{"title":"Determination of pH-BOD-COD and degradation in batang arau watersheds at Padang city","authors":"I. Dewata, R. Zainul","doi":"10.31227/osf.io/efdzj","DOIUrl":"https://doi.org/10.31227/osf.io/efdzj","url":null,"abstract":"This research aims to determine the pH, BOD and COD in river basin region and its relation to the occurrence of damage to the environment. The study was conducted by sampling at six locations representing the upstream region, the central region and the region downstream/estuary for four years, from 2011 until 2014. The sampling locations in the watershed Batang Arau at Padang city, include Lubuk Paraku (section 1), Banyan Lubuk Kilangan (section 2), the center, Bridges Lubeg by pass (section 3), Bridge Aur Duri / Pulau Aia (section 4), downstream, Bridges Aru Padang (section 5) and Muaro Bridge Siti Nurbaya (section 6 ). In the Upstream, for the parameters pH, BOD and COD in 2011 to 2014 received a range of changes in pH of 6-9, unless the parameters BOD in 2012 of about 4.35 mg/L. In the central region (middlestream), namely BOD content of 4.35 mg/L (2011), 4.54 mg/L (2012), 3.36 mg/L (2013) and 2.56 mg/L (2014), approaching the quality standards was set at 3 mg/L. While the pH and COD are below the quality standards every year. In the downstream, the results of BOD of 17.21 mg/L (2011), 21.25 mg/L (2012), 5.04 mg/L (2013) and 3.42 mg/L (2014). Meanwhile, COD 47.5 mg/L (2011), 57.76 mg/L (2012), 11.17 mg/L (2013) and 20, 5 mg/L (2014), while the quality standards for COD by 25 mg/L, and pH parameters within normal limits. From this research, we reported that watersheds degradation has been in downstream area (section 5 and 6), but in upstream and middlestream was still normally and not degraded.","PeriodicalId":15344,"journal":{"name":"Journal of chemical and pharmaceutical research","volume":"151 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2015-12-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83368965","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Private Placement Discount of Chinese Listed Companies Based on the Perspective of the Investors’ Sentiment","authors":"Jun Yu, Zhu-bao Wei, Shu-zhen Wang, J. Tang","doi":"10.1007/978-3-642-38442-4_13","DOIUrl":"https://doi.org/10.1007/978-3-642-38442-4_13","url":null,"abstract":"","PeriodicalId":15344,"journal":{"name":"Journal of chemical and pharmaceutical research","volume":"41 1","pages":"121-130"},"PeriodicalIF":0.0,"publicationDate":"2013-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78099239","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"An equation of state for nonaqueous electrolyte solutions","authors":"Zheng Han","doi":"10.4236/ACES.2012.24061","DOIUrl":"https://doi.org/10.4236/ACES.2012.24061","url":null,"abstract":"A two parameters equation of state (EOS) for nonaqueous electrolyte solutions system has been developed. The equation is in terms of Helmholtz free energy and incorporated with results of low density expansion of non-primitive mean spherical approximation. The EOS was tested for experimental data reported in literatures of 9 nonaqueous single electrolyte solutions of which the temperature was 298.15K, and it also has a good predictive capability for nonaqueous electrolyte solutions at different temperature in this work. The comparasions with EOSs published earlier by other researchers in literatures are carried out in detail.","PeriodicalId":15344,"journal":{"name":"Journal of chemical and pharmaceutical research","volume":"84 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2012-10-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76950420","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Tania C Cordova-Sintjago, Lijuan Fang, Martijn Bruysters, Rob Leurs, Raymond G Booth
{"title":"Molecular determinants of ligand binding at the human histamine H<sub>1</sub> receptor: Site-directed mutagenesis results analyzed with ligand docking and molecular dynamics studies at H<sub>1</sub> homology and crystal structure models.","authors":"Tania C Cordova-Sintjago, Lijuan Fang, Martijn Bruysters, Rob Leurs, Raymond G Booth","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The human histamine H<sub>1</sub> G-protein coupled receptor (GPCR) is an important drug target for inflammatory, sleep, and other neuropsychiatric disorders. To delineate molecular determinants for ligand binding for drug discovery purposes, human H<sub>1</sub> receptor models were built by homology to the crystal structure of the human β<sub>2</sub> adrenoceptor (β<sub>2</sub>AR) and from the recently reported crystal structure of the human H<sub>1</sub> receptor complex with doxepin at 3.1 Å (PDB code 3RZE). Ligand affinity of histamine and the H<sub>1</sub> antagonists mepyramine and (2S, 4R)-(-)-trans-4-phenyl-2-N, N-dimethylaminotetralin (PAT) at wild type and point-mutated (D3.32A, Y3.33A, W4.56A, F5.47A, W6.48A, Y6.51A, F6.52A, F6.55A, Y7.43A) human H<sub>1</sub> receptors were determined experimentally and results analyzed by ligand docking and molecular dynamic studies at WT and point-mutated H<sub>1</sub> receptor models. Differences in ligand binding affinities correlated to differences in ligand binding modes at models built according to homology or crystal structure, indicating, both models are accurate templates for predicting ligand affinity for H<sub>1</sub> drug design.</p>","PeriodicalId":15344,"journal":{"name":"Journal of chemical and pharmaceutical research","volume":"4 6","pages":"2937-2951"},"PeriodicalIF":0.0,"publicationDate":"2012-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4085681/pdf/nihms496523.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"32494199","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Rick Gussio, Michael J Currens, Dominic A Scudiero, Jeffrey A Smith, Deborah A Lannigan, Robert H Shoemaker, Dan W Zaharevitz, Tam Luong Nguyen
{"title":"RSK2 Binding Models Delineate Key Features for Activity.","authors":"Rick Gussio, Michael J Currens, Dominic A Scudiero, Jeffrey A Smith, Deborah A Lannigan, Robert H Shoemaker, Dan W Zaharevitz, Tam Luong Nguyen","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Due to its overexpression and activation in human cancer cells and tissues, an emerging molecular target in cancer therapeutics is p90 ribosomal s6 kinase 2 (RSK2). While a growing number of RSK2 inhibitors have been reported in the literature, only the crystal structure of RSK2 in complex with an AMP analogue provides a structural basis for understanding RSK2 inhibition. To remedy this, we used our fluorescence polarization assay to determine the RSK2 activity for a set of structurally diverse compounds, and followed this by modeling their binding modes in an all-atom, energy refined crystal structure of RSK2. These binding models reveal that Val131 and Leu147 are key interaction sites for potent RSK2 inhibition. This structure-based pharmacophore is an important tool for new lead discovery and refinement.</p>","PeriodicalId":15344,"journal":{"name":"Journal of chemical and pharmaceutical research","volume":"2 5","pages":"587-598"},"PeriodicalIF":0.0,"publicationDate":"2010-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3094916/pdf/nihms276044.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40093478","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}