and modulate, through activation of the PTEN/PI3K/Akt signaling pathway, different molecules involved in apoptosis inhibition (CASP-9, CASP-7, DFF-45, NPM, YWHAZ, Src, PAX2, MAPK8), cell cycle promotion and cancer progression (CDK1, CDK2, CDK8, CHEK1, CHEK2, GSK-3 beta, NPM, PAK1, PP2C-alpha). Moreover, the only R to G mutation at position 76 was found to strongly impact on protein folding and oligomerization by altering the hydrogen bond network. This generates a conformational shift in the p17 R76G mutant which enables a functional epitope(s), masked in refp17, to elicit B-cell growth-promoting signals after its interaction with a still unknown receptor(s). Our findings offer new opportunities to understand the molecular mechanisms accounting for the B-cell growth-promoting activity of vp17s."}

{"project":"LitCoin-sentences","denotations":[{"id":"T1","span":{"begin":0,"end":100},"obj":"Sentence"},{"id":"T2","span":{"begin":101,"end":288},"obj":"Sentence"},{"id":"T3","span":{"begin":289,"end":427},"obj":"Sentence"},{"id":"T4","span":{"begin":428,"end":942},"obj":"Sentence"},{"id":"T5","span":{"begin":943,"end":1099},"obj":"Sentence"},{"id":"T6","span":{"begin":1100,"end":1315},"obj":"Sentence"},{"id":"T7","span":{"begin":1316,"end":1453},"obj":"Sentence"}],"text":"A single amino acid substitution confers B-cell clonogenic activity to the HIV-1 matrix protein p17.\nRecent data highlight the presence, in HIV-1-seropositive patients with lymphoma, of p17 variants (vp17s) endowed with B-cell clonogenicity, suggesting a role of vp17s in lymphomagenesis. We investigated the mechanisms responsible for the functional disparity on B cells between a wild-type p17 (refp17) and a vp17 named S75X. Here, we show that a single Arginine (R) to Glycine (G) mutation at position 76 in the refp17 backbone (p17R76G), as in the S75X variant, is per se sufficient to confer a B-cell clonogenic potential to the viral protein and modulate, through activation of the PTEN/PI3K/Akt signaling pathway, different molecules involved in apoptosis inhibition (CASP-9, CASP-7, DFF-45, NPM, YWHAZ, Src, PAX2, MAPK8), cell cycle promotion and cancer progression (CDK1, CDK2, CDK8, CHEK1, CHEK2, GSK-3 beta, NPM, PAK1, PP2C-alpha). Moreover, the only R to G mutation at position 76 was found to strongly impact on protein folding and oligomerization by altering the hydrogen bond network. This generates a conformational shift in the p17 R76G mutant which enables a functional epitope(s), masked in refp17, to elicit B-cell growth-promoting signals after its interaction with a still unknown receptor(s). Our findings offer new opportunities to understand the molecular mechanisms accounting for the B-cell growth-promoting activity of vp17s."}

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single amino acid substitution confers B-cell clonogenic activity to the HIV-1 matrix protein p17.\nRecent data highlight the presence, in HIV-1-seropositive patients with lymphoma, of p17 variants (vp17s) endowed with B-cell clonogenicity, suggesting a role of vp17s in lymphomagenesis. We investigated the mechanisms responsible for the functional disparity on B cells between a wild-type p17 (refp17) and a vp17 named S75X. Here, we show that a single Arginine (R) to Glycine (G) mutation at position 76 in the refp17 backbone (p17R76G), as in the S75X variant, is per se sufficient to confer a B-cell clonogenic potential to the viral protein and modulate, through activation of the PTEN/PI3K/Akt signaling pathway, different molecules involved in apoptosis inhibition (CASP-9, CASP-7, DFF-45, NPM, YWHAZ, Src, PAX2, MAPK8), cell cycle promotion and cancer progression (CDK1, CDK2, CDK8, CHEK1, CHEK2, GSK-3 beta, NPM, PAK1, PP2C-alpha). Moreover, the only R to G mutation at position 76 was found to strongly impact on protein folding and oligomerization by altering the hydrogen bond network. This generates a conformational shift in the p17 R76G mutant which enables a functional epitope(s), masked in refp17, to elicit B-cell growth-promoting signals after its interaction with a still unknown receptor(s). Our findings offer new opportunities to understand the molecular mechanisms accounting for the B-cell growth-promoting activity of vp17s."}

{"project":"LitCoin_Mondo","denotations":[{"id":"T1","span":{"begin":173,"end":181},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T2","span":{"begin":855,"end":861},"obj":"DiseaseOrPhenotypicFeature"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"0005062"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"0004992"}],"text":"A single amino acid substitution confers B-cell clonogenic activity to the HIV-1 matrix protein p17.\nRecent data highlight the presence, in HIV-1-seropositive patients with lymphoma, of p17 variants (vp17s) endowed with B-cell clonogenicity, suggesting a role of vp17s in lymphomagenesis. We investigated the mechanisms responsible for the functional disparity on B cells between a wild-type p17 (refp17) and a vp17 named S75X. Here, we show that a single Arginine (R) to Glycine (G) mutation at position 76 in the refp17 backbone (p17R76G), as in the S75X variant, is per se sufficient to confer a B-cell clonogenic potential to the viral protein and modulate, through activation of the PTEN/PI3K/Akt signaling pathway, different molecules involved in apoptosis inhibition (CASP-9, CASP-7, DFF-45, NPM, YWHAZ, Src, PAX2, MAPK8), cell cycle promotion and cancer progression (CDK1, CDK2, CDK8, CHEK1, CHEK2, GSK-3 beta, NPM, PAK1, PP2C-alpha). Moreover, the only R to G mutation at position 76 was found to strongly impact on protein folding and oligomerization by altering the hydrogen bond network. This generates a conformational shift in the p17 R76G mutant which enables a functional epitope(s), masked in refp17, to elicit B-cell growth-promoting signals after its interaction with a still unknown receptor(s). Our findings offer new opportunities to understand the molecular mechanisms accounting for the B-cell growth-promoting activity of vp17s."}

{"project":"LitCoin-SeqVar","denotations":[{"id":"T1","span":{"begin":422,"end":426},"obj":"SequenceVariant"},{"id":"T2","span":{"begin":552,"end":556},"obj":"SequenceVariant"},{"id":"T3","span":{"begin":1149,"end":1153},"obj":"SequenceVariant"}],"text":"A single amino acid substitution confers B-cell clonogenic activity to the HIV-1 matrix protein p17.\nRecent data highlight the presence, in HIV-1-seropositive patients with lymphoma, of p17 variants (vp17s) endowed with B-cell clonogenicity, suggesting a role of vp17s in lymphomagenesis. We investigated the mechanisms responsible for the functional disparity on B cells between a wild-type p17 (refp17) and a vp17 named S75X. Here, we show that a single Arginine (R) to Glycine (G) mutation at position 76 in the refp17 backbone (p17R76G), as in the S75X variant, is per se sufficient to confer a B-cell clonogenic potential to the viral protein and modulate, through activation of the PTEN/PI3K/Akt signaling pathway, different molecules involved in apoptosis inhibition (CASP-9, CASP-7, DFF-45, NPM, YWHAZ, Src, PAX2, MAPK8), cell cycle promotion and cancer progression (CDK1, CDK2, CDK8, CHEK1, CHEK2, GSK-3 beta, NPM, PAK1, PP2C-alpha). Moreover, the only R to G mutation at position 76 was found to strongly impact on protein folding and oligomerization by altering the hydrogen bond network. This generates a conformational shift in the p17 R76G mutant which enables a functional epitope(s), masked in refp17, to elicit B-cell growth-promoting signals after its interaction with a still unknown receptor(s). Our findings offer new opportunities to understand the molecular mechanisms accounting for the B-cell growth-promoting activity of vp17s."}

{"project":"LitCoin-GeneOrGeneProduct-v0","denotations":[{"id":"T1","span":{"begin":9,"end":19},"obj":"GeneOrGeneProduct"},{"id":"T2","span":{"begin":43,"end":47},"obj":"GeneOrGeneProduct"},{"id":"T3","span":{"begin":59,"end":67},"obj":"GeneOrGeneProduct"},{"id":"T4","span":{"begin":81,"end":95},"obj":"GeneOrGeneProduct"},{"id":"T5","span":{"begin":222,"end":226},"obj":"GeneOrGeneProduct"},{"id":"T6","span":{"begin":366,"end":371},"obj":"GeneOrGeneProduct"},{"id":"T7","span":{"begin":411,"end":415},"obj":"GeneOrGeneProduct"},{"id":"T8","span":{"begin":484,"end":492},"obj":"GeneOrGeneProduct"},{"id":"T9","span":{"begin":566,"end":572},"obj":"GeneOrGeneProduct"},{"id":"T10","span":{"begin":601,"end":605},"obj":"GeneOrGeneProduct"},{"id":"T11","span":{"begin":634,"end":647},"obj":"GeneOrGeneProduct"},{"id":"T12","span":{"begin":670,"end":680},"obj":"GeneOrGeneProduct"},{"id":"T13","span":{"begin":688,"end":692},"obj":"GeneOrGeneProduct"},{"id":"T14","span":{"begin":693,"end":697},"obj":"GeneOrGeneProduct"},{"id":"T15","span":{"begin":741,"end":762},"obj":"GeneOrGeneProduct"},{"id":"T16","span":{"begin":775,"end":781},"obj":"GeneOrGeneProduct"},{"id":"T17","span":{"begin":783,"end":789},"obj":"GeneOrGeneProduct"},{"id":"T18","span":{"begin":791,"end":797},"obj":"GeneOrGeneProduct"},{"id":"T19","span":{"begin":804,"end":809},"obj":"GeneOrGeneProduct"},{"id":"T20","span":{"begin":816,"end":820},"obj":"GeneOrGeneProduct"},{"id":"T21","span":{"begin":822,"end":827},"obj":"GeneOrGeneProduct"},{"id":"T22","span":{"begin":830,"end":840},"obj":"GeneOrGeneProduct"},{"id":"T23","span":{"begin":875,"end":879},"obj":"GeneOrGeneProduct"},{"id":"T24","span":{"begin":881,"end":885},"obj":"GeneOrGeneProduct"},{"id":"T25","span":{"begin":887,"end":891},"obj":"GeneOrGeneProduct"},{"id":"T26","span":{"begin":893,"end":898},"obj":"GeneOrGeneProduct"},{"id":"T27","span":{"begin":900,"end":905},"obj":"GeneOrGeneProduct"},{"id":"T28","span":{"begin":907,"end":917},"obj":"GeneOrGeneProduct"},{"id":"T29","span":{"begin":924,"end":928},"obj":"GeneOrGeneProduct"},{"id":"T30","span":{"begin":930,"end":940},"obj":"GeneOrGeneProduct"},{"id":"T31","span":{"begin":969,"end":977},"obj":"GeneOrGeneProduct"},{"id":"T32","span":{"begin":1015,"end":1021},"obj":"GeneOrGeneProduct"},{"id":"T33","span":{"begin":1025,"end":1040},"obj":"GeneOrGeneProduct"},{"id":"T34","span":{"begin":1086,"end":1090},"obj":"GeneOrGeneProduct"},{"id":"T35","span":{"begin":1132,"end":1137},"obj":"GeneOrGeneProduct"},{"id":"T36","span":{"begin":1154,"end":1160},"obj":"GeneOrGeneProduct"},{"id":"T37","span":{"begin":1167,"end":1174},"obj":"GeneOrGeneProduct"},{"id":"T38","span":{"begin":1200,"end":1206},"obj":"GeneOrGeneProduct"},{"id":"T39","span":{"begin":1230,"end":1234},"obj":"GeneOrGeneProduct"},{"id":"T40","span":{"begin":1235,"end":1241},"obj":"GeneOrGeneProduct"},{"id":"T41","span":{"begin":1295,"end":1302},"obj":"GeneOrGeneProduct"},{"id":"T42","span":{"begin":1303,"end":1311},"obj":"GeneOrGeneProduct"},{"id":"T43","span":{"begin":1320,"end":1328},"obj":"GeneOrGeneProduct"},{"id":"T44","span":{"begin":1413,"end":1417},"obj":"GeneOrGeneProduct"},{"id":"T45","span":{"begin":1418,"end":1424},"obj":"GeneOrGeneProduct"},{"id":"T46","span":{"begin":1435,"end":1443},"obj":"GeneOrGeneProduct"}],"text":"A single amino acid substitution confers B-cell clonogenic activity to the HIV-1 matrix protein p17.\nRecent data highlight the presence, in HIV-1-seropositive patients with lymphoma, of p17 variants (vp17s) endowed with B-cell clonogenicity, suggesting a role of vp17s in lymphomagenesis. We investigated the mechanisms responsible for the functional disparity on B cells between a wild-type p17 (refp17) and a vp17 named S75X. Here, we show that a single Arginine (R) to Glycine (G) mutation at position 76 in the refp17 backbone (p17R76G), as in the S75X variant, is per se sufficient to confer a B-cell clonogenic potential to the viral protein and modulate, through activation of the PTEN/PI3K/Akt signaling pathway, different molecules involved in apoptosis inhibition (CASP-9, CASP-7, DFF-45, NPM, YWHAZ, Src, PAX2, MAPK8), cell cycle promotion and cancer progression (CDK1, CDK2, CDK8, CHEK1, CHEK2, GSK-3 beta, NPM, PAK1, PP2C-alpha). Moreover, the only R to G mutation at position 76 was found to strongly impact on protein folding and oligomerization by altering the hydrogen bond network. This generates a conformational shift in the p17 R76G mutant which enables a functional epitope(s), masked in refp17, to elicit B-cell growth-promoting signals after its interaction with a still unknown receptor(s). Our findings offer new opportunities to understand the molecular mechanisms accounting for the B-cell growth-promoting activity of vp17s."}

{"project":"LitCoin-GeneOrGeneProduct-v2","denotations":[{"id":"T1","span":{"begin":9,"end":19},"obj":"GeneOrGeneProduct"},{"id":"T2","span":{"begin":43,"end":47},"obj":"GeneOrGeneProduct"},{"id":"T3","span":{"begin":81,"end":95},"obj":"GeneOrGeneProduct"},{"id":"T4","span":{"begin":222,"end":226},"obj":"GeneOrGeneProduct"},{"id":"T5","span":{"begin":601,"end":605},"obj":"GeneOrGeneProduct"},{"id":"T6","span":{"begin":634,"end":647},"obj":"GeneOrGeneProduct"},{"id":"T7","span":{"begin":688,"end":692},"obj":"GeneOrGeneProduct"},{"id":"T8","span":{"begin":693,"end":697},"obj":"GeneOrGeneProduct"},{"id":"T9","span":{"begin":741,"end":762},"obj":"GeneOrGeneProduct"},{"id":"T10","span":{"begin":775,"end":781},"obj":"GeneOrGeneProduct"},{"id":"T11","span":{"begin":783,"end":789},"obj":"GeneOrGeneProduct"},{"id":"T12","span":{"begin":791,"end":797},"obj":"GeneOrGeneProduct"},{"id":"T13","span":{"begin":804,"end":809},"obj":"GeneOrGeneProduct"},{"id":"T14","span":{"begin":816,"end":820},"obj":"GeneOrGeneProduct"},{"id":"T15","span":{"begin":822,"end":827},"obj":"GeneOrGeneProduct"},{"id":"T16","span":{"begin":830,"end":840},"obj":"GeneOrGeneProduct"},{"id":"T17","span":{"begin":875,"end":879},"obj":"GeneOrGeneProduct"},{"id":"T18","span":{"begin":881,"end":885},"obj":"GeneOrGeneProduct"},{"id":"T19","span":{"begin":887,"end":891},"obj":"GeneOrGeneProduct"},{"id":"T20","span":{"begin":893,"end":898},"obj":"GeneOrGeneProduct"},{"id":"T21","span":{"begin":900,"end":905},"obj":"GeneOrGeneProduct"},{"id":"T22","span":{"begin":907,"end":917},"obj":"GeneOrGeneProduct"},{"id":"T23","span":{"begin":924,"end":928},"obj":"GeneOrGeneProduct"},{"id":"T24","span":{"begin":930,"end":940},"obj":"GeneOrGeneProduct"},{"id":"T25","span":{"begin":1015,"end":1021},"obj":"GeneOrGeneProduct"},{"id":"T26","span":{"begin":1025,"end":1040},"obj":"GeneOrGeneProduct"},{"id":"T27","span":{"begin":1086,"end":1090},"obj":"GeneOrGeneProduct"},{"id":"T28","span":{"begin":1154,"end":1160},"obj":"GeneOrGeneProduct"},{"id":"T29","span":{"begin":1230,"end":1234},"obj":"GeneOrGeneProduct"},{"id":"T30","span":{"begin":1235,"end":1241},"obj":"GeneOrGeneProduct"},{"id":"T31","span":{"begin":1295,"end":1302},"obj":"GeneOrGeneProduct"},{"id":"T32","span":{"begin":1303,"end":1311},"obj":"GeneOrGeneProduct"},{"id":"T33","span":{"begin":1413,"end":1417},"obj":"GeneOrGeneProduct"},{"id":"T34","span":{"begin":1418,"end":1424},"obj":"GeneOrGeneProduct"}],"text":"A single amino acid substitution confers B-cell clonogenic activity to the HIV-1 matrix protein p17.\nRecent data highlight the presence, in HIV-1-seropositive patients with lymphoma, of p17 variants (vp17s) endowed with B-cell clonogenicity, suggesting a role of vp17s in lymphomagenesis. We investigated the mechanisms responsible for the functional disparity on B cells between a wild-type p17 (refp17) and a vp17 named S75X. Here, we show that a single Arginine (R) to Glycine (G) mutation at position 76 in the refp17 backbone (p17R76G), as in the S75X variant, is per se sufficient to confer a B-cell clonogenic potential to the viral protein and modulate, through activation of the PTEN/PI3K/Akt signaling pathway, different molecules involved in apoptosis inhibition (CASP-9, CASP-7, DFF-45, NPM, YWHAZ, Src, PAX2, MAPK8), cell cycle promotion and cancer progression (CDK1, CDK2, CDK8, CHEK1, CHEK2, GSK-3 beta, NPM, PAK1, PP2C-alpha). Moreover, the only R to G mutation at position 76 was found to strongly impact on protein folding and oligomerization by altering the hydrogen bond network. This generates a conformational shift in the p17 R76G mutant which enables a functional epitope(s), masked in refp17, to elicit B-cell growth-promoting signals after its interaction with a still unknown receptor(s). Our findings offer new opportunities to understand the molecular mechanisms accounting for the B-cell growth-promoting activity of vp17s."}

{"project":"LitCoin-Disease-MeSH","denotations":[{"id":"T1","span":{"begin":173,"end":181},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T2","span":{"begin":855,"end":861},"obj":"DiseaseOrPhenotypicFeature"}],"attributes":[{"id":"A1","pred":"originalLabel","subj":"T1","obj":"D008223"},{"id":"A2","pred":"originalLabel","subj":"T2","obj":"D009369"}],"text":"A single amino acid substitution confers B-cell clonogenic activity to the HIV-1 matrix protein p17.\nRecent data highlight the presence, in HIV-1-seropositive patients with lymphoma, of p17 variants (vp17s) endowed with B-cell clonogenicity, suggesting a role of vp17s in lymphomagenesis. We investigated the mechanisms responsible for the functional disparity on B cells between a wild-type p17 (refp17) and a vp17 named S75X. Here, we show that a single Arginine (R) to Glycine (G) mutation at position 76 in the refp17 backbone (p17R76G), as in the S75X variant, is per se sufficient to confer a B-cell clonogenic potential to the viral protein and modulate, through activation of the PTEN/PI3K/Akt signaling pathway, different molecules involved in apoptosis inhibition (CASP-9, CASP-7, DFF-45, NPM, YWHAZ, Src, PAX2, MAPK8), cell cycle promotion and cancer progression (CDK1, CDK2, CDK8, CHEK1, CHEK2, GSK-3 beta, NPM, PAK1, PP2C-alpha). Moreover, the only R to G mutation at position 76 was found to strongly impact on protein folding and oligomerization by altering the hydrogen bond network. This generates a conformational shift in the p17 R76G mutant which enables a functional epitope(s), masked in refp17, to elicit B-cell growth-promoting signals after its interaction with a still unknown receptor(s). Our findings offer new opportunities to understand the molecular mechanisms accounting for the B-cell growth-promoting activity of vp17s."}

{"project":"LitCoin-GeneOrGeneProduct-v3","denotations":[{"id":"T1","span":{"begin":81,"end":95},"obj":"GeneOrGeneProduct"},{"id":"T2","span":{"begin":634,"end":647},"obj":"GeneOrGeneProduct"},{"id":"T3","span":{"begin":688,"end":692},"obj":"GeneOrGeneProduct"},{"id":"T4","span":{"begin":693,"end":697},"obj":"GeneOrGeneProduct"},{"id":"T5","span":{"begin":698,"end":701},"obj":"GeneOrGeneProduct"},{"id":"T6","span":{"begin":741,"end":762},"obj":"GeneOrGeneProduct"},{"id":"T7","span":{"begin":775,"end":781},"obj":"GeneOrGeneProduct"},{"id":"T8","span":{"begin":783,"end":789},"obj":"GeneOrGeneProduct"},{"id":"T9","span":{"begin":791,"end":797},"obj":"GeneOrGeneProduct"},{"id":"T10","span":{"begin":804,"end":809},"obj":"GeneOrGeneProduct"},{"id":"T11","span":{"begin":816,"end":820},"obj":"GeneOrGeneProduct"},{"id":"T12","span":{"begin":822,"end":827},"obj":"GeneOrGeneProduct"},{"id":"T13","span":{"begin":875,"end":879},"obj":"GeneOrGeneProduct"},{"id":"T14","span":{"begin":881,"end":885},"obj":"GeneOrGeneProduct"},{"id":"T15","span":{"begin":887,"end":891},"obj":"GeneOrGeneProduct"},{"id":"T16","span":{"begin":893,"end":898},"obj":"GeneOrGeneProduct"},{"id":"T17","span":{"begin":900,"end":905},"obj":"GeneOrGeneProduct"},{"id":"T18","span":{"begin":907,"end":917},"obj":"GeneOrGeneProduct"},{"id":"T19","span":{"begin":924,"end":928},"obj":"GeneOrGeneProduct"},{"id":"T20","span":{"begin":930,"end":940},"obj":"GeneOrGeneProduct"},{"id":"T21","span":{"begin":1025,"end":1040},"obj":"GeneOrGeneProduct"},{"id":"T22","span":{"begin":1086,"end":1090},"obj":"GeneOrGeneProduct"}],"text":"A single amino acid substitution confers B-cell clonogenic activity to the HIV-1 matrix protein p17.\nRecent data highlight the presence, in HIV-1-seropositive patients with lymphoma, of p17 variants (vp17s) endowed with B-cell clonogenicity, suggesting a role of vp17s in lymphomagenesis. We investigated the mechanisms responsible for the functional disparity on B cells between a wild-type p17 (refp17) and a vp17 named S75X. Here, we show that a single Arginine (R) to Glycine (G) mutation at position 76 in the refp17 backbone (p17R76G), as in the S75X variant, is per se sufficient to confer a B-cell clonogenic potential to the viral protein and modulate, through activation of the PTEN/PI3K/Akt signaling pathway, different molecules involved in apoptosis inhibition (CASP-9, CASP-7, DFF-45, NPM, YWHAZ, Src, PAX2, MAPK8), cell cycle promotion and cancer progression (CDK1, CDK2, CDK8, CHEK1, CHEK2, GSK-3 beta, NPM, PAK1, PP2C-alpha). Moreover, the only R to G mutation at position 76 was found to strongly impact on protein folding and oligomerization by altering the hydrogen bond network. This generates a conformational shift in the p17 R76G mutant which enables a functional epitope(s), masked in refp17, to elicit B-cell growth-promoting signals after its interaction with a still unknown receptor(s). Our findings offer new opportunities to understand the molecular mechanisms accounting for the B-cell growth-promoting activity of vp17s."}

{"project":"LitCoin_Mondo_095","denotations":[{"id":"T1","span":{"begin":173,"end":181},"obj":"DiseaseOrPhenotypicFeature"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"0005062"},{"id":"A2","pred":"mondo_id","subj":"T1","obj":"0003660"},{"id":"A3","pred":"mondo_id","subj":"T1","obj":"0003659"}],"text":"A single amino acid substitution confers B-cell clonogenic activity to the HIV-1 matrix protein p17.\nRecent data highlight the presence, in HIV-1-seropositive patients with lymphoma, of p17 variants (vp17s) endowed with B-cell clonogenicity, suggesting a role of vp17s in lymphomagenesis. We investigated the mechanisms responsible for the functional disparity on B cells between a wild-type p17 (refp17) and a vp17 named S75X. Here, we show that a single Arginine (R) to Glycine (G) mutation at position 76 in the refp17 backbone (p17R76G), as in the S75X variant, is per se sufficient to confer a B-cell clonogenic potential to the viral protein and modulate, through activation of the PTEN/PI3K/Akt signaling pathway, different molecules involved in apoptosis inhibition (CASP-9, CASP-7, DFF-45, NPM, YWHAZ, Src, PAX2, MAPK8), cell cycle promotion and cancer progression (CDK1, CDK2, CDK8, CHEK1, CHEK2, GSK-3 beta, NPM, PAK1, PP2C-alpha). Moreover, the only R to G mutation at position 76 was found to strongly impact on protein folding and oligomerization by altering the hydrogen bond network. This generates a conformational shift in the p17 R76G mutant which enables a functional epitope(s), masked in refp17, to elicit B-cell growth-promoting signals after its interaction with a still unknown receptor(s). Our findings offer new opportunities to understand the molecular mechanisms accounting for the B-cell growth-promoting activity of vp17s."}

{"project":"LitCoin-MeSH-Disease-2","denotations":[{"id":"T1","span":{"begin":75,"end":78},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T2","span":{"begin":140,"end":158},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T3","span":{"begin":173,"end":181},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T4","span":{"begin":272,"end":287},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T5","span":{"begin":855,"end":861},"obj":"DiseaseOrPhenotypicFeature"}],"attributes":[{"id":"A1","pred":"ID:","subj":"T1","obj":"DISEASE"},{"id":"A2","pred":"ID:","subj":"T2","obj":"DISEASE"},{"id":"A3","pred":"ID:","subj":"T3","obj":"D008223"},{"id":"A4","pred":"ID:","subj":"T4","obj":"DISEASE"},{"id":"A5","pred":"ID:","subj":"T5","obj":"D009369"}],"text":"A single amino acid substitution confers B-cell clonogenic activity to the HIV-1 matrix protein p17.\nRecent data highlight the presence, in HIV-1-seropositive patients with lymphoma, of p17 variants (vp17s) endowed with B-cell clonogenicity, suggesting a role of vp17s in lymphomagenesis. We investigated the mechanisms responsible for the functional disparity on B cells between a wild-type p17 (refp17) and a vp17 named S75X. Here, we show that a single Arginine (R) to Glycine (G) mutation at position 76 in the refp17 backbone (p17R76G), as in the S75X variant, is per se sufficient to confer a B-cell clonogenic potential to the viral protein and modulate, through activation of the PTEN/PI3K/Akt signaling pathway, different molecules involved in apoptosis inhibition (CASP-9, CASP-7, DFF-45, NPM, YWHAZ, Src, PAX2, MAPK8), cell cycle promotion and cancer progression (CDK1, CDK2, CDK8, CHEK1, CHEK2, GSK-3 beta, NPM, PAK1, PP2C-alpha). Moreover, the only R to G mutation at position 76 was found to strongly impact on protein folding and oligomerization by altering the hydrogen bond network. This generates a conformational shift in the p17 R76G mutant which enables a functional epitope(s), masked in refp17, to elicit B-cell growth-promoting signals after its interaction with a still unknown receptor(s). Our findings offer new opportunities to understand the molecular mechanisms accounting for the B-cell growth-promoting activity of vp17s."}

{"project":"LitCoin-MONDO_bioort2019","denotations":[{"id":"T1","span":{"begin":140,"end":158},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T2","span":{"begin":173,"end":181},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T3","span":{"begin":272,"end":287},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T4","span":{"begin":855,"end":861},"obj":"DiseaseOrPhenotypicFeature"}],"attributes":[{"id":"A1","pred":"#label","subj":"T1","obj":"DISEASE"},{"id":"A2","pred":"#label","subj":"T2","obj":"D008223"},{"id":"A3","pred":"#label","subj":"T3","obj":"DISEASE"},{"id":"A4","pred":"#label","subj":"T4","obj":"D009369"}],"text":"A single amino acid substitution confers B-cell clonogenic activity to the HIV-1 matrix protein p17.\nRecent data highlight the presence, in HIV-1-seropositive patients with lymphoma, of p17 variants (vp17s) endowed with B-cell clonogenicity, suggesting a role of vp17s in lymphomagenesis. We investigated the mechanisms responsible for the functional disparity on B cells between a wild-type p17 (refp17) and a vp17 named S75X. Here, we show that a single Arginine (R) to Glycine (G) mutation at position 76 in the refp17 backbone (p17R76G), as in the S75X variant, is per se sufficient to confer a B-cell clonogenic potential to the viral protein and modulate, through activation of the PTEN/PI3K/Akt signaling pathway, different molecules involved in apoptosis inhibition (CASP-9, CASP-7, DFF-45, NPM, YWHAZ, Src, PAX2, MAPK8), cell cycle promotion and cancer progression (CDK1, CDK2, CDK8, CHEK1, CHEK2, GSK-3 beta, NPM, PAK1, PP2C-alpha). Moreover, the only R to G mutation at position 76 was found to strongly impact on protein folding and oligomerization by altering the hydrogen bond network. This generates a conformational shift in the p17 R76G mutant which enables a functional epitope(s), masked in refp17, to elicit B-cell growth-promoting signals after its interaction with a still unknown receptor(s). Our findings offer new opportunities to understand the molecular mechanisms accounting for the B-cell growth-promoting activity of vp17s."}

{"project":"LitCoin-NCBITaxon-2","denotations":[{"id":"T1","span":{"begin":75,"end":80},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":140,"end":145},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":159,"end":167},"obj":"OrganismTaxon"}],"text":"A single amino acid substitution confers B-cell clonogenic activity to the HIV-1 matrix protein p17.\nRecent data highlight the presence, in HIV-1-seropositive patients with lymphoma, of p17 variants (vp17s) endowed with B-cell clonogenicity, suggesting a role of vp17s in lymphomagenesis. We investigated the mechanisms responsible for the functional disparity on B cells between a wild-type p17 (refp17) and a vp17 named S75X. Here, we show that a single Arginine (R) to Glycine (G) mutation at position 76 in the refp17 backbone (p17R76G), as in the S75X variant, is per se sufficient to confer a B-cell clonogenic potential to the viral protein and modulate, through activation of the PTEN/PI3K/Akt signaling pathway, different molecules involved in apoptosis inhibition (CASP-9, CASP-7, DFF-45, NPM, YWHAZ, Src, PAX2, MAPK8), cell cycle promotion and cancer progression (CDK1, CDK2, CDK8, CHEK1, CHEK2, GSK-3 beta, NPM, PAK1, PP2C-alpha). Moreover, the only R to G mutation at position 76 was found to strongly impact on protein folding and oligomerization by altering the hydrogen bond network. This generates a conformational shift in the p17 R76G mutant which enables a functional epitope(s), masked in refp17, to elicit B-cell growth-promoting signals after its interaction with a still unknown receptor(s). Our findings offer new opportunities to understand the molecular mechanisms accounting for the B-cell growth-promoting activity of vp17s."}

{"project":"LitCoin-Chemical-MeSH-CHEBI","denotations":[{"id":"T1","span":{"begin":456,"end":464},"obj":"ChemicalEntity"},{"id":"T2","span":{"begin":472,"end":479},"obj":"ChemicalEntity"},{"id":"T3","span":{"begin":1077,"end":1085},"obj":"ChemicalEntity"},{"id":"T5","span":{"begin":1188,"end":1195},"obj":"ChemicalEntity"}],"attributes":[{"id":"A1","pred":"ID:","subj":"T1","obj":"http://purl.obolibrary.org/obo/CHEBI_29016"},{"id":"A2","pred":"ID:","subj":"T2","obj":"http://purl.obolibrary.org/obo/CHEBI_15428"},{"id":"A3","pred":"ID:","subj":"T3","obj":"D006859"},{"id":"A4","pred":"ID:","subj":"T3","obj":"http://purl.obolibrary.org/obo/CHEBI_49637"},{"id":"A5","pred":"ID:","subj":"T5","obj":"D000939"}],"text":"A single amino acid substitution confers B-cell clonogenic activity to the HIV-1 matrix protein p17.\nRecent data highlight the presence, in HIV-1-seropositive patients with lymphoma, of p17 variants (vp17s) endowed with B-cell clonogenicity, suggesting a role of vp17s in lymphomagenesis. We investigated the mechanisms responsible for the functional disparity on B cells between a wild-type p17 (refp17) and a vp17 named S75X. Here, we show that a single Arginine (R) to Glycine (G) mutation at position 76 in the refp17 backbone (p17R76G), as in the S75X variant, is per se sufficient to confer a B-cell clonogenic potential to the viral protein and modulate, through activation of the PTEN/PI3K/Akt signaling pathway, different molecules involved in apoptosis inhibition (CASP-9, CASP-7, DFF-45, NPM, YWHAZ, Src, PAX2, MAPK8), cell cycle promotion and cancer progression (CDK1, CDK2, CDK8, CHEK1, CHEK2, GSK-3 beta, NPM, PAK1, PP2C-alpha). Moreover, the only R to G mutation at position 76 was found to strongly impact on protein folding and oligomerization by altering the hydrogen bond network. This generates a conformational shift in the p17 R76G mutant which enables a functional epitope(s), masked in refp17, to elicit B-cell growth-promoting signals after its interaction with a still unknown receptor(s). Our findings offer new opportunities to understand the molecular mechanisms accounting for the B-cell growth-promoting activity of vp17s."}

{"project":"LitCoin-training-merged","denotations":[{"id":"T5","span":{"begin":1188,"end":1195},"obj":"ChemicalEntity"},{"id":"T3","span":{"begin":1077,"end":1085},"obj":"ChemicalEntity"},{"id":"T2","span":{"begin":472,"end":479},"obj":"ChemicalEntity"},{"id":"T1","span":{"begin":456,"end":464},"obj":"ChemicalEntity"},{"id":"T22","span":{"begin":1086,"end":1090},"obj":"GeneOrGeneProduct"},{"id":"T21","span":{"begin":1025,"end":1040},"obj":"GeneOrGeneProduct"},{"id":"T20","span":{"begin":930,"end":940},"obj":"GeneOrGeneProduct"},{"id":"T19","span":{"begin":924,"end":928},"obj":"GeneOrGeneProduct"},{"id":"T18","span":{"begin":907,"end":917},"obj":"GeneOrGeneProduct"},{"id":"T17","span":{"begin":900,"end":905},"obj":"GeneOrGeneProduct"},{"id":"T16","span":{"begin":893,"end":898},"obj":"GeneOrGeneProduct"},{"id":"T15","span":{"begin":887,"end":891},"obj":"GeneOrGeneProduct"},{"id":"T14","span":{"begin":881,"end":885},"obj":"GeneOrGeneProduct"},{"id":"T13","span":{"begin":875,"end":879},"obj":"GeneOrGeneProduct"},{"id":"T12","span":{"begin":822,"end":827},"obj":"GeneOrGeneProduct"},{"id":"T11","span":{"begin":816,"end":820},"obj":"GeneOrGeneProduct"},{"id":"T10","span":{"begin":804,"end":809},"obj":"GeneOrGeneProduct"},{"id":"T9","span":{"begin":791,"end":797},"obj":"GeneOrGeneProduct"},{"id":"T8","span":{"begin":783,"end":789},"obj":"GeneOrGeneProduct"},{"id":"T7","span":{"begin":775,"end":781},"obj":"GeneOrGeneProduct"},{"id":"T6","span":{"begin":741,"end":762},"obj":"GeneOrGeneProduct"},{"id":"T88995","span":{"begin":698,"end":701},"obj":"GeneOrGeneProduct"},{"id":"T4","span":{"begin":693,"end":697},"obj":"GeneOrGeneProduct"},{"id":"T49561","span":{"begin":688,"end":692},"obj":"GeneOrGeneProduct"},{"id":"T33109","span":{"begin":634,"end":647},"obj":"GeneOrGeneProduct"},{"id":"T17656","span":{"begin":81,"end":95},"obj":"GeneOrGeneProduct"},{"id":"T40648","span":{"begin":855,"end":861},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T58876","span":{"begin":272,"end":287},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T95805","span":{"begin":173,"end":181},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T98244","span":{"begin":140,"end":158},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T92018","span":{"begin":159,"end":167},"obj":"OrganismTaxon"},{"id":"T57228","span":{"begin":140,"end":145},"obj":"OrganismTaxon"},{"id":"T50946","span":{"begin":75,"end":80},"obj":"OrganismTaxon"},{"id":"T75572","span":{"begin":1149,"end":1153},"obj":"SequenceVariant"},{"id":"T29712","span":{"begin":552,"end":556},"obj":"SequenceVariant"},{"id":"T47249","span":{"begin":422,"end":426},"obj":"SequenceVariant"}],"attributes":[{"id":"A1","pred":"ID:","subj":"T1","obj":"http://purl.obolibrary.org/obo/CHEBI_29016"},{"id":"A25526","pred":"#label","subj":"T95805","obj":"D008223"},{"id":"A3","pred":"ID:","subj":"T3","obj":"D006859"},{"id":"A4","pred":"ID:","subj":"T3","obj":"http://purl.obolibrary.org/obo/CHEBI_49637"},{"id":"A96010","pred":"#label","subj":"T40648","obj":"D009369"},{"id":"A2","pred":"ID:","subj":"T2","obj":"http://purl.obolibrary.org/obo/CHEBI_15428"},{"id":"A5","pred":"ID:","subj":"T5","obj":"D000939"},{"id":"A1268","pred":"#label","subj":"T98244","obj":"DISEASE"},{"id":"A53756","pred":"#label","subj":"T58876","obj":"DISEASE"}],"text":"A single amino acid substitution confers B-cell clonogenic activity to the HIV-1 matrix protein p17.\nRecent data highlight the presence, in HIV-1-seropositive patients with lymphoma, of p17 variants (vp17s) endowed with B-cell clonogenicity, suggesting a role of vp17s in lymphomagenesis. We investigated the mechanisms responsible for the functional disparity on B cells between a wild-type p17 (refp17) and a vp17 named S75X. Here, we show that a single Arginine (R) to Glycine (G) mutation at position 76 in the refp17 backbone (p17R76G), as in the S75X variant, is per se sufficient to confer a B-cell clonogenic potential to the viral protein and modulate, through activation of the PTEN/PI3K/Akt signaling pathway, different molecules involved in apoptosis inhibition (CASP-9, CASP-7, DFF-45, NPM, YWHAZ, Src, PAX2, MAPK8), cell cycle promotion and cancer progression (CDK1, CDK2, CDK8, CHEK1, CHEK2, GSK-3 beta, NPM, PAK1, PP2C-alpha). Moreover, the only R to G mutation at position 76 was found to strongly impact on protein folding and oligomerization by altering the hydrogen bond network. This generates a conformational shift in the p17 R76G mutant which enables a functional epitope(s), masked in refp17, to elicit B-cell growth-promoting signals after its interaction with a still unknown receptor(s). Our findings offer new opportunities to understand the molecular mechanisms accounting for the B-cell growth-promoting activity of vp17s."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":173,"end":181},"obj":"Disease"},{"id":"T2","span":{"begin":855,"end":861},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0005062"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0004992"}],"text":"A single amino acid substitution confers B-cell clonogenic activity to the HIV-1 matrix protein p17.\nRecent data highlight the presence, in HIV-1-seropositive patients with lymphoma, of p17 variants (vp17s) endowed with B-cell clonogenicity, suggesting a role of vp17s in lymphomagenesis. We investigated the mechanisms responsible for the functional disparity on B cells between a wild-type p17 (refp17) and a vp17 named S75X. Here, we show that a single Arginine (R) to Glycine (G) mutation at position 76 in the refp17 backbone (p17R76G), as in the S75X variant, is per se sufficient to confer a B-cell clonogenic potential to the viral protein and modulate, through activation of the PTEN/PI3K/Akt signaling pathway, different molecules involved in apoptosis inhibition (CASP-9, CASP-7, DFF-45, NPM, YWHAZ, Src, PAX2, MAPK8), cell cycle promotion and cancer progression (CDK1, CDK2, CDK8, CHEK1, CHEK2, GSK-3 beta, NPM, PAK1, PP2C-alpha). Moreover, the only R to G mutation at position 76 was found to strongly impact on protein folding and oligomerization by altering the hydrogen bond network. This generates a conformational shift in the p17 R76G mutant which enables a functional epitope(s), masked in refp17, to elicit B-cell growth-promoting signals after its interaction with a still unknown receptor(s). Our findings offer new opportunities to understand the molecular mechanisms accounting for the B-cell growth-promoting activity of vp17s."}

{"project":"HP-phenotype","denotations":[{"id":"T1","span":{"begin":173,"end":181},"obj":"Phenotype"},{"id":"T2","span":{"begin":855,"end":861},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0002665"},{"id":"A2","pred":"hp_id","subj":"T2","obj":"HP:0002664"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"A single amino acid substitution confers B-cell clonogenic activity to the HIV-1 matrix protein p17.\nRecent data highlight the presence, in HIV-1-seropositive patients with lymphoma, of p17 variants (vp17s) endowed with B-cell clonogenicity, suggesting a role of vp17s in lymphomagenesis. We investigated the mechanisms responsible for the functional disparity on B cells between a wild-type p17 (refp17) and a vp17 named S75X. Here, we show that a single Arginine (R) to Glycine (G) mutation at position 76 in the refp17 backbone (p17R76G), as in the S75X variant, is per se sufficient to confer a B-cell clonogenic potential to the viral protein and modulate, through activation of the PTEN/PI3K/Akt signaling pathway, different molecules involved in apoptosis inhibition (CASP-9, CASP-7, DFF-45, NPM, YWHAZ, Src, PAX2, MAPK8), cell cycle promotion and cancer progression (CDK1, CDK2, CDK8, CHEK1, CHEK2, GSK-3 beta, NPM, PAK1, PP2C-alpha). Moreover, the only R to G mutation at position 76 was found to strongly impact on protein folding and oligomerization by altering the hydrogen bond network. This generates a conformational shift in the p17 R76G mutant which enables a functional epitope(s), masked in refp17, to elicit B-cell growth-promoting signals after its interaction with a still unknown receptor(s). Our findings offer new opportunities to understand the molecular mechanisms accounting for the B-cell growth-promoting activity of vp17s."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":472,"end":479},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"3846"}],"text":"A single amino acid substitution confers B-cell clonogenic activity to the HIV-1 matrix protein p17.\nRecent data highlight the presence, in HIV-1-seropositive patients with lymphoma, of p17 variants (vp17s) endowed with B-cell clonogenicity, suggesting a role of vp17s in lymphomagenesis. We investigated the mechanisms responsible for the functional disparity on B cells between a wild-type p17 (refp17) and a vp17 named S75X. Here, we show that a single Arginine (R) to Glycine (G) mutation at position 76 in the refp17 backbone (p17R76G), as in the S75X variant, is per se sufficient to confer a B-cell clonogenic potential to the viral protein and modulate, through activation of the PTEN/PI3K/Akt signaling pathway, different molecules involved in apoptosis inhibition (CASP-9, CASP-7, DFF-45, NPM, YWHAZ, Src, PAX2, MAPK8), cell cycle promotion and cancer progression (CDK1, CDK2, CDK8, CHEK1, CHEK2, GSK-3 beta, NPM, PAK1, PP2C-alpha). Moreover, the only R to G mutation at position 76 was found to strongly impact on protein folding and oligomerization by altering the hydrogen bond network. This generates a conformational shift in the p17 R76G mutant which enables a functional epitope(s), masked in refp17, to elicit B-cell growth-promoting signals after its interaction with a still unknown receptor(s). Our findings offer new opportunities to understand the molecular mechanisms accounting for the B-cell growth-promoting activity of vp17s."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":41,"end":47},"obj":"Body_part"},{"id":"T2","span":{"begin":220,"end":226},"obj":"Body_part"},{"id":"T3","span":{"begin":522,"end":530},"obj":"Body_part"},{"id":"T4","span":{"begin":599,"end":605},"obj":"Body_part"},{"id":"T5","span":{"begin":830,"end":840},"obj":"Body_part"},{"id":"T6","span":{"begin":1228,"end":1234},"obj":"Body_part"},{"id":"T7","span":{"begin":1411,"end":1417},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000236"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000236"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0001130"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL_0000236"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_2000098"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CL_0000236"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CL_0000236"}],"text":"A single amino acid substitution confers B-cell clonogenic activity to the HIV-1 matrix protein p17.\nRecent data highlight the presence, in HIV-1-seropositive patients with lymphoma, of p17 variants (vp17s) endowed with B-cell clonogenicity, suggesting a role of vp17s in lymphomagenesis. We investigated the mechanisms responsible for the functional disparity on B cells between a wild-type p17 (refp17) and a vp17 named S75X. Here, we show that a single Arginine (R) to Glycine (G) mutation at position 76 in the refp17 backbone (p17R76G), as in the S75X variant, is per se sufficient to confer a B-cell clonogenic potential to the viral protein and modulate, through activation of the PTEN/PI3K/Akt signaling pathway, different molecules involved in apoptosis inhibition (CASP-9, CASP-7, DFF-45, NPM, YWHAZ, Src, PAX2, MAPK8), cell cycle promotion and cancer progression (CDK1, CDK2, CDK8, CHEK1, CHEK2, GSK-3 beta, NPM, PAK1, PP2C-alpha). Moreover, the only R to G mutation at position 76 was found to strongly impact on protein folding and oligomerization by altering the hydrogen bond network. This generates a conformational shift in the p17 R76G mutant which enables a functional epitope(s), masked in refp17, to elicit B-cell growth-promoting signals after its interaction with a still unknown receptor(s). Our findings offer new opportunities to understand the molecular mechanisms accounting for the B-cell growth-promoting activity of vp17s."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":41,"end":47},"obj":"Cell"},{"id":"T2","span":{"begin":220,"end":226},"obj":"Cell"},{"id":"T3","span":{"begin":364,"end":371},"obj":"Cell"},{"id":"T4","span":{"begin":597,"end":605},"obj":"Cell"},{"id":"T5","span":{"begin":599,"end":605},"obj":"Cell"},{"id":"T6","span":{"begin":1228,"end":1234},"obj":"Cell"},{"id":"T7","span":{"begin":1411,"end":1417},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000236"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000236"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000236"},{"id":"A4","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:4023097"},{"id":"A5","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0000236"},{"id":"A6","pred":"cl_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CL:0000236"},{"id":"A7","pred":"cl_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CL:0000236"}],"text":"A single amino acid substitution confers B-cell clonogenic activity to the HIV-1 matrix protein p17.\nRecent data highlight the presence, in HIV-1-seropositive patients with lymphoma, of p17 variants (vp17s) endowed with B-cell clonogenicity, suggesting a role of vp17s in lymphomagenesis. We investigated the mechanisms responsible for the functional disparity on B cells between a wild-type p17 (refp17) and a vp17 named S75X. Here, we show that a single Arginine (R) to Glycine (G) mutation at position 76 in the refp17 backbone (p17R76G), as in the S75X variant, is per se sufficient to confer a B-cell clonogenic potential to the viral protein and modulate, through activation of the PTEN/PI3K/Akt signaling pathway, different molecules involved in apoptosis inhibition (CASP-9, CASP-7, DFF-45, NPM, YWHAZ, Src, PAX2, MAPK8), cell cycle promotion and cancer progression (CDK1, CDK2, CDK8, CHEK1, CHEK2, GSK-3 beta, NPM, PAK1, PP2C-alpha). Moreover, the only R to G mutation at position 76 was found to strongly impact on protein folding and oligomerization by altering the hydrogen bond network. This generates a conformational shift in the p17 R76G mutant which enables a functional epitope(s), masked in refp17, to elicit B-cell growth-promoting signals after its interaction with a still unknown receptor(s). Our findings offer new opportunities to understand the molecular mechanisms accounting for the B-cell growth-promoting activity of vp17s."}