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DS.d1350 | 18820241 | [
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DS.d1355 | 18820913 | [
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DS.d1356 | 18821018 | [
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DS.d1359 | 18821127 | [
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DS.d1363 | 18822099 | [
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] | [] | [] | [] |
DS.d1370 | 18823436 | [
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DS.d1371 | 18823687 | [
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DS.d1372 | 18823722 | [
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DS.d1373 | 18823727 | [
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DS.d1375 | 18823877 | [
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] | [] | [] | [] |
DS.d1376 | 18823890 | [
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DS.d1377 | 18823964 | [
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DS.d1378 | 18824011 | [
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] | [] | [] | [] |
DS.d1379 | 18824106 | [
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DS.d1380 | 18824121 | [
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] | [] | [] | [] |
DS.d1383 | 18824476 | [
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] |
DS.d1384 | 18824496 | [
{
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}
] |
DS.d1385 | 18824518 | [
{
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173,
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] |
DS.d1386 | 18824524 | [
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] |
DS.d1387 | 18824527 | [
{
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] | [] | [] | [
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] |
DS.d1388 | 18824596 | [
{
"id": "DS.d1388.s0",
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"text": [
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],
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] | [] | [] | [
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}
] |
DS.d1389 | 18824635 | [
{
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"text": [
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],
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] | [
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] | [] | [] | [
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] |
DS.d1390 | 18825162 | [
{
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"text": [
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],
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] | [] | [] | [] |
DS.d1391 | 18825163 | [
{
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"text": [
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],
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},
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{
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"text": [
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],
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]
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] | [] | [] | [] |
DS.d1393 | 18825335 | [
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DS.d1394 | 18825368 | [
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] | [] | [] | [] |
DS.d1395 | 18825380 | [
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DS.d1396 | 18825527 | [
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"Eight newly synthesized carbacylamidophosphates with the general formula RC(O) NHP (O) Cl2 with R = pCl-C6H4 1a, pBr-C6H4 2a, C6H5 3a, and pMe-C6H4 4a and RC(O) NHP (O)(NC4H8O)2 R = pCl-C6H4 1b, pBr-C6H4 2b, C6H5 3b, pMe-C6H4 4b, were selected to compare the inhibition kinetic parameters, IC50, Ki, kp and KD, on human erythrocyte acetylcholinesterase (hAChE) and bovine serum butyrylcholinesterase (BuChE), Also, the in vivo inhibition potency of compound 2a, 2b and 3a, were studied."
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] | [] | [] | [] |
DS.d1397 | 18825528 | [
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"text": [
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] | [] | [] | [] |
DS.d1398 | 18825531 | [
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}
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DS.d1399 | 18825537 | [
{
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DS.d1400 | 18825553 | [
{
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]
}
] | [] | [] | [] |
DS.d1401 | 18825555 | [
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],
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]
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DS.d1409 | 18827746 | [
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DS.d1410 | 18827747 | [
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DS.d1412 | 18828007 | [
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DS.d1416 | 18829132 | [
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DS.d1418 | 18829281 | [
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DS.d1419 | 18829286 | [
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DS.d1420 | 18829287 | [
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DS.d1421 | 18829372 | [
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DS.d1422 | 18829677 | [
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DS.d1423 | 18829704 | [
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DS.d1424 | 18829979 | [
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] | [] | [] | [] |
DS.d1425 | 18830228 | [
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DS.d1426 | 18830381 | [
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] | [] | [] | [] |
DS.d1427 | 18830594 | [
{
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"type": "compound",
"text": [
"cAMP"
],
"offsets": [
[
68,
72
]
],
"normalized": [
{
"db_name": "PubChem",
"db_id": "6076"
}
]
},
{
"id": "DS.d1427.s0.e2",
"type": "protein",
"text": [
"CREB"
],
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77,
81
]
],
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"db_id": "P15337"
},
{
"db_name": "UniProt",
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},
{
"db_name": "UniProt",
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},
{
"db_name": "UniProt",
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},
{
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"db_id": "P51985"
},
{
"db_name": "UniProt",
"db_id": "Q01147"
}
]
}
] | [] | [] | [
{
"id": "DS.d1427.s0.i0",
"type": "compound-protein-interaction",
"arg1_id": "DS.d1427.s0.e0",
"arg2_id": "DS.d1427.s0.e2",
"normalized": []
}
] |
DS.d1428 | 18830620 | [
{
"id": "DS.d1428.s0",
"type": "",
"text": [
"Complex modulation of L-type Ca(2+) current inactivation by sorcin in isolated rabbit cardiomyocytes."
],
"offsets": [
[
0,
101
]
]
}
] | [
{
"id": "DS.d1428.s0.e0",
"type": "compound",
"text": [
"Ca(2"
],
"offsets": [
[
29,
33
]
],
"normalized": [
{
"db_name": "PubChem",
"db_id": "271"
}
]
},
{
"id": "DS.d1428.s0.e1",
"type": "protein",
"text": [
"sorcin"
],
"offsets": [
[
60,
66
]
],
"normalized": [
{
"db_name": "UniProt",
"db_id": "P05044"
},
{
"db_name": "UniProt",
"db_id": "P30626"
},
{
"db_name": "UniProt",
"db_id": "Q5R4U9"
},
{
"db_name": "UniProt",
"db_id": "Q6P069"
},
{
"db_name": "UniProt",
"db_id": "Q94743"
}
]
}
] | [] | [] | [
{
"id": "DS.d1428.s0.i0",
"type": "compound-protein-interaction",
"arg1_id": "DS.d1428.s0.e0",
"arg2_id": "DS.d1428.s0.e1",
"normalized": []
}
] |
DS.d1429 | 18830680 | [
{
"id": "DS.d1429.s0",
"type": "",
"text": [
"Donor testicular cells were prepared from heterozygous chicken beta actin (CAG)/enhanced green fluorescent protein (EGFP)-transgenic rats (EGFP Tg rats) during the second week after birth and injected into the seminiferous tubules of the MT-myc Tg rats (line-A and-B; both subfertile) or rats pretreated with busulfan to remove endogenous spermatogonia."
],
"offsets": [
[
0,
353
]
]
}
] | [
{
"id": "DS.d1429.s0.e0",
"type": "protein",
"text": [
"beta actin"
],
"offsets": [
[
63,
73
]
],
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"db_id": "O18840"
},
{
"db_name": "UniProt",
"db_id": "O42161"
},
{
"db_name": "UniProt",
"db_id": "O93400"
},
{
"db_name": "UniProt",
"db_id": "P15475"
},
{
"db_name": "UniProt",
"db_id": "P29751"
},
{
"db_name": "UniProt",
"db_id": "P48975"
},
{
"db_name": "UniProt",
"db_id": "P60706"
},
{
"db_name": "UniProt",
"db_id": "P60707"
},
{
"db_name": "UniProt",
"db_id": "P60708"
},
{
"db_name": "UniProt",
"db_id": "P60709"
},
{
"db_name": "UniProt",
"db_id": "P60710"
},
{
"db_name": "UniProt",
"db_id": "P60711"
},
{
"db_name": "UniProt",
"db_id": "P60712"
},
{
"db_name": "UniProt",
"db_id": "P60713"
},
{
"db_name": "UniProt",
"db_id": "P68143"
},
{
"db_name": "UniProt",
"db_id": "P79818"
},
{
"db_name": "UniProt",
"db_id": "P83750"
},
{
"db_name": "UniProt",
"db_id": "P83751"
},
{
"db_name": "UniProt",
"db_id": "P84336"
},
{
"db_name": "UniProt",
"db_id": "P84856"
},
{
"db_name": "UniProt",
"db_id": "Q0PGG4"
},
{
"db_name": "UniProt",
"db_id": "Q4L0Y2"
},
{
"db_name": "UniProt",
"db_id": "Q5R1X3"
},
{
"db_name": "UniProt",
"db_id": "Q711N9"
},
{
"db_name": "UniProt",
"db_id": "Q71FK5"
},
{
"db_name": "UniProt",
"db_id": "Q76N69"
},
{
"db_name": "UniProt",
"db_id": "Q91ZK5"
},
{
"db_name": "UniProt",
"db_id": "Q9Y702"
}
]
},
{
"id": "DS.d1429.s0.e1",
"type": "protein",
"text": [
"CAG"
],
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[
75,
78
]
],
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{
"db_name": "UniProt",
"db_id": "Q00398"
}
]
},
{
"id": "DS.d1429.s0.e2",
"type": "protein",
"text": [
"green fluorescent protein"
],
"offsets": [
[
89,
114
]
],
"normalized": [
{
"db_name": "UniProt",
"db_id": "P42212"
}
]
},
{
"id": "DS.d1429.s0.e3",
"type": "compound",
"text": [
"busulfan"
],
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[
309,
317
]
],
"normalized": [
{
"db_name": "PubChem",
"db_id": "2478"
}
]
}
] | [] | [] | [] |
DS.d1430 | 18830721 | [
{
"id": "DS.d1430.s0",
"type": "",
"text": [
"Models of noncoupled dinuclear copper centers in azurin."
],
"offsets": [
[
0,
56
]
]
},
{
"id": "DS.d1430.s1",
"type": "",
"text": [
"Toward this goal, models of the noncoupled copper centers found in the enzymes peptidyl alpha-hydroxylating monooxygenase (PHM), dopamine beta-monooxygenase (DBM), and nitrite reductase (NiR) were designed into the small soluble protein azurin."
],
"offsets": [
[
57,
301
]
]
},
{
"id": "DS.d1430.s2",
"type": "",
"text": [
"The models are significant because they maintain the existing type 1 (T1) copper, electron transfer site of azurin while including the second designed type 2 (T2) copper center that mimics the T2 catalytic sites in the target enzymes."
],
"offsets": [
[
302,
536
]
]
}
] | [
{
"id": "DS.d1430.s0.e0",
"type": "compound",
"text": [
"copper"
],
"offsets": [
[
31,
37
]
],
"normalized": [
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"db_name": "PubChem",
"db_id": "23978"
}
]
},
{
"id": "DS.d1430.s0.e1",
"type": "protein",
"text": [
"azurin"
],
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[
49,
55
]
],
"normalized": [
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"db_name": "UniProt",
"db_id": "P00279"
},
{
"db_name": "UniProt",
"db_id": "P00281"
},
{
"db_name": "UniProt",
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},
{
"db_name": "UniProt",
"db_id": "P00284"
},
{
"db_name": "UniProt",
"db_id": "P00285"
},
{
"db_name": "UniProt",
"db_id": "P00286"
},
{
"db_name": "UniProt",
"db_id": "P34097"
},
{
"db_name": "UniProt",
"db_id": "P80546"
}
]
},
{
"id": "DS.d1430.s1.e0",
"type": "compound",
"text": [
"copper"
],
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[
100,
106
]
],
"normalized": [
{
"db_name": "PubChem",
"db_id": "23978"
}
]
},
{
"id": "DS.d1430.s1.e1",
"type": "protein",
"text": [
"PHM"
],
"offsets": [
[
180,
183
]
],
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{
"db_name": "UniProt",
"db_id": "P10731"
},
{
"db_name": "UniProt",
"db_id": "P14925"
},
{
"db_name": "UniProt",
"db_id": "P19021"
},
{
"db_name": "UniProt",
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},
{
"db_name": "UniProt",
"db_id": "P97467"
},
{
"db_name": "UniProt",
"db_id": "Q95XM2"
}
]
},
{
"id": "DS.d1430.s1.e2",
"type": "protein",
"text": [
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],
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186,
213
]
],
"normalized": [
{
"db_name": "UniProt",
"db_id": "P09172"
},
{
"db_name": "UniProt",
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},
{
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},
{
"db_name": "UniProt",
"db_id": "Q64237"
}
]
},
{
"id": "DS.d1430.s1.e3",
"type": "protein",
"text": [
"NiR"
],
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[
244,
247
]
],
"normalized": [
{
"db_name": "UniProt",
"db_id": "Q39161"
},
{
"db_name": "UniProt",
"db_id": "Q43090"
}
]
},
{
"id": "DS.d1430.s1.e4",
"type": "protein",
"text": [
"azurin"
],
"offsets": [
[
294,
300
]
],
"normalized": [
{
"db_name": "UniProt",
"db_id": "P00279"
},
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},
{
"db_name": "UniProt",
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},
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{
"db_name": "UniProt",
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},
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"db_name": "UniProt",
"db_id": "P00286"
},
{
"db_name": "UniProt",
"db_id": "P34097"
},
{
"db_name": "UniProt",
"db_id": "P80546"
}
]
},
{
"id": "DS.d1430.s2.e0",
"type": "compound",
"text": [
"copper"
],
"offsets": [
[
376,
382
]
],
"normalized": [
{
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"db_id": "23978"
}
]
},
{
"id": "DS.d1430.s2.e1",
"type": "protein",
"text": [
"azurin"
],
"offsets": [
[
410,
416
]
],
"normalized": [
{
"db_name": "UniProt",
"db_id": "P00279"
},
{
"db_name": "UniProt",
"db_id": "P00281"
},
{
"db_name": "UniProt",
"db_id": "P00283"
},
{
"db_name": "UniProt",
"db_id": "P00284"
},
{
"db_name": "UniProt",
"db_id": "P00285"
},
{
"db_name": "UniProt",
"db_id": "P00286"
},
{
"db_name": "UniProt",
"db_id": "P34097"
},
{
"db_name": "UniProt",
"db_id": "P80546"
}
]
},
{
"id": "DS.d1430.s2.e2",
"type": "compound",
"text": [
"copper"
],
"offsets": [
[
465,
471
]
],
"normalized": [
{
"db_name": "PubChem",
"db_id": "23978"
}
]
}
] | [] | [] | [
{
"id": "DS.d1430.s0.i0",
"type": "compound-protein-interaction",
"arg1_id": "DS.d1430.s0.e0",
"arg2_id": "DS.d1430.s0.e1",
"normalized": []
},
{
"id": "DS.d1430.s1.i0",
"type": "compound-protein-interaction",
"arg1_id": "DS.d1430.s1.e0",
"arg2_id": "DS.d1430.s1.e1",
"normalized": []
},
{
"id": "DS.d1430.s1.i1",
"type": "compound-protein-interaction",
"arg1_id": "DS.d1430.s1.e0",
"arg2_id": "DS.d1430.s1.e4",
"normalized": []
},
{
"id": "DS.d1430.s1.i2",
"type": "compound-protein-interaction",
"arg1_id": "DS.d1430.s1.e0",
"arg2_id": "DS.d1430.s1.e3",
"normalized": []
},
{
"id": "DS.d1430.s1.i3",
"type": "compound-protein-interaction",
"arg1_id": "DS.d1430.s1.e0",
"arg2_id": "DS.d1430.s1.e2",
"normalized": []
},
{
"id": "DS.d1430.s2.i0",
"type": "compound-protein-interaction",
"arg1_id": "DS.d1430.s2.e0",
"arg2_id": "DS.d1430.s2.e1",
"normalized": []
}
] |
DS.d1431 | 18830722 | [
{
"id": "DS.d1431.s0",
"type": "",
"text": [
"Intraprotein electron transfer (IET) from flavin mononucleotide (FMN) to heme is essential in NO synthesis by NO synthase (NOS)."
],
"offsets": [
[
0,
128
]
]
}
] | [
{
"id": "DS.d1431.s0.e0",
"type": "compound",
"text": [
"flavin mononucleotide"
],
"offsets": [
[
42,
63
]
],
"normalized": [
{
"db_name": "PubChem",
"db_id": "710"
},
{
"db_name": "PubChem",
"db_id": "8965"
},
{
"db_name": "PubChem",
"db_id": "643976"
}
]
},
{
"id": "DS.d1431.s0.e1",
"type": "compound",
"text": [
"FMN"
],
"offsets": [
[
65,
68
]
],
"normalized": [
{
"db_name": "PubChem",
"db_id": "710"
},
{
"db_name": "PubChem",
"db_id": "8965"
},
{
"db_name": "PubChem",
"db_id": "643976"
}
]
},
{
"id": "DS.d1431.s0.e2",
"type": "compound",
"text": [
"heme"
],
"offsets": [
[
73,
77
]
],
"normalized": [
{
"db_name": "PubChem",
"db_id": "4971"
}
]
},
{
"id": "DS.d1431.s0.e3",
"type": "protein",
"text": [
"NOS"
],
"offsets": [
[
123,
126
]
],
"normalized": [
{
"db_name": "UniProt",
"db_id": "O54705"
},
{
"db_name": "UniProt",
"db_id": "O61309"
},
{
"db_name": "UniProt",
"db_id": "O61608"
},
{
"db_name": "UniProt",
"db_id": "Q26240"
},
{
"db_name": "UniProt",
"db_id": "Q28969"
},
{
"db_name": "UniProt",
"db_id": "Q9I9M2"
}
]
}
] | [] | [] | [
{
"id": "DS.d1431.s0.i0",
"type": "compound-protein-interaction",
"arg1_id": "DS.d1431.s0.e0",
"arg2_id": "DS.d1431.s0.e3",
"normalized": []
},
{
"id": "DS.d1431.s0.i1",
"type": "compound-protein-interaction",
"arg1_id": "DS.d1431.s0.e2",
"arg2_id": "DS.d1431.s0.e3",
"normalized": []
},
{
"id": "DS.d1431.s0.i2",
"type": "compound-protein-interaction",
"arg1_id": "DS.d1431.s0.e1",
"arg2_id": "DS.d1431.s0.e3",
"normalized": []
}
] |
DS.d1432 | 18830729 | [
{
"id": "DS.d1432.s0",
"type": "",
"text": [
"The esterase and lipase activities were determined by the hydrolysis of pNPB and pNPP, respectively."
],
"offsets": [
[
0,
100
]
]
}
] | [
{
"id": "DS.d1432.s0.e0",
"type": "protein",
"text": [
"esterase"
],
"offsets": [
[
4,
12
]
],
"normalized": [
{
"db_name": "UniProt",
"db_id": "P16397"
},
{
"db_name": "UniProt",
"db_id": "P18773"
}
]
},
{
"id": "DS.d1432.s0.e1",
"type": "protein",
"text": [
"lipase"
],
"offsets": [
[
17,
23
]
],
"normalized": [
{
"db_name": "UniProt",
"db_id": "Q7M4U7"
}
]
},
{
"id": "DS.d1432.s0.e2",
"type": "compound",
"text": [
"pNPP"
],
"offsets": [
[
81,
85
]
],
"normalized": [
{
"db_name": "PubChem",
"db_id": "378"
}
]
}
] | [] | [] | [
{
"id": "DS.d1432.s0.i0",
"type": "compound-protein-interaction",
"arg1_id": "DS.d1432.s0.e2",
"arg2_id": "DS.d1432.s0.e1",
"normalized": []
},
{
"id": "DS.d1432.s0.i1",
"type": "compound-protein-interaction",
"arg1_id": "DS.d1432.s0.e2",
"arg2_id": "DS.d1432.s0.e0",
"normalized": []
}
] |
DS.d1433 | 18830730 | [
{
"id": "DS.d1433.s0",
"type": "",
"text": [
"In the present work, the activity of the enzymes xylose reductase (XR); xylitol dehydrogenase (XD); and glucose-6-phosphate dehydrogenase (G6PD) during cultivation of Candida guilliermondii on rice straw hemicellulosic hydrolysate was measured and correlated with xylitol production under different pH values (around 4.5 and 7.5) and initial xylose concentration (around 30 and 70 g l(-1))."
],
"offsets": [
[
0,
390
]
]
}
] | [
{
"id": "DS.d1433.s0.e0",
"type": "protein",
"text": [
"xylose reductase"
],
"offsets": [
[
49,
65
]
],
"normalized": [
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"db_name": "UniProt",
"db_id": "P38715"
}
]
},
{
"id": "DS.d1433.s0.e1",
"type": "protein",
"text": [
"xylitol dehydrogenase"
],
"offsets": [
[
72,
93
]
],
"normalized": [
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"db_name": "UniProt",
"db_id": "P22144"
},
{
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},
{
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"db_id": "Q59545"
},
{
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"db_id": "Q8U7Y1"
},
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"db_id": "Q92MT4"
},
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"db_id": "Q98D10"
}
]
},
{
"id": "DS.d1433.s0.e2",
"type": "protein",
"text": [
"G6PD"
],
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139,
143
]
],
"normalized": [
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"db_id": "O00091"
},
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},
{
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},
{
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{
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"db_id": "P0A584"
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{
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{
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"db_id": "P0A586"
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{
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"db_id": "P0AC53"
},
{
"db_name": "UniProt",
"db_id": "P0AC54"
},
{
"db_name": "UniProt",
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DS.d1442 | 18830972 | [
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DS.d1443 | 18831007 | [
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DS.d1444 | 18831010 | [
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DS.d1445 | 18831033 | [
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