Search results for "030102 biochemistry & molecular biology"

showing 4 items of 174 documents

OpenTIMS, TimsPy, and TimsR: Open and Easy Access to timsTOF Raw Data

2021

The Bruker timsTOF Pro is an instrument that couples trapped ion mobility spectrometry (TIMS) to high-resolution time-of-flight (TOF) mass spectrometry (MS). For proteomics, lipidomics, and metabolomics applications, the instrument is typically interfaced with a liquid chromatography (LC) system. The resulting LC-TIMS-MS data sets are, in general, several gigabytes in size and are stored in the proprietary Bruker Tims data format (TDF). The raw data can be accessed using proprietary binaries in C, C++, and Python on Windows and Linux operating systems. Here we introduce a suite of computer programs for data accession, including OpenTIMS, TimsR, and TimsPy. OpenTIMS is a C++ library capable …

Proteomics0301 basic medicineSwift030102 biochemistry & molecular biologyComputer scienceReading (computer)SuiteGeneral Chemistrycomputer.file_formatPython (programming language)Hierarchical Data Formatcomputer.software_genreBiochemistryMass Spectrometry03 medical and health sciences030104 developmental biologyData accessIon Mobility SpectrometryOperating systemRaw datacomputerSoftwareChromatography Liquidcomputer.programming_languageCodebaseJournal of Proteome Research
researchProduct

Proteomic composition of Nipah virus-like particles

2017

Abstract Virions are often described as virus-only entities with no cellular components with the exception of the lipids in their membranes. However, advances in proteomics are revealing substantial amounts of host proteins in the viral particles. In the case of Nipah virus (NiV), the viral components in the virion have been known for some time. Nonetheless, no information has been obtained regarding the cellular proteins in the viral particles. To address this question, we produced Virus-Like Particles (VLPs) for NiV by expressing the F, G and M proteins in human-derived cells. Next, the proteomic content in these VLPs was analyzed by LC-MS/MS. We identified 67 human proteins including sol…

Proteomics0301 basic medicinevirusesNipah virusHost–pathogen interactionBiophysicsBiologyProteomicsBiochemistryVirusViral Proteins03 medical and health sciencesViral life cycleViral envelopeTandem Mass SpectrometryViral entryHumans030102 biochemistry & molecular biologyNipah VirusVirionVirology030104 developmental biologyCellular componentHost-Pathogen InteractionsChromatography LiquidProtein BindingJournal of Proteomics
researchProduct

APOBEC4 Enhances the Replication of HIV-1

2016

APOBEC4 (A4) is a member of the AID/APOBEC family of cytidine deaminases. In this study we found a high mRNA expression of A4 in human testis. In contrast, there were only low levels of A4 mRNA detectable in 293T, HeLa, Jurkat or A3.01 cells. Ectopic expression of A4 in HeLa cells resulted in mostly cytoplasmic localization of the protein. To test whether A4 has antiviral activity similar to that of proteins of the APOBEC3 (A3) subfamily, A4 was co-expressed in 293T cells with wild type HIV-1 and HIV-1 luciferase reporter viruses. We found that A4 did not inhibit the replication of HIV-1 but instead enhanced the production of HIV-1 in a dose-dependent manner and seemed to act on the viral L…

RNA virusesMale0301 basic medicineMolecular biologylcsh:MedicineArtificial Gene Amplification and ExtensionCytidinePathology and Laboratory MedicineVirus ReplicationBiochemistryPolymerase Chain ReactionJurkat cellschemistry.chemical_compoundCytidine deaminationImmunodeficiency VirusesTranscription (biology)TestisMedicine and Health Scienceslcsh:SciencePromoter Regions GeneticMultidisciplinaryCytidineTransfectionEnzymesImmunoblot AnalysisMedical MicrobiologyDeaminationViral PathogensViruses293T cellsCell linesPathogensOxidoreductasesBiological culturesLuciferaseResearch ArticleMolecular Probe TechniquesDNA constructionBiologyMicrobiologyCell Line03 medical and health sciencesCytidine DeaminaseRetrovirusesHumansMicrobial PathogensHIV Long Terminal Repeat030102 biochemistry & molecular biologylcsh:RLentivirusHEK 293 cellsOrganismsBiology and Life SciencesHIVProteinsPromoterMolecular biologyResearch and analysis methodsMolecular biology techniques030104 developmental biologychemistryPlasmid ConstructionHIV-1Enzymologylcsh:QEctopic expressionCloningPLOS ONE
researchProduct

2018

Tetraspanins (Tspans) are a family of four-span transmembrane proteins, known as plasma membrane “master organizers.” They form Tspan-enriched microdomains (TEMs or TERMs) through lateral association with one another and other membrane proteins. If multiple microdomains associate with each other, larger platforms can form. For infection, viruses interact with multiple cell surface components, including receptors, activating proteases, and signaling molecules. It appears that Tspans, such as CD151, CD82, CD81, CD63, CD9, Tspan9, and Tspan7, coordinate these associations by concentrating the interacting partners into Tspan platforms. In addition to mediating viral attachment and entry, these …

lcsh:Immunologic diseases. Allergy0301 basic medicineCell signalingTetraspaninsMini ReviewreceptorImmunology610 MedizinbuddingvirusBiologyVirusStructure-Activity Relationship03 medical and health sciencesMembrane MicrodomainsTetraspanintrafficking610 Medical sciencesAnimalsHumansendocytosisImmunology and Allergy030102 biochemistry & molecular biologymicrodomainLipid microdomainMembrane ProteinsVirus InternalizationTransmembrane proteinCell biologytetraspanin030104 developmental biologyMembrane proteinViral replicationVirus DiseasesHost-Pathogen Interactionsentrylcsh:RC581-607BiomarkersCD81Frontiers in Immunology
researchProduct