Link Prediction Investigation of Dynamic Information Flow in Epilepsy

This work was supported partly by the National Natural Science Foundation of China (Grant No.81460206 and No.81660298), Scientific Research Foundation for Doctors of Guizhou Medical University (No.Yuan Bo He J [2014] 003) and by the 2011 Collaborative Innovation Program of Guizhou Province (No. 2015–04 to ZZ).Peer reviewedPublisher PD

Self correction of refractive error among young people in rural China: results of cross sectional investigation

Objective To compare outcomes between adjustable spectacles and conventional methods for refraction in young people

The Embedding Problem for Markov Models of Nucleotide Substitution

10.1371/journal.pone.0069187PLoS ONE87-POLN

HPLC Determination and Pharmacokinetic Study of Homoeriodictyol-7-O-â- D- glucopyranoside in Rat Plasma and Tissues

Homoeriodictyol-7-O-β-D-glucopyranoside (HEDT-Glu) was isolated from Viscum coloratum and identified by MS, 1H- and 13C-NMR. A HPLC method was developed for determination of HEDT-Glu in rat plasma and tissues. All biological samples were pretreated by protein precipitation with acetone. Vanillin was selected as internal standard. The mobile phase consisted of methanol–water–glacial acetic acid (45 : 55 : 0.5, v/v/v). Good linearity were observed over the concentration ranges of 0.1—200.0 μg·ml−1 in rat plasma and 0.05—5.0 μg·ml−1 in tissues. Both intra- and inter-day precisions of HEDT-Glu, expressed as the relative standard deviation, were less than 13.1%. Accuracy, expressed as the relative error, ranged from −0.8 to 5.4% in plasma and from −5.6 to 9.4% in tissues. The mean extraction recovery of HEDT-Glu was above 73.17% in biological samples. The described assay method was successfully applied to the pre-clinical pharmacokinetic study of HEDT-Glu. After intravenous administration of HEDT-Glu to rat, AUC and CLtot were 16.04±3.19 μg·h·ml−1 and 0.85±0.17 l·kg−1·h−1, respectively. T1/2,α and t1/2,β were 0.06±0.01 h and 1.27±0.31 h, respectively. HEDT-Glu was cleared from the blood and mainly distributed to the liver and small intestine

NIST Interlaboratory Study on Glycosylation Analysis of Monoclonal Antibodies: Comparison of Results from Diverse Analytical Methods

Glycosylation is a topic of intense current interest in the development of biopharmaceuticals because it is related to drug safety and efficacy. This work describes results of an interlaboratory study on the glycosylation of the Primary Sample (PS) of NISTmAb, a monoclonal antibody reference material. Seventy-six laboratories from industry, university, research, government, and hospital sectors in Europe, North America, Asia, and Australia submit- Avenue, Silver Spring, Maryland 20993; 22Glycoscience Research Laboratory, Genos, Borongajska cesta 83h, 10 000 Zagreb, Croatia; 23Faculty of Pharmacy and Biochemistry, University of Zagreb, A. Kovacˇ ic´ a 1, 10 000 Zagreb, Croatia; 24Department of Chemistry, Georgia State University, 100 Piedmont Avenue, Atlanta, Georgia 30303; 25glyXera GmbH, Brenneckestrasse 20 * ZENIT / 39120 Magdeburg, Germany; 26Health Products and Foods Branch, Health Canada, AL 2201E, 251 Sir Frederick Banting Driveway, Ottawa, Ontario, K1A 0K9 Canada; 27Graduate School of Advanced Sciences of Matter, Hiroshima University, 1-3-1 Kagamiyama Higashi-Hiroshima 739–8530 Japan; 28ImmunoGen, 830 Winter Street, Waltham, Massachusetts 02451; 29Department of Medical Physiology, Jagiellonian University Medical College, ul. Michalowskiego 12, 31–126 Krakow, Poland; 30Department of Pathology, Johns Hopkins University, 400 N. Broadway Street Baltimore, Maryland 21287; 31Mass Spec Core Facility, KBI Biopharma, 1101 Hamlin Road Durham, North Carolina 27704; 32Division of Mass Spectrometry, Korea Basic Science Institute, 162 YeonGuDanji-Ro, Ochang-eup, Cheongwon-gu, Cheongju Chungbuk, 363–883 Korea (South); 33Advanced Therapy Products Research Division, Korea National Institute of Food and Drug Safety, 187 Osongsaengmyeong 2-ro Osong-eup, Heungdeok-gu, Cheongju-si, Chungcheongbuk-do, 363–700, Korea (South); 34Center for Proteomics and Metabolomics, Leiden University Medical Center, P.O. Box 9600, 2300 RC Leiden, The Netherlands; 35Ludger Limited, Culham Science Centre, Abingdon, Oxfordshire, OX14 3EB, United Kingdom; 36Biomolecular Discovery and Design Research Centre and ARC Centre of Excellence for Nanoscale BioPhotonics (CNBP), Macquarie University, North Ryde, Australia; 37Proteomics, Central European Institute for Technology, Masaryk University, Kamenice 5, A26, 625 00 BRNO, Czech Republic; 38Max Planck Institute for Dynamics of Complex Technical Systems, Sandtorstrasse 1, 39106 Magdeburg, Germany; 39Department of Biomolecular Sciences, Max Planck Institute of Colloids and Interfaces, 14424 Potsdam, Germany; 40AstraZeneca, Granta Park, Cambridgeshire, CB21 6GH United Kingdom; 41Merck, 2015 Galloping Hill Rd, Kenilworth, New Jersey 07033; 42Analytical R&D, MilliporeSigma, 2909 Laclede Ave. St. Louis, Missouri 63103; 43MS Bioworks, LLC, 3950 Varsity Drive Ann Arbor, Michigan 48108; 44MSD, Molenstraat 110, 5342 CC Oss, The Netherlands; 45Exploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, 5–1 Higashiyama, Myodaiji, Okazaki 444–8787 Japan; 46Graduate School of Pharmaceutical Sciences, Nagoya City University, 3–1 Tanabe-dori, Mizuhoku, Nagoya 467–8603 Japan; 47Medical & Biological Laboratories Co., Ltd, 2-22-8 Chikusa, Chikusa-ku, Nagoya 464–0858 Japan; 48National Institute for Biological Standards and Control, Blanche Lane, South Mimms, Potters Bar, Hertfordshire EN6 3QG United Kingdom; 49Division of Biological Chemistry & Biologicals, National Institute of Health Sciences, 1-18-1 Kamiyoga, Setagaya-ku, Tokyo 158–8501 Japan; 50New England Biolabs, Inc., 240 County Road, Ipswich, Massachusetts 01938; 51New York University, 100 Washington Square East New York City, New York 10003; 52Target Discovery Institute, Nuffield Department of Medicine, University of Oxford, Roosevelt Drive, Oxford, OX3 7FZ, United Kingdom; 53GlycoScience Group, The National Institute for Bioprocessing Research and Training, Fosters Avenue, Mount Merrion, Blackrock, Co. Dublin, Ireland; 54Department of Chemistry, North Carolina State University, 2620 Yarborough Drive Raleigh, North Carolina 27695; 55Pantheon, 201 College Road East Princeton, New Jersey 08540; 56Pfizer Inc., 1 Burtt Road Andover, Massachusetts 01810; 57Proteodynamics, ZI La Varenne 20–22 rue Henri et Gilberte Goudier 63200 RIOM, France; 58ProZyme, Inc., 3832 Bay Center Place Hayward, California 94545; 59Koichi Tanaka Mass Spectrometry Research Laboratory, Shimadzu Corporation, 1 Nishinokyo Kuwabara-cho Nakagyo-ku, Kyoto, 604 8511 Japan; 60Children’s GMP LLC, St. Jude Children’s Research Hospital, 262 Danny Thomas Place Memphis, Tennessee 38105; 61Sumitomo Bakelite Co., Ltd., 1–5 Muromati 1-Chome, Nishiku, Kobe, 651–2241 Japan; 62Synthon Biopharmaceuticals, Microweg 22 P.O. Box 7071, 6503 GN Nijmegen, The Netherlands; 63Takeda Pharmaceuticals International Co., 40 Landsdowne Street Cambridge, Massachusetts 02139; 64Department of Chemistry and Biochemistry, Texas Tech University, 2500 Broadway, Lubbock, Texas 79409; 65Thermo Fisher Scientific, 1214 Oakmead Parkway Sunnyvale, California 94085; 66United States Pharmacopeia India Pvt. Ltd. IKP Knowledge Park, Genome Valley, Shamirpet, Turkapally Village, Medchal District, Hyderabad 500 101 Telangana, India; 67Alberta Glycomics Centre, University of Alberta, Edmonton, Alberta T6G 2G2 Canada; 68Department of Chemistry, University of Alberta, Edmonton, Alberta T6G 2G2 Canada; 69Department of Chemistry, University of California, One Shields Ave, Davis, California 95616; 70Horva´ th Csaba Memorial Laboratory for Bioseparation Sciences, Research Center for Molecular Medicine, Doctoral School of Molecular Medicine, Faculty of Medicine, University of Debrecen, Debrecen, Egyetem ter 1, Hungary; 71Translational Glycomics Research Group, Research Institute of Biomolecular and Chemical Engineering, University of Pannonia, Veszprem, Egyetem ut 10, Hungary; 72Delaware Biotechnology Institute, University of Delaware, 15 Innovation Way Newark, Delaware 19711; 73Proteomics Core Facility, University of Gothenburg, Medicinaregatan 1G SE 41390 Gothenburg, Sweden; 74Department of Medical Biochemistry and Cell Biology, University of Gothenburg, Institute of Biomedicine, Sahlgrenska Academy, Medicinaregatan 9A, Box 440, 405 30, Gothenburg, Sweden; 75Department of Clinical Chemistry and Transfusion Medicine, Sahlgrenska Academy at the University of Gothenburg, Bruna Straket 16, 41345 Gothenburg, Sweden; 76Department of Chemistry, University of Hamburg, Martin Luther King Pl. 6 20146 Hamburg, Germany; 77Department of Chemistry, University of Manitoba, 144 Dysart Road, Winnipeg, Manitoba, Canada R3T 2N2; 78Laboratory of Mass Spectrometry of Interactions and Systems, University of Strasbourg, UMR Unistra-CNRS 7140, France; 79Natural and Medical Sciences Institute, University of Tu¨ bingen, Markwiesenstrae 55, 72770 Reutlingen, Germany; 80Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands; 81Division of Bioanalytical Chemistry, Amsterdam Institute for Molecules, Medicines and Systems, Vrije Universiteit Amsterdam, de Boelelaan 1085, 1081 HV Amsterdam, The Netherlands; 82Department of Chemistry, Waters Corporation, 34 Maple Street Milford, Massachusetts 01757; 83Zoetis, 333 Portage St. Kalamazoo, Michigan 49007 Author’s Choice—Final version open access under the terms of the Creative Commons CC-BY license. Received July 24, 2019, and in revised form, August 26, 2019 Published, MCP Papers in Press, October 7, 2019, DOI 10.1074/mcp.RA119.001677 ER: NISTmAb Glycosylation Interlaboratory Study 12 Molecular & Cellular Proteomics 19.1 Downloaded from https://www.mcponline.org by guest on January 20, 2020 ted a total of 103 reports on glycan distributions. The principal objective of this study was to report and compare results for the full range of analytical methods presently used in the glycosylation analysis of mAbs. Therefore, participation was unrestricted, with laboratories choosing their own measurement techniques. Protein glycosylation was determined in various ways, including at the level of intact mAb, protein fragments, glycopeptides, or released glycans, using a wide variety of methods for derivatization, separation, identification, and quantification. Consequently, the diversity of results was enormous, with the number of glycan compositions identified by each laboratory ranging from 4 to 48. In total, one hundred sixteen glycan compositions were reported, of which 57 compositions could be assigned consensus abundance values. These consensus medians provide communityderived values for NISTmAb PS. Agreement with the consensus medians did not depend on the specific method or laboratory type. The study provides a view of the current state-of-the-art for biologic glycosylation measurement and suggests a clear need for harmonization of glycosylation analysis methods. Molecular & Cellular Proteomics 19: 11–30, 2020. DOI: 10.1074/mcp.RA119.001677.L

Vegetation and climate changes in the western Chinese Loess Plateau since the Last Glacial Maximum

Pollen analysis was conducted for loess deposits from three sites in the western Chinese Loess Plateau, i.e. the loess area west of the Liupan Mountains. Results show that during the Last Glacial Maximum (LGM), in-situ vegetation was dominated by Artemisia and some drought-tolerant species such as Echinops-type, Chenopodiaceae, Nitraria, and Ephedra, while coniferous forest (mainly Picea) flourished in nearby river valleys. During the Holocene Optimum, Picea almost disappeared, and Echinops-type, Chenopodiaceae, Nitraria and Ephedra decreased; vegetation was characterized by Artemisia, Taraxacum-type, Polygonaceae and Leguminosae, implying the climate was warmer and wetter than during the LGM. During the late Holocene, Chenopodiaceae, indicator of human-managed habitats, increased in the study area, indicating enhanced human activity. The climate was warmer and more humid in the loess areas east of the Liupan Mountains than in the west during both the LGM and Holocene Optimum. Likewise, a significant difference in specific plant types was observed between the east and west since the LGM. During the LGM, Pinus and some broadleaf trees emerged, but no Picea forest grew, while in the west, vegetation was characterized by desert shrub and desert steppe in situ, and by dark coniferous forests (mainly Picea) in nearby river valleys. During the Holocene Optimum, treeline advanced upward as a result of increased temperature. Picea thus withdrew from the western loess areas. Therefore, temperature is the major factor controlling the growth of Picea in the Chinese Loess Plateau. (C) 2014 Elsevier Ltd and INQUA. All rights reserved

Changes in plant richness and evenness since Marine Isotope Stage 2 on the Chinese Loess Plateau

The warming period from Marine Isotope Stage 2 (MIS 2) to the mid-Holocene provides a useful analog for assessing the impact of global warming on plant diversity. Previously published pollen records from ten loess sections across the Chinese Loess Plateau (CLP) have shown that herbs were dominant during both MIS 2 and the mid-Holocene. During MIS 2, the vegetation in the eastern part was characterized mainly by Artemisia, together with Taraxacum-type, Echinops-type and Chenopodiaceae; and by Echinops-type, Chenopodiaceae, Nitraria, Ephedra and Picea in the western part. During the mid-Holocene, Artemisia remained dominant, while Echinops-type, Chenopodiaceae, Nitraria, Ephedra and Picea decreased, and Poaceae became more prevalent. From west to east during the mid-Holocene, Corylus, Quercus and Pinus increased, while Artemisia and Taraxacum-type decreased. In the present study, two indices of plant diversity (richness and evenness) were analyzed using these published pollen data. The results demonstrate that from MIS 2 to the mid-Holocene, plant richness increased at most of the studied sites, while plant evenness decreased. The increase in plant richness during the warming interval is in accordance with numerous geological records, but differs from modern observations of the response of biodiversity to ongoing global warming. The decrease in plant evenness is attributed to the increase in precipitation, associated with the intensification of the East Asian summer monsoon, which resulted in an increase in the dominance of Artemisia, and the corresponding inhibition in the growth of other species. Therefore, our results imply that plant richness in northern China would be expected to increase in a climate warming scenario, while changes in plant evenness would largely depend on interspecific competition within a plant community. (C) 2017 Elsevier B.V. All rights reserved

Teaching of Organic Chemistry of Cultivating Applied Pharmaceutical Talents

In order to effectively cultivate applied pharmaceutical talents, aiming at the current teaching situation of organic chemistry, the basic course of pharmaceutical specialty, including the problems of curriculum setting, experimental teaching, and the integration of classroom and professional knowledge, it is proposed to overcome the problem of curriculum setting by combining "online+offline" in teaching. It should overcome the problems in experimental teaching with the help of virtual simulation platform. By cultivating students’ organic chemistry thinking and paying attention to the integration of subject and professional knowledge, students’ recognition of organic chemistry course can be improved, and the quality of training can be improved