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Chan Park, Seok,Shinzawa, Hideyuki,Qian, Jue,Chung, Hoeil,Ozaki, Yukihiro,Arnold, Mark A. Royal Society of Chemistry 2011 The Analyst Vol.136 No.15
<P>A novel strategy is demonstrated to improve the accuracy for determination of polyethylene (PE) density using Raman spectroscopy by optimizing the temperature of sample measurement. Spectral features associated with the conformation change of the polymer induced by temperature may provide valuable information to quantify important polymer properties such as density. To evaluate possible existence of an optimal temperature providing improved quantitative accuracy, Raman spectra of PE pellets with different densities were collected at eight different temperatures from 30 to 100 °C at 10 °C intervals. Using the spectral datasets collected at each temperature, partial least squares (PLS) models were developed using the reference PE density values determined by a standard density gradient method at 23 °C. Interestingly, the most accurate determination of density was realized at 70 °C. Multiple perturbation two-dimensional (MP2D) correlation analysis and differential scanning calorimetry (DSC) were used to examine the origin of improved accuracy at 70 °C. From these analyses, the pre-melt behavior of the PE samples was identified below their melting temperatures. Structural variations induced at the pre-melt stages enhance Raman spectral selectivity among the samples, thereby providing more accurate determination of PE density. The MP2D correlation analysis revealed the unforeseen thermal behavior of PE samples and successfully explained the improved accuracy at 70 °C.</P> <P>Graphic Abstract</P><P>Optimization of Raman spectral collection temperature improved the accuracy for determination of polyethylene (PE) density. <IMG SRC='http://pubs.rsc.org/services/images/RSCpubs.ePlatform.Service.FreeContent.ImageService.svc/ImageService/image/GA?id=c1an15231a'> </P>
Meeting Report: Translational Advances in Cancer Prevention Agent Development Meeting
Mark Steven Miller,Peter J. Allen,Powel H. Brown,Andrew T. Chan,Margie L. Clapper,Roderick H. Dashwood,Shadmehr Demehri,Mary L. Disis,Raymond N. DuBois,Robert J. Glynn,Thomas W. Kensler,Seema A. Khan 대한암예방학회 2021 Journal of cancer prevention Vol.26 No.1
The Division of Cancer Prevention of the National Cancer Institute (NCI) and the Office of Disease Prevention of the National Institutes of Health co-sponsored the Translational Advances in Cancer Prevention Agent Development Meeting on August 27 to 28, 2020. The goals of this meeting were to foster the exchange of ideas and stimulate new collaborative interactions among leading cancer prevention researchers from basic and clinical research; highlight new and emerging trends in immunoprevention and chemoprevention as well as new information from clinical trials; and provide information to the extramural research community on the significant resources available from the NCI to promote prevention agent development and rapid translation to clinical trials. The meeting included two plenary talks and five sessions covering the range from pre-clinical studies with chemo/immunopreventive agents to ongoing cancer prevention clinical trials. In addition, two NCI informational sessions describing contract resources for the preclinical agent development and cooperative grants for the Cancer Prevention Clinical Trials Network were also presented.
( Mark S. Sulkowski ),( Henry Lik Yuen Chan ),( Jordan J. Feld ),( Kosh Agarwal ),( Christophe Hezode ),( Tarik Asselah ),( Peter J. Ruane ),( Norbert Gruener ),( Armand Abergel ),( Alessandra Mangia 대한간학회 2016 춘·추계 학술대회 (KASL) Vol.2016 No.1
Background: Velpatasvir (VEL) is a pangenotypic HCV-NS5A inhibitor. This Phase 3 study evaluated treatment with a fixed dose combination of SOF/VEL for 12 weeks in patients with genotype 1, 2, 4, 5, or 6 HCV infection. Methods: Patients with genotype 1, 2, 4, or 6 chronic HCV infection were randomized 5:1 to received SOF/VEL (400 mg /100 mg daily) or placebo for 12 weeks. Patients with genotype 5 infection were enrolled to the SOF/VEL treatment group and patients with genotype 3 were evaluated in a separate study. Results: 740 patients were enrolled at 81 international sites: 60% male, 79% white, 32% treatment-experienced (TE), and 19% compensated- cirrhosis. Of the 624 patients treated with SOF/VEL, the genotype distribution was 53% GT1, 17% GT2, 19% GT4, 6% GT5 and 7 % GT6. Overall SVR12 for SOF/VEL-treated patients was 99.0% and the study met its primary efficacy endpoint. SVR12 rates by HCV genotype are presented in the table. Two of 328 patients (0.6%) with genotype-1 infection had virologic relapse. No patients with genotype 2, 4, 5, or 6, including 48 with cirrhosis, had virologic failure. Four patients did not achieve SVR12 for non-virologic reasons. AEs and laboratory abnormalities were similar in the SOF/VEL-treated patients compared with the 116 placebo-treated patients. One patient discontinued SOF/VEL treatment due to adverse-events. Conclusions: Treatment with the once daily, all-oral, single tablet regimen of SOF/VEL for 12 weeks is well tolerated and results in high SVR12 rates in treatment-naive and treatment-experienced genotype 1, 2, 4, 5, and 6 HCV-infected patients with and without cirrhosis.
Ligand Binding Properties of the N-Terminal Domain of Riboflavin Synthase from Escherichia coli
( Chan Yong Lee ),( Boris Illarionov ),( Young Eun Woo ),( Kristina Kemter ),( Ryu Ryun Kim ),( Sabine Eberhardt ),( Mark Cushman ),( Wolfgang Eisenreich ),( Markus Fischer ),( Adelbert Bacher ) 생화학분자생물학회 2007 BMB Reports Vol.40 No.2
Park, Chan H.,Kimler, Bruce F.,Yi, Seong Yoon,Park, Se Hoon,Kim, Kihyun,Jung, Chul Won,Kim, Sun Hee,Lee, Eun Ryung,Rha, Miyong,Kim, Seonwoo,Park, Mary H.,Lee, Sook J.,Park, Hye K.,Lee, Mark H.,Yoon, S Blackwell Publishing Ltd 2009 European journal of haematology Vol.83 No.2
<P>Abstract</P><P>Purpose: </P><P><SMALL>L</SMALL>-ascorbic acid (LAA) modifies the <I>in vitro</I> growth of leukemic cells from ∼50% of patients with acute myeloid leukemia (AML) or myelodysplastic syndromes (MDS). To test the hypothesis that depletion of LAA, alternating with supplementation to prevent scurvy, would provide therapeutic benefit, a single-arm pilot trial was conducted (ClinicalTrials.gov identifier: NCT00329498).</P><P>Experimental results: </P><P>During depletion phase, patients with refractory AML or MDS were placed on a diet deficient in LAA; during supplementation phase, patients received daily intravenous administration of LAA. An <I>in vitro</I> assay was performed pretherapy for LAA sensitivity of leukemic cells from individual patients.</P><P>Results: </P><P>Of 18 patients enrolled, eight of 16 evaluable patients demonstrated a clinical response. Responses were obtained during depletion (four patients) as well as during supplementation (five patients) but at a pharmacologic plasma level achievable only with intravenous administration. Of nine patients for whom the <I>in vitro</I> assay indicated their leukemic cells were sensitive to LAA, seven exhibited a clinical response; compared with none of six patients who were insensitive to LAA.</P><P>Conclusions: </P><P>The clinical benefit, along with a conspicuous absence of significant adverse events, suggests that further testing of LAA depletion alternating with pharmacologic dose intravenous supplementation in patients with these and other malignancies is warranted.</P>
Ligand Binding Properties of the N-Terminal Domain of Riboflavin Synthase from Escherichia coli
Lee, Chan-Yong,Illarionov, Boris,Woo, Young-Eun,Kemter, Kristina,Kim, Ryu-Ryun,Eberhardt, Sabine,Cushman, Mark,Eisenreich, Wolfgang,Fischer, Markus,Bacher, Adelbert Korean Society for Biochemistry and Molecular Biol 2007 Journal of biochemistry and molecular biology Vol.40 No.2
Riboflavin synthase from Escherichia coli is a homotrimer of 23.4 kDa subunits and catalyzes the formation of one molecule each of riboflavin and 5-amino-6-ribitylamino- 2,4(1H,3H)-pyrimidinedione by the transfer of a 4-carbon moiety between two molecules of the substrate, 6,7- dimethyl-8-ribityllumazine. Each subunit comprises two closely similar folding domains. Recombinant expression of the N-terminal domain is known to provide a $C_2$-symmetric homodimer. In this study, the binding properties of wild type as well as two mutated proteins of N-terminal domain of riboflavin synthase with various ligands were tested. The replacement of the amino acid residue A43, located in the second shell of riboflavin synthase active center, in the recombinant N-terminal domain dimer reduces the affinity for 6,7-dimethyl-8-ribityllumazine. The mutation of the amino acid residue C48 forming part of activity cavity of the enzyme causes significant $^{19}F$ NMR chemical shift modulation of trifluoromethyl derivatives of 6,7-dimethyl-8-ribityllumazine in complex with the protein, while substitution of A43 results in smaller chemical shift changes.