-- DBMS: bigquery
CREATE TABLE `bigquery-public-data.ebi_chembl.docs_30`
(
  doc_id INT64 NOT NULL OPTIONS(description="Unique ID for the document"),
  journal STRING OPTIONS(description="Abbreviated journal name for an article"),
  year INT64 OPTIONS(description="Year of journal article publication"),
  volume STRING OPTIONS(description="Volume of journal article"),
  issue STRING OPTIONS(description="Issue of journal article"),
  first_page STRING OPTIONS(description="First page number of journal article"),
  last_page STRING OPTIONS(description="Last page number of journal article"),
  pubmed_id INT64 OPTIONS(description="NIH pubmed record ID, where available"),
  doi STRING OPTIONS(description=" Digital object identifier for this reference"),
  chembl_id STRING NOT NULL OPTIONS(description="ChEMBL identifier for this document (for use on web interface etc)"),
  title STRING OPTIONS(description=" Document title (e.g., Publication title or description of dataset)"),
  doc_type STRING NOT NULL OPTIONS(description="Type of the document (e.g., Publication, Deposited dataset)"),
  authors STRING OPTIONS(description="For a deposited dataset, the authors carrying out the screening and/or submitting the dataset."),
  abstract STRING OPTIONS(description="For a deposited dataset, a brief description of the dataset."),
  patent_id STRING OPTIONS(description="Patent ID for this document"),
  ridx STRING NOT NULL OPTIONS(description="The Depositor Defined Reference Identifier"),
  src_id INT64 NOT NULL OPTIONS(description="Foreign key to Source table, indicating the source of this document")
);

INSERT INTO `bigquery-public-data.ebi_chembl.docs_30` (doc_id, journal, year, volume, issue, first_page, last_page, pubmed_id, doi, chembl_id, title, doc_type, authors, abstract, patent_id, ridx, src_id) VALUES (116888, 'PNAS', 2015, NULL, '34', '10768', '10773', 26261308, '10.1073/pnas.1501956112', 'CHEMBL4649984', 'CBP30, a selective CBP/p300 bromodomain inhibitor, suppresses human Th17 responses.', 'PUBLICATION', 'Hammitzsch A,Tallant C,Fedorov O,O''Mahony A,Brennan PE,Hay DA,Martinez FO,Al-Mossawi MH,de Wit J,Vecellio M,Wells C,Wordsworth P,Muller S,Knapp S,Bowness P.', 'Th17 responses are critical to a variety of human autoimmune diseases, and therapeutic targeting with monoclonal antibodies against IL-17 and IL-23 has shown considerable promise. Here, we report data to support selective bromodomain blockade of the transcriptional coactivators CBP (CREB binding protein) and p300 as an alternative approach to inhibit human Th17 responses. We show that CBP30 has marked molecular specificity for the bromodomains of CBP and p300, compared with 43 other bromodomains. In unbiased cellular testing on a diverse panel of cultured primary human cells, CBP30 reduced immune cell production of IL-17A and other proinflammatory cytokines. CBP30 also inhibited IL-17A secretion by Th17 cells from healthy donors and patients with ankylosing spondylitis and psoriatic arthritis. Transcriptional profiling of human T cells after CBP30 treatment showed a much more restricted effect on gene expression than that observed with the pan-BET (bromo and extraterminal domain protein family) bromodomain inhibitor JQ1. This selective targeting of the CBP/p300 bromodomain by CBP30 will potentially lead to fewer side effects than with the broadly acting epigenetic inhibitors currently in clinical trials.', NULL, 'SGC-CBP30_26261308', 55), (116897, 'Nature', 2010, NULL, '7327', '1067', '1073', 20871596, '10.1038/nature09504', 'CHEMBL4649993', 'Selective inhibition of BET bromodomains', 'PUBLICATION', 'Filippakopoulos P, Qi J, Picaud S, Shen Y, Smith WB, Fedorov O, Morse EM, Keates T, Hickman TT, Felletar I, Philpott M, Munro S, McKeown MR, Wang Y, Christie AL, West N, Cameron MJ, Schwartz B, Heightman TD, La Thangue N, French CA, Wiest O, Kung AL, Knapp S, Bradner JE.', 'Epigenetic proteins are intently pursued targets in ligand discovery. So far, successful efforts have been limited to chromatin modifying enzymes, or so-called epigenetic ''writers'' and ''erasers''. Potent inhibitors of histone binding modules have not yet been described. Here we report a cell-permeable small molecule (JQ1) that binds competitively to acetyl-lysine recognition motifs, or bromodomains. High potency and specificity towards a subset of human bromodomains is explained by co-crystal structures with bromodomain and extra-terminal (BET) family member BRD4, revealing excellent shape complementarity with the acetyl-lysine binding cavity. Recurrent translocation of BRD4 is observed in a genetically-defined, incurable subtype of human squamous carcinoma. Competitive binding by JQ1 displaces the BRD4 fusion oncoprotein from chromatin, prompting squamous differentiation and specific antiproliferative effects in BRD4-dependent cell lines and patient-derived xenograft models. These data establish proof-of-concept for targeting protein-protein interactions of epigenetic ''readers'', and provide a versatile chemical scaffold for the development of chemical probes more broadly throughout the bromodomain family.', NULL, 'JQ1_20871596', 55), (116900, 'Nature', 2010, NULL, '7327', '1067', '1073', 20871596, '10.1038/nature09504', 'CHEMBL4649996', 'Selective inhibition of BET bromodomains.', 'PUBLICATION', 'Filippakopoulos P, Qi J, Picaud S, Shen Y, Smith WB, Fedorov O, Morse EM, Keates T, Hickman TT, Felletar I, Philpott M, Munro S, McKeown MR, Wang Y, Christie AL, West N, Cameron MJ, Schwartz B, Heightman TD, La Thangue N, French CA, Wiest O, Kung AL, Knapp S, Bradner JE.', 'Epigenetic proteins are intently pursued targets in ligand discovery. So far, successful efforts have been limited to chromatin modifying enzymes, or so-called epigenetic ''writers'' and ''erasers''. Potent inhibitors of histone binding modules have not yet been described. Here we report a cell-permeable small molecule (JQ1) that binds competitively to acetyl-lysine recognition motifs, or bromodomains. High potency and specificity towards a subset of human bromodomains is explained by co-crystal structures with bromodomain and extra-terminal (BET) family member BRD4, revealing excellent shape complementarity with the acetyl-lysine binding cavity. Recurrent translocation of BRD4 is observed in a genetically-defined, incurable subtype of human squamous carcinoma. Competitive binding by JQ1 displaces the BRD4 fusion oncoprotein from chromatin, prompting squamous differentiation and specific antiproliferative effects in BRD4-dependent cell lines and patient-derived xenograft models. These data establish proof-of-concept for targeting protein-protein interactions of epigenetic ''readers'', and provide a versatile chemical scaffold for the development of chemical probes more broadly throughout the bromodomain family.', NULL, '(+)-JQ1_20871596', 55), (69727, 'Chem Cent J', 2012, '6', '28', NULL, NULL, 22483270, '10.1186/1752-153x-6-28', 'CHEMBL3046882', 'Synthesis and antibacterial activity against ralstonia solanacearum for novel hydrazone derivatives containing a pyridine moiety.', 'PUBLICATION', 'Wu J, Kang S, Song B, Hu D, He M, Jin L, Yang S.', 'BACKGROUND: Ralstonia solanacearum, one of the most important bacterial diseases on plants, is a devastating, soil-borne plant pathogen with a global distribution and an unusually wide host range. In order to discover new bioactive molecules and pesticides acting on tobacco bacterial wilt, we sought to combine the active structure of hydrazone and pyridine together to design and synthesize a series of novel hydrazone derivatives containing a pyridine moiety. RESULTS: A series of hydrazone derivatives containing a pyridine moiety were synthesized. Their structures were characterized by 1 H-NMR, 13 C-NMR, IR, and elemental analysis. The preliminary biological activity tests showed that compound 3e and 3g exhibited more than 80% activity against Ralstonia solanacearum at 500 mg/L, especially compound 3g displayed relatively good activity to reach 57.0% at 200 mg/L. CONCLUSION: A practical synthetic route to hydrazone derivatives containing a pyridine moiety by the reaction of intermediates 2 with different aldehydes in ethanol at room temperature using 2-chloronicotinic acid and 2-amino-5-chloro-3-methylbenzoic acid as start materials is presented. This study suggests that the hydrazone derivatives containing a substituted pyridine ring could inhibit the growth of Ralstonia solanacearum.', NULL, 'CLD0', 1), (118892, 'ACS Med Chem Lett', 2016, '7', '2.0', '182', '187', 26985295, '10.1021/acsmedchemlett.5b00396', 'CHEMBL4715707', 'Allosteric Indole Amide Inhibitors of p97: Identification of a Novel Probe of the Ubiquitin Pathway.', 'PUBLICATION', 'Alverez C,Bulfer SL,Chakrasali R,Chimenti MS,Deshaies RJ,Green N,Kelly M,LaPorte MG,Lewis TS,Liang M,Moore WJ,Neitz RJ,Peshkov VA,Walters MA,Zhang F,Arkin MR,Wipf P,Huryn DM', 'A high-throughput screen to discover inhibitors of p97 ATPase activity identified an indole amide that bound to an allosteric site of the protein. Medicinal chemistry optimization led to improvements in potency and solubility. Indole amide 3 represents a novel uncompetitive inhibitor with excellent physical and pharmaceutical properties that can be used as a starting point for drug discovery efforts.', NULL, '26985295', 1);