Search results for "structures"

showing 10 items of 4815 documents

Thermal-,Pressure-, and Light-Induced Spin Transition in Novel Cyanide-Bridged FeII-AgI Bimetallic Compounds with Three-Dimensional Interpenetrating …

2002

[EN] Low-spin, high-spin and spin-transition behaviours have been observed for the doubly interpenetrating three-dimensional bimetallic compounds {Fe-II(pz)[Ag(CN)(2)](2)}.pz (pz= pyrazine), {Fe-II(4,4'-bipy)(2)[Ag(CN)(2)](2)} (4,4'-bipy-4,4'-bipyridine), and {Fe-II-(bpe)(2)[Ag(CN)(2)](2)} (bpe = bispyridylethylene), respectively. The single crystals of the bpe derivative undergo a spin transition with a large hysteresis loop at about 95 K. After several warming and cooling cycles, the single crystals become a microcrystalline powder with 50% spin transition. Influence of pressure- as well as light-induced excited spin-state trapping (LIESST) on the thermal 50% spin transition of the microc…

CyanidesSpin statesPyrazineChemistryIronOrganic ChemistrySpin transitionGeneral ChemistrySpin crossoverCooperative phenomenaInterpenetrating 3D structuresCatalysisLIESSTCrystallographychemistry.chemical_compoundBipyridineNuclear magnetic resonanceMicrocrystallineSpin crossoverFISICA APLICADABimetallic strip
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A Note on Keys and Keystreams of Chacha20 for Multi-key Channels

2018

In this paper we analyze the keystreams generated by the Chacha20 stream cipher. We also compare these to the ones generated by its predecessor, the RC4 stream cipher. Due to the proposed multi-key channels in the upcoming TLS 1.3 standard we analyze the behavior of the keystream in the boundary case where there is a single bit difference between two keys used for the initiation of the stream cipher algorithms. The goal is to check whether a single bit change in the key has any predictable influence on the bits of the keystream output.

Cybersecuritybusiness.industryComputer scienceKeystreamBoundary (topology)Stream cipher020206 networking & telecommunications02 engineering and technologyRC4Symmetric-key algorithmChacha200202 electrical engineering electronic engineering information engineering020201 artificial intelligence & image processingHardware_ARITHMETICANDLOGICSTRUCTURESbusinessSymmetric encryptionStream cipherAlgorithm
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Versatile Direct and Transpose Matrix Multiplication with Chained Operations: An Optimized Architecture Using Circulant Matrices

2016

With growing demands in real-time control, classification or prediction, algorithms become more complex while low power and small size devices are required. Matrix multiplication (direct or transpose) is common for such computation algorithms. In numerous algorithms, it is also required to perform matrix multiplication repeatedly, where the result of a multiplication is further multiplied again. This work describes a versatile computation procedure and architecture: one of the matrices is stored in internal memory in its circulant form, then, a sequence of direct or transpose multiplications can be performed without timing penalty. The architecture proposes a RAM-ALU block for each matrix c…

Cycles per instructionBlock matrix020206 networking & telecommunications02 engineering and technologyParallel computingMatrix chain multiplicationMatrix multiplication020202 computer hardware & architectureTheoretical Computer ScienceMatrix (mathematics)Computational Theory and MathematicsHardware and ArchitectureTranspose0202 electrical engineering electronic engineering information engineeringMultiplicationHardware_ARITHMETICANDLOGICSTRUCTURESArithmeticCirculant matrixSoftwareMathematicsIEEE Transactions on Computers
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Liver Fat, Adipose Tissue, and Body Composition Changes After Switching from a Protease Inhibitor or Efavirenz to Raltegravir.

2021

Integrase inhibitors appear to increase body weight, but paradoxically some data indicate that raltegravir (RAL) may decrease liver fat. Our objective was to study the effects of switching from a protease inhibitor (PI) or efavirenz (EFV) to RAL on liver fat, body composition, and metabolic parameters among people living with HIV (PLWH) with high risk for nonalcoholic fatty liver disease (NAFLD). We randomized overweight PLWH with signs of metabolic syndrome to switch a PI or EFV to RAL (

Cyclopropanesmedicine.medical_specialtyanimal structuresEfavirenzIntegrase inhibitorAdipose tissueHIV Infections03 medical and health scienceschemistry.chemical_compound0302 clinical medicineAdipocyteInternal medicineRaltegravir PotassiumNonalcoholic fatty liver diseasemedicineHumansProtease inhibitor (pharmacology)Protease Inhibitors030212 general & internal medicinebusiness.industryPublic Health Environmental and Occupational Healthmedicine.diseaseRaltegravir3. Good healthBenzoxazinesInfectious DiseasesEndocrinologychemistryAdipose TissueLiverAlkynesBody Composition030211 gastroenterology & hepatologymedicine.symptombusinessWeight gainmedicine.drugAIDS patient care and STDs
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Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1.

1999

AbstractThe interaction of cytoplasmic dynein with its cargoes is thought to be indirectly mediated by dynactin, a complex that binds to the dynein intermediate chain. However, the roles of other dynein subunits in cargo binding have been unknown. Here we demonstrate that dynein translocates rhodopsin-bearing vesicles along microtubules. This interaction occurs directly between the C-terminal cytoplasmic tail of rhodopsin and Tctex-1, a dynein light chain. C-terminal rhodopsin mutations responsible for retinitis pigmentosa inhibit this interaction. Our results point to an alternative docking mechanism for cytoplasmic dynein, provide novel insights into the role of motor proteins in the pola…

CytoplasmRhodopsingenetic structuresMicrotubule-associated proteinRecombinant Fusion ProteinsDyneinMolecular Sequence DataReceptors Cell Surfacemacromolecular substancesBiologyT-Complex Genome RegionMicrotubulesGeneral Biochemistry Genetics and Molecular BiologyMotor protein03 medical and health sciencesMice0302 clinical medicineMicrotubuleAnimalsAmino Acid Sequence030304 developmental biologyt-Complex Genome Region0303 health sciencesBinding SitesBiochemistry Genetics and Molecular Biology(all)DyneinsNuclear ProteinsBiological Transport3. Good healthCell biologyCytoplasmRhodopsinMutagenesisDynactinbiology.proteinMicrotubule ProteinsCattlesense organsMicrotubule-Associated Proteins030217 neurology & neurosurgeryPhotoreceptor Cells VertebrateCell
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Automatic Counting of Intra-Cellular Ribonucleo-Protein Aggregates in Saccharomyces cerevisiae Using a Textural Approach.

2019

AbstractIn the context of microbiology, recent studies show the importance of ribonucleo-protein aggregates (RNPs) for the understanding of mechanisms involved in cell responses to specific environmental conditions. The assembly and disassembly of aggregates is a dynamic process, the characterization of the stage of their evolution can be performed by the evaluation of their number. The aim of this study is to propose a method to automatically determine the count of RNPs. We show that the determination of a precise count is an issue by itself and hence, we propose three textural approaches: a classical point of view using Haralick features, a frequency point of view with generalized Fourier…

CytoplasmSaccharomyces cerevisiae ProteinsZernike polynomialsComputer scienceSaccharomyces cerevisiaeGreen Fluorescent Proteins0211 other engineering and technologiessub-cellular structuresContext (language use)02 engineering and technologySaccharomyces cerevisiaeProtein aggregationribonucleo-protein aggregatesCytoplasmic GranulesModels BiologicalPoly(A)-Binding Proteins03 medical and health sciencessymbols.namesakeProtein Aggregates[SDV.IDA]Life Sciences [q-bio]/Food engineeringGeneralized Fourier descriptorsInstrumentation030304 developmental biology021110 strategic defence & security studies0303 health sciencesFusionHaralickbiologyZernikeA proteinbiology.organism_classificationFourier transformMicroscopy FluorescenceRibonucleoproteinssymbolsBiological systemMicroscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada
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Nuclear Translocation of Papillomavirus Minor Capsid Protein L2 Requires Hsc70

2004

ABSTRACT Minor capsid protein L2 of papillomaviruses plays an essential role in virus assembly by recruiting viral components to PML bodies, the proposed sites of virus morphogenesis. We demonstrate here that the function of L2 in virus assembly requires the chaperone Hsc70. Hsc70 was found dispersed in naturally infected keratinocytes and cultured cells. A dramatic relocation of Hsc70 from the cytoplasm to PML bodies was induced in these cells by L2 expression. Hsc70-L2 complex formation was confirmed by coimmunoprecipitation. The complex was modulated by the cochaperones Hip and Bag-1, which stabilize and destabilize Hsc70-substrate complexes, respectively. Cytoplasmic depletion of Hsc70 …

Cytoplasmanimal structuresImmunoprecipitationvirusesImmunologyActive Transport Cell Nucleusmacromolecular substancesBiologyMicrobiologyVirusGreen fluorescent proteinCell Line TumorVirologyAnimalsHSP70 Heat-Shock ProteinsCOS cellsHSC70 Heat-Shock ProteinsVirionOncogene Proteins ViralMolecular biologyVirus-Cell InteractionsTransport proteinCell biologyProtein TransportCapsidCytoplasmInsect ScienceChaperone (protein)COS Cellsembryonic structuresbiology.proteinCapsid ProteinsJournal of Virology
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Interaction of Mitogen-activated Protein Kinases with the Kinase Interaction Motif of the Tyrosine Phosphatase PTP-SL Provides Substrate Specificity …

1999

ERK1 and ERK2 associate with the tyrosine phosphatase PTP-SL through a kinase interaction motif (KIM) located in the juxtamembrane region of PTP-SL. A glutathione S-transferase (GST)-PTP-SL fusion protein containing the KIM associated with ERK1 and ERK2 as well as with p38/HOG, but not with the related JNK1 kinase or with protein kinase A or C. Accordingly, ERK2 showed in vitro substrate specificity to phosphorylate GST-PTP-SL in comparison with GST-c-Jun. Furthermore, tyrosine dephosphorylation of ERK2 by the PTP-SLDeltaKIM mutant was impaired. The in vitro association of ERK1/2 with GST-PTP-SL was highly stable; however, low concentrations of nucleotides partially dissociated the ERK1/2.P…

Cytoplasmanimal structuresProtein Kinase C-alphaRecombinant Fusion ProteinsCèl·lulesNerve Tissue ProteinsProtein tyrosine phosphataseMitogen-activated protein kinase kinaseTransfectionenvironment and public healthBiochemistrySH3 domainReceptor tyrosine kinaseMAP2K7Substrate SpecificitySerineAnimalsc-RafAmino Acid SequenceMolecular BiologyProtein Kinase CSequence DeletionMitogen-Activated Protein Kinase 1Binding SitesMitogen-Activated Protein Kinase 3biologyCyclin-dependent kinase 2Intracellular Signaling Peptides and ProteinsJNK Mitogen-Activated Protein KinasesCell BiologyCyclic AMP-Dependent Protein KinasesIsoenzymesenzymes and coenzymes (carbohydrates)KineticsBiochemistryAmino Acid SubstitutionCOS CellsCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinMutagenesis Site-DirectedCyclin-dependent kinase 9CattleMitogen-Activated Protein KinasesProtein Tyrosine PhosphatasesProteïnes
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A novel regulatory mechanism of MAP kinases activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphatase

1999

Protein tyrosine phosphatase PTP-SL retains mitogen-activated protein (MAP) kinases in the cytoplasm in an inactive form by association through a kinase interaction motif (KIM) and tyrosine dephosphorylation. The related tyrosine phosphatases PTP-SL and STEP were phosphorylated by the cAMP-dependent protein kinase A (PKA). The PKA phosphorylation site on PTP-SL was identified as the Ser231 residue, located within the KIM. Upon phosphorylation of Ser231, PTP-SL binding and tyrosine dephosphorylation of the MAP kinases extracellular signal–regulated kinase (ERK)1/2 and p38α were impaired. Furthermore, treatment of COS-7 cells with PKA activators, or overexpression of the Cα catalytic subunit …

Cytoplasmanimal structuresRecombinant Fusion ProteinsCèl·lulesAmino Acid MotifsNerve Tissue ProteinsProtein tyrosine phosphataseSH2 domainTransfectionenvironment and public healthModels Biologicalp38 Mitogen-Activated Protein KinasesReceptor tyrosine kinaseSH3 domainCell LinePhosphoserinetyrosine phosphatasesAnimalsHumansProtein phosphorylationPKAReceptor-Like Protein Tyrosine Phosphatases Class 7PhosphorylationPTP-SLCell NucleusMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3biologyBrief ReportIntracellular Signaling Peptides and ProteinsBiological TransportCell BiologyProtein Tyrosine Phosphatases Non-ReceptorCyclic AMP-Dependent Protein KinasesEnzyme Activationenzymes and coenzymes (carbohydrates)MAP kinasesBiochemistryMitogen-activated protein kinaseCOS CellsMutationbiology.proteinPhosphorylationMitogen-Activated Protein KinasesProtein Tyrosine PhosphatasesEnzimssignal transductionProto-oncogene tyrosine-protein kinase Src
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Nuclear and Cytoplasmic Soluble Proteins Extraction from a Small Quantity of Drosophila’s Whole Larvae and Tissues

2015

The identification and study of protein’s function in several model organisms is carried out using both nuclear and cytoplasmic extracts. For a long time, Drosophila’s embryos have represented the main source for protein extractions, although in the last year, the importance of collecting proteins extracts also from larval tissues has also been understood. Here we report a very simple protocol, improved by a previously developed method, to produce in a single extraction both highly stable nuclear and cytoplasmic protein extracts from a small quantity of whole Drosophila’s larvae or tissues, suitable for biochemical analyses like co-immunoprecipitation.

Cytoplasmanimal structuresved/biology.organism_classification_rank.speciesBiologyCell FractionationCatalysislcsh:ChemistryInorganic ChemistryCytoplasmic proteinBotanyTechnical NoteAnimalsDrosophila ProteinsPhysical and Theoretical ChemistryModel organismlcsh:QH301-705.5Molecular BiologyDrosophilaSpectroscopyCell NucleusLarvaved/biologyOrganic ChemistryExtraction (chemistry)fungiproteins extractionEmbryoGeneral Medicinebiology.organism_classificationhnRNPsComputer Science ApplicationsDrosophila melanogasterlcsh:Biology (General)lcsh:QD1-999BiochemistryCytoplasmLarvaDrosophilaFunction (biology)International Journal of Molecular Sciences
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