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Institution

UPRRP College of Natural Sciences

About: UPRRP College of Natural Sciences is a based out in . It is known for research contribution in the topics: Apoptosis & Population. The organization has 9323 authors who have published 11826 publications receiving 284172 citations.


Papers
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Journal ArticleDOI
TL;DR: A simple synthesis of Rh-Fe(3)O(4) heterodimer nanocrystals was achieved by controlled one-pot thermolysis and exhibited excellent activities for the selective reduction of nitroarenes and alkenes.

106 citations

Journal ArticleDOI
TL;DR: This review highlights potential use of neferine, liensinine, isoliens inine, and nuciferine in clinical trials and mechanism of the potential chemical entities from N.nucifera via structure activity relationship needs to be explored to guarantee the stability and safety for the clinical use.
Abstract: Nelumbo nucifera, also known as sacred lotus, has primarily been used as food throughout the Asian continent, and its medicinal values have been described in Ayurvedic and Traditional Chinese Medicine. The purpose of this study is to systematically characterize the chemical profiling and pharmacological activities of N. nucifera. Herein, we critically reviewed and analysed the phytochemical and pharmacological reports of N. nucifera. Our search for the keyword 'Nelumbo nucifera pharmacology' in all databases reported in Web of Science yielded 373 results excluding reviews and abstracts in document types. Two hundred and forty-three spectrum natural compounds from different parts of N. nucifera belonging to diverse chemical groups, including alkaloids, flavonoids, glycosides, terpenoids, steroids, fatty acids, proteins, minerals, and vitamins have been reported. In addition, distinct pharmacological activities, mainly against cancer, microbial infection, diabetes, inflammation, atherosclerosis, and obesity, have been associated with crude extracts, fractions, and isolated compounds. This review highlights potential use of neferine, liensinine, isoliensinine, and nuciferine in clinical trials. In depth, mechanism of the potential chemical entities from N. nucifera via structure activity relationship needs to be explored to guarantee the stability and safety for the clinical use. Copyright © 2016 John Wiley & Sons, Ltd.

106 citations

Journal ArticleDOI
Joaquim Radua, Eduard Vieta, Russell T. Shinohara1, Peter Kochunov2, Yann Quidé3, Yann Quidé4, Melissa J. Green3, Melissa J. Green4, Cynthia Shannon Weickert4, Cynthia Shannon Weickert3, Cynthia Shannon Weickert5, Thomas W. Weickert4, Thomas W. Weickert3, Jason M. Bruggemann1, Jason M. Bruggemann4, Tilo Kircher6, Igor Nenadic6, Murray J. Cairns7, Marc L. Seal8, Ulrich Schall7, Frans Henskens7, Janice M. Fullerton4, Janice M. Fullerton3, Bryan J. Mowry9, Christos Pantelis8, Rhoshel K. Lenroot10, Rhoshel K. Lenroot4, Rhoshel K. Lenroot3, Vanessa Cropley8, Carmel M. Loughland7, Rodney J. Scott7, Daniel H. Wolf1, Theodore D. Satterthwaite1, Yunlong Tan, Kang Sim11, Kang Sim12, Fabrizio Piras, Gianfranco Spalletta13, Nerisa Banaj, Edith Pomarol-Clotet, Aleix Solanes, Anton Albajes-Eizagirre, Erick J. Canales-Rodríguez, S. Sarró14, Annabella Di Giorgio15, Annabella Di Giorgio16, Alessandro Bertolino16, Michael Stäblein17, Viola Oertel17, Christian Knöchel17, Stefan Borgwardt18, Stefan S. du Plessis19, Je-Yeon Yun20, Je-Yeon Yun21, Jun Soo Kwon20, Jun Soo Kwon22, Udo Dannlowski23, Tim Hahn23, Dominik Grotegerd23, Clara Alloza24, Celso Arango, Joost Janssen24, Covadonga M. Díaz-Caneja, Wenhao Jiang25, Vince D. Calhoun26, Stefan Ehrlich27, Kun Yang28, Nicola G. Cascella28, Yoichiro Takayanagi28, Yoichiro Takayanagi29, Akira Sawa28, Alexander Tomyshev, Irina V. Lebedeva, Kaleda Vg, Matthias Kirschner30, Matthias Kirschner31, Cyril Höschl32, Cyril Höschl33, David Tomecek32, David Tomecek34, David Tomecek35, Antonin Skoch32, Therese van Amelsvoort36, Geor Bakker36, Anthony A. James37, Adrian Preda38, Andrea Weideman38, Dan J. Stein39, Fleur M. Howells39, Anne Uhlmann39, Anne Uhlmann27, Henk Temmingh39, Carlos López-Jaramillo40, Ana M. Díaz-Zuluaga40, Lydia Fortea, Eloy Martinez-Heras41, Elisabeth Solana41, Sara Llufriu41, Neda Jahanshad42, Paul M. Thompson42, Jessica A. Turner25, Theo G.M. van Erp38, David C. Glahn43, David C. Glahn44, David C. Glahn45, Godfrey D. Pearlson46, Godfrey D. Pearlson45, Elliot Hong2, Axel Krug6, Vaughan J. Carr4, Vaughan J. Carr47, Paul A. Tooney7, Gavin Cooper7, Paul E. Rasser7, Patricia T. Michie7, Stanley V. Catts9, Raquel E. Gur1, Ruben C. Gur1, Fude Yang, Fengmei Fan, Jingxu Chen, Hua Guo, Shuping Tan, Zhiren Wang, Hong Xiang, Federica Piras, Francesca Assogna, Raymond Salvador, Peter J. McKenna, Aurora Bonvino16, Margaret D. King10, Stefan Kaiser48, Dana Nguyen38, Julian A Pineda-Zapata 
TL;DR: Whether the batch adjustment method, ComBat, can further reduce site-related heterogeneity and thus increase statistical power and recommend applying the ComBat function to attenuate potential effects of site in ENIGMA projects and other multi-site structural imaging work.

106 citations

Journal ArticleDOI
TL;DR: In human A549 non–small lung cancer cells, kaempferol strongly blocked the enhancement of cell migration by TGF-β1–induced EMT through recovering the loss of E-cadherin and suppressing the induction of mesenchymal markers as well as the upregulation of TGF–mediated matrix metalloproteinase-2 activity.

106 citations

Journal ArticleDOI
TL;DR: Comparisons with the structures of the enzyme I–HPr and IIAGlc–glycerol kinase complexes reveal how similar binding surfaces can be formed with underlying backbone scaffolds that are structurally dissimilar and highlight the role of redundancy and side chain conformational plasticity.
Abstract: The solution structure of the second protein-protein complex of the Escherichia coli phosphoenolpyruvate: sugar phosphotransferase system, that between histidine-containing phosphocarrier protein (HPr) and glucose-specific enzyme IIA(Glucose) (IIA(Glc)), has been determined by NMR spectroscopy, including the use of dipolar couplings to provide long-range orientational information and newly developed rigid body minimization and constrained/restrained simulated annealing methods. A protruding convex surface on HPr interacts with a complementary concave depression on IIA(Glc). Both binding surfaces comprise a central hydrophobic core region surrounded by a ring of polar and charged residues, positive for HPr and negative for IIA(Glc). Formation of the unphosphorylated complex, as well as the phosphorylated transition state, involves little or no change in the protein backbones, but there are conformational rearrangements of the interfacial side chains. Both HPr and IIA(Glc) recognize a variety of structurally diverse proteins. Comparisons with the structures of the enzyme I-HPr and IIA(Glc)-glycerol kinase complexes reveal how similar binding surfaces can be formed with underlying backbone scaffolds that are structurally dissimilar and highlight the role of redundancy and side chain conformational plasticity.

105 citations


Authors

Showing all 9323 results

NameH-indexPapersCitations
Hyun-Chul Kim1764076183227
Alfred L. Goldberg15647488296
Stephen J. O'Brien153106293025
Taeghwan Hyeon13956375814
Keiji Tanaka12959482885
Csaba Szabó12395861791
Young Hee Lee122116861107
Angus C. Nairn11846944330
John P. Giesy114116262790
Graham L. Collingridge10335351160
Ki-Hyun Kim99191152157
Andrew D. Ellington9656943262
Nam-Gyu Park9442048648
Steven J. Cooke9393734644
Lenore Fahrig8924640968
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Performance
Metrics
No. of papers from the Institution in previous years
YearPapers
202221
2021898
2020932
2019762
2018777
2017765