The first step to installing COMSOL Multiphysics is verifying you have your license information. When you purchase a license, you will receive it in the form of a .dat file as an attachment from an @comsol.com email address. You must upload this active .dat license file to your COMSOL Access account before you can download the installer. (License files and the information about them are emailed to the contact that COMSOL has listed in its system; you may need to contact the person responsible for your organization's license files in order to download the installer.)
The solution is to update the on-site COMSOL License Manager software from COMSOL version 6.0 to version 6.1. Step-by-step instructions can be found below.Note: the COMSOL 6.1 license manager binaries and license files are backward compatible with COMSOL installations back to version 3.5a. This means that existing installations of COMSOL 6.0 and earlier will continue to function as normal after the license manager has been updated to version 6.1.
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Go to the Config Services page. Change the paths to lmgrd.exe, and license.dat so that they all point to the COMSOL 6.1 installation directory. Starting with the version of the Flexnet distributed with COMSOL Multiphysics 5.4, the permissions where the license manager is allowed to write has been changed. The current recommendation is to store the debug log file, comsol61.log in the directory C:\ProgramData\COMSOL.
Stop the COMSOL license manager: Make the comsol60/multiphysics/license/$arch directory the current directory, where $arch is either glnxa64 (64-bit Linux), glnxarm64 (ARM Linux), maci64 (64-bit macOS), or macarm64 (ARM macOS). Stop the 6.0 license manager with the lmdown command:
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This study evaluates the metabolic profile of JM216 [bis(acetato)ammine-dichloro(cyclohexylamine) platinum(IV)], the first orally administrable platinum complex, in plasma ultrafiltrates of 12 patients (n = 2-4 time points per patient) following different doses of drug (120, 200, 340, 420, 560 mg/m2). The biotransformation profile was evaluated by high-performance liquid chromatography (HPLC) followed by atomic absorption spectrophotometry (AA). The AA profiles were compared with those previously identified by HPLC on line with mass spectrometry (HPLC-MS) in plasma incubated with JM216. A total of six platinum peaks (Rt = 5.5, 7.2, 10.6, 12.4, 15.6, and 21.6 min, respectively) were observed in patients' plasma ultrafiltrate samples, of which only four appeared during the first 6 h post-treatment. Four of these coeluted with those observed and identified previously in plasma incubation medium. No parent JM216 was detected. The major metabolite seen in patients was the Pt II complex JM118 [cis-amminedichloro-(cyclohexylamine)platinum(II)] and was observed in all the patients. Interestingly, the second metabolite was shown to coelute with the Pt IV species JM383 [bis-acetatoammine(cyclohexylamine)dihydroxoplatinum (IV)]. Both JM118 and JM383 were identified by HPLC-MS in a clinical sample. Peak C, which was a minor product (less than 5% of the free platinum), coeluted with JM559 [bis-acetatoammine-chloro(cyclohexylalamine)hydroxoplatin um(IV)]. The cytotoxicity profile of all three metabolites in a panel of cisplatin-sensitive and -resistant human ovarian carcinoma cell lines was very close to that of the parent drug. In addition, the concentrations of JM118 reached in patients' plasma ultrafiltrate were comparable with the cytotoxic levels of the compound determined in the ovarian carcinoma panel of cell lines. Two metabolites were seen in patients but not in the in vitro incubation medium, suggesting the involvement of a possible enzymatic reaction. Thus, the
Genome-wide experimental studies in Saccharomyces cerevisiae reveal that autonomous replicating sequence (ARS) requires an essential consensus sequence (ACS) for replication activity. Computational studies identified thousands of ACS like patterns in the genome. However, only a few hundreds of these sites act as replicating sites and the rest are considered as dormant or evolving sites. In a bid to understand the sequence makeup of replication sites, a content and context-based analysis was performed on a set of replicating ACS sequences that binds to origin-recognition complex (ORC) denoted as ORC-ACS and non-replicating ACS sequences (nrACS), that are not bound by ORC. In this study, DNA properties such as base composition, correlation, sequence dependent thermodynamic and DNA structural profiles, and their positions have been considered for characterizing ORC-ACS and nrACS. Analysis reveals that ORC-ACS depict marked differences in nucleotide composition and context features in its vicinity compared to nrACS. Interestingly, an A-rich motif was also discovered in ORC-ACS sequences within its nucleosome-free region. Profound changes in the conformational features, such as DNA helical twist, inclination angle and stacking energy between ORC-ACS and nrACS were observed. Distribution of ACS motifs in the non-coding segments points to the locations of ORC-ACS which are found far away from the adjacent gene start position compared to nrACS thereby enabling an accessible environment for ORC-proteins. Our attempt is novel in considering the contextual view of ACS and its flanking region along with nucleosome positioning in the S. cerevisiae genome and may be useful for any computational prediction scheme. 2ff7e9595c
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