This product is isolated and purified from the herbs of Rabdosia lophanthoides
(6β,7α)-6,7,12-Trihydroxy-11,14-dioxoabieta-8,12-dien-16-yl acetate/1,4-Phenanthrenedione, 2-[2-(acetyloxy)-1-methylethyl]-4b,5,6,7,8,8a,9,10-octahydro-3,9,10-trihydroxy-4b,8,8-trimethyl-, (4bS,8aS,9S,10S)-
Soluble in Chloroform,Dichloromethane,Ethyl Acetate,DMSO,Acetone,etc.
551.3±50.0 °C at 760 mmHg
HS Code Reference
Personal Projective Equipment
For Reference Standard and R&D, Not for Human Use Directly.
provides coniferyl ferulate(CAS#:120462-45-5) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate
We have examined the effect of stearylamine (SA) in liposomes on the viability of Plasmodium falciparum in culture by studying the inhibition of incorporation of [3H]-hypoxanthine in the nucleic acid of parasites. Stearylamine in liposomes significantly inhibits the growth of the parasites depending on the phospholipids composition. The maximum inhibition was observed when SA was delivered through Soya phosphatidylcholine (SPC) liposomes. The chain length of alkyl group and density of SA in liposomes play a significant role in inhibiting the growth of the parasites. Incorporation of either cholesterol or Distearylphosphatidylethanolamine−Methoxy-Polyethylene glycol-2000 (DSPE-mPEG-2000) in Soya phosphatidylcholine-stearylamine (SPC-SA) liposomes improves the efficacy. Intraerythrocytic entry of intact SPC-SA liposomes into infected erythrocytes was visualized using fluorescent microscopy. No hemolysis was observed in uninfected erythrocytes, and slight hemolysis was noted in infected erythrocytes at high concentrations of SPC-SA liposomes. Overall, our data suggested SA in SPC-liposomes might have potential application in malaria chemotherapy.
Inhibition of the Growth of Plasmodium falciparum in Culture by Stearylamine-Phosphatidylcholine Liposomes
Gulam Mustafa Hasan, Neha Garg, Enna Dogra, Ranu Surolia, and Prahlad Chandra Ghosh *
Chronic Obstructive Pulmonary Disease (COPD) is characterised by reduced lung function and is the third leading cause of death globally. Through genome-wide association discovery in 48,943 individuals, selected from extremes of the lung function distribution in UK Biobank, and follow-up in 95,375 individuals, we increased the yield of independent signals for lung function from 54 to 97. A genetic risk score was associated with COPD susceptibility (odds ratios per standard deviation of the risk score (~6 alleles) (95% confidence interval) 1.24 (1.20-1.27), P=5.05×10-49) and we observed a 3.7 fold difference in COPD risk between highest and lowest genetic risk score deciles in UK Biobank. The 97 signals show enrichment in development, elastic fibres and epigenetic regulation pathways. We highlight targets for drugs and compounds in development for COPD and asthma (genes in the inositol phosphate metabolism pathway and CHRM3) and describe targets for potential drug repositioning from other clinical indications.
Genome-wide association analyses for lung function and chronic obstructive pulmonary disease identify new loci and potential druggable targets
Louise V Wain,1,2 Nick Shrine,1 Maria Soler Artigas,1 A Mesut Erzurumluoglu,1 Boris Noyvert,1 Lara Bossini-Castillo,3 Ma’en Obeidat,4 Amanda P Henry,5 Michael A Portelli,5 Robert J Hall,5 Charlotte K Billington,5 Tracy L Rimington,5 Anthony G Fenech,6 Catherine John,1 Tineka Blake,1 Victoria E Jackson,1 Richard J Allen,1 Bram P Prins,7 Understanding Society Scientific Group,8 Archie Campbell,9,10 David J Porteous,9,10 Marjo-Riitta Jarvelin,11,12,13,14 Matthias Wielscher,11 Alan L James,15,16,17 Jennie Hui,15,18,19,20 Nicholas J Wareham,21 Jing Hua Zhao,21 James F Wilson,22,23 Peter K Joshi,22 Beate Stubbe,24 Rajesh Rawal,25 Holger Schulz,26,27 Medea Imboden,28,29 Nicole M Probst-Hensch,28,29 Stefan Karrasch,26,30 Christian Gieger,25 Ian J Deary,31,32 Sarah E Harris,9,31 Jonathan Marten,23 Igor Rudan,22 Stefan Enroth,33 Ulf Gyllensten,33 Shona M Kerr,23 Ozren Polasek,22,34 Mika Kahonen,35 Ida Surakka,36,37 Veronique Vitart,23 Caroline Hayward,23 Terho Lehtimaki,38,39 Olli T Raitakari,40,41 David M Evans,42,43 A John Henderson,44 Craig E Pennell,45 Carol A Wang,45 Peter D Sly,46 Emily S Wan,47,48 Robert Busch,47,48 Brian D Hobbs,47,48 Augusto A Litonjua,47,48 David W Sparrow,49,50 Amund Gulsvik,51 Per S Bakke,51 James D Crapo,52,53 Terri H Beaty,54 Nadia N Hansel,55 Rasika A Mathias,56 Ingo Ruczinski,57 Kathleen C Barnes,58 Yohan Bosse,59,60 Philippe Joubert,60,61 Maarten van den Berge,62 Corry-Anke Brandsma,63 Peter D Pare,4,64 Don D Sin,4,64 David C Nickle,65 Ke Hao,66 Omri Gottesman,67 Frederick E Dewey,67 Shannon E Bruse,67 David J Carey,68 H Lester Kirchner,68 Geisinger-Regeneron DiscovEHR Collaboration,8 Stefan Jonsson,69 Gudmar Thorleifsson,69 Ingileif Jonsdottir,69,70 Thorarinn Gislason,70,71 Kari Stefansson,69,70 Claudia Schurmann,72,73 Girish Nadkarni,72 Erwin P Bottinger,72 Ruth JF Loos,72,73,74 Robin G Walters,75 Zhengming Chen,75 Iona Y Millwood,75,76 Julien Vaucher,75 Om P Kurmi,75 Liming Li,77,78 Anna L Hansell,79,80 Chris Brightling,2,81 Eleftheria Zeggini,7 Michael H Cho,47,48 Edwin K Silverman,47,48 Ian Sayers,5 Gosia Trynka,3 Andrew P Morris,82 David P Strachan,83 Ian P Hall,5 and Martin D Tobin1,2
2017 Aug 6.
53BP1 is a mediator of DNA damage response (DDR) and a tumor suppressor whose accumulation on damaged chromatin promotes DNA repair and enhances DDR signaling. Using foci formation of 53BP1 as a readout in two human cell lines, we performed an siRNA-based functional high-content microscopy screen for modulators of cellular response to ionizing radiation (IR). Here, we provide the complete results of this screen as an information resource, and validate and functionally characterize one of the identified ‘hits’: a nuclear pore component NUP153 as a novel factor specifically required for 53BP1 nuclear import. Using a range of cell and molecular biology approaches including live-cell imaging, we show that knockdown of NUP153 prevents 53BP1, but not several other DDR factors, from entering the nuclei in the newly forming daughter cells. This translates into decreased IR-induced 53BP1 focus formation, delayed DNA repair and impaired cell survival after IR. In addition, NUP153 depletion exacerbates DNA damage caused by replication stress. Finally, we show that the C-terminal part of NUP153 is required for effective 53BP1 nuclear import, and that 53BP1 is imported to the nucleus through the NUP153-importin-β interplay. Our data define the structure-function relationships within this emerging 53BP1-NUP153/importin-β pathway and implicate this mechanism in the maintenance of genome integrity.
DNA repair, siRNA screen, 53BP1 nuclear import, nucleoporin NUP153, cell survival, ionizing radiation
Nucleoporin NUP153 guards genome integrity by promoting nuclear import of 53BP1
P Moudry,1,2 C Lukas,2 L Macurek,1 B Neumann,3 J-K Heriche,3 R Pepperkok,3 J Ellenberg,3 Z Hodny,1 J Lukas,2,* and J Bartek1,2,4,*