Search results for "Dimerization"

showing 10 items of 143 documents

Greatly enhanced intermolecular π-dimer formation of a porphyrin trimer radical trications through multiple π bonds.

2010

A trefoil-like porphyrin trimer linked by triphenylamine (TPA-TPZn(3)) was synthesized. A three-electron oxidation of TPA-TPZn(3) forms a radical trication (TPA-TPZn(3)(3+)), in which each porphyrin ring undergoes a one-electron oxidation. The radical trication TPA-TPZn(3)(3+) spontaneously dimerizes to afford (TPA-TPZn(3))(2)(6+) in CH(2)Cl(2) . The characteristic charge-resonance band due to the charge delocalization over the π system of (TPA-TPZn(3))(2)(6+) was observed in the NIR region. The initial oxidation potential of TPA-TPZn(3) is negatively shifted relative to that of the corresponding monomer porphyrin, which results from the stabilization of the oxidized state of TPA-TPZn(3) as…

PorphyrinsMolecular StructureDimerOrganic ChemistryElectron Spin Resonance SpectroscopyTemperatureTrimerElectronsGeneral ChemistryPhotochemistryTriphenylaminePorphyrinCatalysislaw.inventionchemistry.chemical_compoundchemistryRadical ionlawStability constants of complexesCationsPi interactionElectron paramagnetic resonanceDimerizationOxidation-ReductionChemistry (Weinheim an der Bergstrasse, Germany)
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Sequence evolution, processing, and posttranslational modification of zonadhesin D domains in primates, as inferred from cDNA data

2005

Zonadhesin is a mammalian transmembrane sperm ligand. Precursor zonadhesin essentially consists of MAM (meprin/A5 antigen/mu receptor tyrosine phosphatase) domains, a mucin-like repeat, and D domains (homologous to von Willebrand D). Recent immunovisualization and binding assays indicate that zonadhesin D domains 1–3 bind postacrosomally to the zona pellucida. This feature has attracted considerable interest in the evolution of zonadhesin and its possible biological and biomedical implications. Previous molecular evolutionary analyses, however, were confined to cDNA sequences of only few distantly related species. Moreover, except for rabbit and pig, little is known about zonadhesin’s proce…

PrimatesDNA ComplementaryBase pairMolecular Sequence DataBiologyPROSITEEvolution MolecularComplementary DNAGeneticsmedicineAnimalsAmino Acid SequenceSelection GeneticZona pellucidaPhylogenyGeneticsComputational BiologyMembrane ProteinsGeneral MedicineLigand (biochemistry)Transmembrane proteinProtein Structure Tertiarymedicine.anatomical_structureEvolutionary biologyGenBankDimerizationProtein Processing Post-TranslationalSequence AlignmentFunction (biology)Protein Modification TranslationalGene
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The abrogation of the HOXB7/PBX2 complex induces apoptosis in melanoma through the miR-221&222-c-FOS pathway.

2013

Cutaneous melanoma is the fastest increasing cancer worldwide. Although several molecular abnormalities have been associated with melanoma progression, the underlying mechanisms are still largely unknown and few targeted therapies are under evaluation. Here we show that the HOXB7/PBX2 dimer acts as a positive transcriptional regulator of the oncogenic microRNA-221 and -222. In addition, demonstrating c-FOS as a direct target of miR-221&222, we identify a HOXB7/PBX2→miR-221&222 →c-FOS regulatory link, whereby the abrogation of functional HOXB7/PBX2 dimers leads to reduced miR-221&222 transcription and elevated c-FOS expression with consequent cell death. Taking advantage of the treatment wit…

Programmed cell deathCancer ResearchSkin NeoplasmsTranscription GeneticApoptosisSmall Interferingc-FosPolymerase Chain ReactionCell LineGeneticCell Line TumorProto-Oncogene ProteinsHOXB7/PBX2 complexmicroRNATranscriptional regulationmedicinemelanomaHumansPBXRNA Small InterferingDNA PrimersHomeodomain Proteinsc-FOS pathwayTumorbiologymicroRNABase SequenceMelanomaHOXB7; HXR9 peptide; melanoma; microRNA; PBX; Apoptosis; Base Sequence; Cell Line Tumor; DNA Primers; Dimerization; Homeodomain Proteins; Humans; Melanoma; MicroRNAs; Polymerase Chain Reaction; Proto-Oncogene Proteins; Proto-Oncogene Proteins c-fos; RNA Small Interfering; Skin Neoplasms; Transcription Genetic; Cancer Research; Oncologymedicine.diseaseMicroRNAsHXR9 peptideOncologyApoptosisCell cultureCutaneous melanomaHOXB7/PBX2 complex ;melanoma ;c-FOS pathwayCancer researchbiology.proteinHOXB7RNATranscriptionDimerizationProto-Oncogene Proteins c-fosCancer Cell Biology
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Co-regulator recruitment and the mechanism of retinoic acid receptor synergy.

2002

Crystal structure and co-regulator interaction studies have led to a general mechanistic view of the initial steps of nuclear receptor (NR) action. Agonist-induced transconformation of the ligand-binding domain (holo-LBD) leads to the formation of co-activator complexes, and destabilizes the co-repressor complexes bound to the ligand-free (apo) LBD. However, the molecular basis of retinoid-X receptor (RXR) 'subordination' in heterodimers, an essential mechanism to avoid signalling pathway promiscuity, has remained elusive. RXR, in contrast to its heterodimer partner, cannot autonomously induce transcription on binding of cognate agonists. Here we show that RXR can bind ligand and recruit co…

Protein ConformationReceptors Retinoic AcidPlasma protein bindingRetinoid X receptorLigandsNuclear Receptor Coactivator 2Structure-Activity RelationshipmedicineNuclear Receptor Co-Repressor 2Binding siteNuclear receptor co-repressor 2PhysicsMultidisciplinaryCell biologyDNA-Binding ProteinsRepressor ProteinsRetinoic acid receptorRetinoid X ReceptorsMechanism of actionBiochemistryNuclear receptorModels Chemicalembryonic structuresNuclear receptor coactivator 2medicine.symptomDimerizationProtein BindingTranscription FactorsNature
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Influence of hydrophobic matching on association of model transmembrane fragments containing a minimised glycophorin A dimerisation motif

2005

AbstractThe principles that govern the folding and packing of membrane proteins are still not completely understood. In the present work, we have revisited the glycophorin A (GpA) dimerisation motif that mediates transmembrane (TM) helix association, one of the best-suited models of membrane protein oligomerisation. By using artificial polyleucine TM segments we have demonstrated in this study that a pattern of only five amino acids (GVxxGVxxT) promotes specific dimerisation. Further, we have used this minimised GpA motif to assess the influence of hydrophobic matching on the TM helix packing process in detergent micelles and found that this factor modulates helix–helix association and/or d…

Protein FoldingRecombinant Fusion ProteinsAmino Acid MotifsMolecular Sequence DataBiophysicsBiochemistryMicelleHydrophobic mismatchHydrophobic mismatchStructural BiologyLeucineHelix packingGeneticsGlycophorinAnimalsHumansAmino Acid SequenceGlycophorinsMolecular BiologyPolyacrylamide gel electrophoresischemistry.chemical_classificationbiologyChemistryGlycophorin AProteïnes de membranaMembrane ProteinsMembrane protein associationCell BiologyTransmembrane proteinAmino acidTransmembrane domainBiochemistryMembrane proteinMutationTransmembrane helixBiophysicsbiology.proteinPeptidesDimerizationHydrophobic and Hydrophilic Interactions
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Wild-type Cu/Zn superoxide dismutase (SOD1) does not facilitate, but impedes the formation of protein aggregates of amyotrophic lateral sclerosis cau…

2009

Aggregation of Cu/Zn superoxide dismutase (SOD1) is a hallmark of a subset of familial amyotrophic lateral sclerosis (ALS) cases. The expression of wild-type SOD1 [SOD(hWT)] surprisingly exacerbates the phenotype of mutant SOD1 in vivo. Here we studied whether SOD1(hWT) may affect mutant SOD1 aggregation by employing fluorescence microscopy techniques combined with lifetime-based Förster resonance energy transfer (FRET). Only a very minor fraction of SOD1(hWT) was observed in aggregates induced by mutant SOD1(G37R), SOD1(G85R) or SOD1(G93C). Quite in contrast, co-expression of SOD(hWT) reduced the amount of mutant SOD1 in the aggregate fraction. Furthermore, we did not detect endogenous mou…

Protein Foldinganimal diseasesSOD1HeterodimerizationMice TransgenicEndogenyProtein aggregationCell Linelcsh:RC321-571MiceSuperoxide Dismutase-1In vivoFluorescence microscopeAnimalsHumanslcsh:Neurosciences. Biological psychiatry. NeuropsychiatrySuperoxide DismutaseChemistryWild typenutritional and metabolic diseasesAmyotrophic lateral sclerosisPhenotypeMolecular biologynervous system diseasesFörster resonance energy transferSolubilitynervous systemNeurologyFLIM-based FRETMutationProtein MultimerizationProtein aggregationNeurobiology of Disease
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Humoral autoreactivity directed against surfactant protein-A (SP-A) in rheumatoid arthritis synovial fluids.

2000

SUMMARY SP-A is found principally in the lung, and has been associated with lamellar bodies also found in the synovial joint. Both SP-A and C1q contain collagen-like regions, and SP-A and C1q have some structural similarities, both having a globular head region and a collagen-like tail. Here we are able to show that (i) autoreactivity to SP-A, as expressed by IgG and IgM autoantibodies, is present in synovial fluid (SF) isolated from patients with rheumatoid arthritis (RA); (ii) in absorption experiments only a limited degree of cross-reactivity between autoantibodies reactive with C1q and SP-A is observed; (iii) there is no cross-reactivity between autoantibodies reactive with type II coll…

Pulmonary Surfactant-Associated ProteinsKnee JointProteolipidsImmunologyType II collagenchemical and pharmacologic phenomenamedicine.disease_causeAutoantigensImmunoglobulin GAutoimmunityArthritis RheumatoidRheumatic DiseaseAntigenSynovial jointSynovial FluidmedicineImmunology and AllergySynovial fluidAnimalsHumansskin and connective tissue diseasesAutoantibodiesbiologyPulmonary Surfactant-Associated Protein AChemistryComplement C1qAutoantibodyPulmonary Surfactantsmedicine.anatomical_structureImmunoglobulin MImmunoglobulin MImmunoglobulin GImmunologybiology.proteinBinding Sites AntibodyCollagenPeptidesChickensDimerizationClinical and experimental immunology
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Structure and Matrix Isolation Infrared Spectrum of Formyl Fluoride Dimer:  Blue-Shift of the C−H Stretching Frequency

2006

Infrared spectroscopy (IR) of formyl fluoride (HCOF) dimer is studied in low-temperature argon and krypton matrixes. New IR absorptions, ca. 17 cm(-1) blue shifted from the monomer C-H stretching fundamental, are assigned to the HCOF dimer. The MP2/6-311++G calculations were utilized to define structures and harmonic frequencies of various HCOF dimers. Among the four optimized structures, the dimer having two C-H...O hydrogen bonds possesses strongest intermolecular bonding. The calculated harmonic frequencies of this dimer structure are shifted from the monomer similarly as observed in the experiment. Thus, we suggest that the experimentally observed blue shifted C-H bands belong to the di…

Quantitative Biology::BiomoleculesFormatesSpectrophotometry InfraredHydrogen bondInfraredDimerKryptonIntermolecular forceMatrix isolationchemistry.chemical_elementInfrared spectroscopyPhotochemistrySensitivity and SpecificityFluoridesCrystallographychemistry.chemical_compoundModels ChemicalchemistryPhysics::Atomic and Molecular ClustersQuantum TheoryComputer SimulationPhysical and Theoretical ChemistryDimerizationFormyl fluorideThe Journal of Physical Chemistry A
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Molecular Basis of DNA Photodimerization: Intrinsic Production of Cyclobutane Cytosine Dimers

2008

Based on CASPT2 results, the present contribution establishes for the first time that cytosine photodimer formation (CC) is mediated along the triplet and singlet manifold by a singlet-triplet crossing, (T1/S0)X, and by a conical intersection, (S1/S0)CI, respectively. The former can be accessed in a barrierless way from a great variety of photochemical avenues and exhibits a covalent single bond between the ethene C6-C6' carbon atoms of each monomer. The efficiency of the stepwise triplet mechanism, however, would be modulated by the effectiveness of the intersystem crossing mechanism. The results provide the grounds for the understanding of the potential photogenotoxicity of endogenous and…

Quantitative Biology::BiomoleculesPhotochemistryUltraviolet RaysChemistryDNAGeneral ChemistryConical intersectionPhotochemistryBiochemistryCatalysisCyclobutaneCytosinechemistry.chemical_compoundColloid and Surface ChemistryIntersystem crossingPyrimidine DimersCovalent bondExcited stateNucleic Acid ConformationSingle bondSinglet stateDimerizationCytosineDNA DamageJournal of the American Chemical Society
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Cytoplasmic STAT proteins associate prior to activation

2000

The commonly accepted model of STAT factor activation at the cytoplasmic part of the receptor assumes that signal transducers and activators of transcription (STATs) are recruited from a cytoplasmic pool of monomeric STAT proteins. Based on a previous observation that non-phosphorylated STAT3-Src homology 2 domains dimerize in vitro, we investigated whether the observed dimerization is of physiological relevance within the cellular context. We show that STAT1 and STAT3 are pre-associated in non-stimulated cells. Apparently, these complexes are not able to translocate into the nucleus. We provide evidence that the event of STAT activation is more complex than previously assumed.

STAT3 Transcription FactorCytoplasmCarcinoma HepatocellularMolecular Sequence DataCross ReactionsTransfectionCytoplasmic partBiochemistrystatTumor Cells CulturedAnimalsHumansProtein inhibitor of activated STATAmino Acid SequenceSTAT1PhosphorylationSTAT3MelanomaMolecular BiologySTAT4STAT6biologyInterleukin-6Liver NeoplasmsCell BiologyPrecipitin TestsMolecular biologyCell biologyDNA-Binding ProteinsSTAT1 Transcription FactorCOS CellsTrans-Activatorsbiology.proteinSTAT proteinTyrosineDimerizationResearch ArticleBiochemical Journal
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