Search results for "motif"

showing 10 items of 290 documents

Phosphorylated immunoreceptor tyrosine-based activation motifs and integrin cytoplasmic domains activate spleen tyrosine kinase via distinct mechanis…

2018

Spleen tyrosine kinase (Syk) is involved in cellular adhesion and also in the activation and development of hematopoietic cells. Syk activation induced by genomic rearrangement has been linked to certain T-cell lymphomas, and Syk inhibitors have been shown to prolong survival of patients with B-cell lineage malignancies. Syk is activated either by its interaction with a double-phosphorylated immunoreceptor tyrosine-based activation motif (pITAM), which induces rearrangements in the Syk structure, or by the phosphorylation of specific tyrosine residues. In addition to its immunoreceptor function, Syk is activated downstream of integrin pathways, and integrins bind to the same region in Syk a…

0301 basic medicinekinaasitCell signalingentsyymitIntegrinsintegrinIntegrinAmino Acid MotifsMutation MissenseSykPeptidechemical and pharmacologic phenomenaBiochemistryspleen tyrosine kinase (Syk)environment and public healthBiokemia solu- ja molekyylibiologia - Biochemistry cell and molecular biology03 medical and health sciencesProtein DomainsLääketieteen bioteknologia - Medical biotechnologyenzyme kineticshemic and lymphatic diseasescell signalingHumansSyk KinaseTyrosinePhosphorylationCell adhesionMolecular Biologychemistry.chemical_classificationsoluviestintäintegriinit030102 biochemistry & molecular biologybiologyChemistryta1182hemic and immune systemsCell Biology3. Good healthCell biologyEnzyme Activationenzymes and coenzymes (carbohydrates)030104 developmental biologyAmino Acid SubstitutionCytoplasmbiology.proteinPhosphorylationPeptidessurface plasmon resonance (SPR)Signal Transduction
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Recombinant mussel protein Pvfp-5β: A potential tissue bioadhesive

2019

During their lifecycle, many marine organisms rely on natural adhesives to attach to wet surfaces for movement and self-defence in aqueous tidal environments. Adhesive proteins from mussels are biocompatible and elicit only minimal immune responses in humans. Therefore these proteins have received increased attention for their potential applications in medicine, biomaterials and biotechnology. The Asian green mussel Perna viridis secretes several byssal plaque proteins, molecules that help anchor the mussel to surfaces. Among these proteins, protein-5β (Pvfp-5β) initiates interactions with the substrate, displacing interfacial water molecules before binding to the surface. Here, we establis…

0301 basic medicinemedicine.disease_causeBiochemistryepidermal growth factor (EGF)law.inventionMiceCell Movementlawbiophysicsstructural biologyrecombinantCells CulturedbiologyChemistryMarine proteinsAdhesionRecombinant ProteinsadhesionProtein Structure and FoldingRecombinant DNAadhesion proteinsbiomaterialsPernaCell SurvivalSurface PropertiesBioadhesivemussel03 medical and health sciencesmedicineAnimalsHumansMolecular BiologyEscherichia coliCell ProliferationTissue Engineering030102 biochemistry & molecular biologyProteinsCell BiologyMusselbiology.organism_classificationEGF-like motifs; Marine proteins; adhesion; adhesion proteins; biomaterials; biophysics; epidermal growth factor (EGF); structural biologyEGF-like motifs030104 developmental biologyStructural biologyCell cultureNIH 3T3 CellsBiophysicsTissue AdhesivesHeLa CellsPerna viridisJournal of Biological Chemistry
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Structural Basis of the High Affinity Interaction between the Alphavirus Nonstructural Protein-3 (nsP3) and the SH3 Domain of Amphiphysin-2

2016

We show that a peptide from Chikungunya virus nsP3 protein spanning residues 1728–1744 binds the amphiphysin-2 (BIN1) Src homology-3 (SH3) domain with an unusually high affinity (Kd 24 nM). Our NMR solution complex structure together with isothermal titration calorimetry data on several related viral and cellular peptide ligands reveal that this exceptional affinity originates from interactions between multiple basic residues in the target peptide and the extensive negatively charged binding surface of amphiphysin-2 SH3. Remarkably, these arginines show no fixed conformation in the complex structure, indicating that a transient or fluctuating polyelectrostatic interaction accounts for this …

0301 basic medicinenuclear magnetic resonance (NMR)Amino Acid MotifsStatic ElectricityPeptideTarget peptidePlasma protein bindingViral Nonstructural ProteinsBiologyhost-pathogen interactionBiochemistrySH3 domainsrc Homology Domainsamphiphysin SH3Structure-Activity Relationship03 medical and health sciencesProtein structuredynaminHumansShort linear motifprotein structureNuclear Magnetic Resonance BiomolecularMolecular BiologySrc homology 3 domain (SH3 domain)Adaptor Proteins Signal Transducingchemistry.chemical_classificationTumor Suppressor Proteinsta1182Nuclear ProteinsIsothermal titration calorimetryCell Biologyintrinsically disordered protein030104 developmental biologychemistryBiochemistrynsP3Protein Structure and FoldingAmphiphysinBiophysicsPeptidesChikungunya virusProtein BindingJournal of Biological Chemistry
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Graph-based network analysis of transcriptional regulation pattern divergence in duplicated yeast gene pairs

2019

The genome and interactome of Saccharomyces cerevisiae have been characterized extensively over the course of the past few decades. However, despite many insights gained over the years, both functional studies and evolutionary analyses continue to reveal many complexities and confounding factors in the construction of reliable transcriptional regulatory network models. We present here a graph-based technique for comparing transcriptional regulatory networks based on network motif similarity for gene pairs. We construct interaction graphs for duplicated transcription factor pairs traceable to the ancestral whole-genome duplication as well as other paralogues in Saccharomyces cerevisiae. We c…

0303 health sciencesGene regulatory networkComputational biologyBiologyGenomeInteractomeGenetic divergence03 medical and health sciencesNetwork motif0302 clinical medicineGene duplicationDivergence (statistics)Gene030217 neurology & neurosurgery030304 developmental biologyProceedings of the Tenth International Conference on Computational Systems-Biology and Bioinformatics
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Network motif-based analysis of regulatory patterns in paralogous gene pairs

2020

Current high-throughput experimental techniques make it feasible to infer gene regulatory interactions at the whole-genome level with reasonably good accuracy. Such experimentally inferred regulatory networks have become available for a number of simpler model organisms such as S. cerevisiae, and others. The availability of such networks provides an opportunity to compare gene regulatory processes at the whole genome level, and in particular, to assess similarity of regulatory interactions for homologous gene pairs either from the same or from different species. We present here a new technique for analyzing the regulatory interaction neighborhoods of paralogous gene pairs. Our central focu…

0303 health sciencesGenomeGene regulatory networkComputational BiologyWhole genome duplicationSaccharomyces cerevisiaeComputational biologyParalogous GeneBiologyBiochemistryComputer Science ApplicationsEvolution Molecular03 medical and health sciencesNetwork motif0302 clinical medicineGene DuplicationEscherichia coliAnimalsGene Regulatory NetworksCaenorhabditis elegansMolecular BiologyGene030217 neurology & neurosurgeryTranscription Factors030304 developmental biologyJournal of Bioinformatics and Computational Biology
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MAGA: A Supervised Method to Detect Motifs From Annotated Groups in Alignments

2020

Multiple sequence alignments are usually phylogenetically driven. They are studied in the framework of evolution. But sometimes, it is interesting to study residue conservation at positions unconstrained by evolutionary rules. We present a supervised method to access a layer of information difficult to appreciate visually when many protein sequences are aligned. This new tool (MAGA; http://cbdm-01.zdv.uni-mainz.de/~munoz/maga/ ) locates positions in multiple sequence alignments differentially conserved in manually defined groups of sequences.

0303 health sciencesmultiple sequence alignmentsSequence analysisComputer science0206 medical engineeringMethods and ProtocolsSequence analysislcsh:Evolution02 engineering and technologyComputational biologyComputer Science Applications03 medical and health sciencesmotif findingcomputational biologyweb servicesGeneticslcsh:QH359-425020602 bioinformaticsEcology Evolution Behavior and Systematics030304 developmental biologyEvolutionary Bioinformatics
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Small Residues Inhibit Homo-Dimerization of the Human Carbonic Anhydrase XII Transmembrane Domain

2021

Amino acids with small side chains and motifs of small residues in a distance of four are rather abundant in human single-span transmembrane helices. While interaction of such helices appears to be common, the role of the small residues in mediating and/or stabilizing transmembrane helix oligomers remains mostly elusive. Yet, the mere existence of (small)xxx(small) motifs in transmembrane helices is frequently used to model dimeric TM helix structures. The single transmembrane helix of the human carbonic anhydrases XII contains a large number of amino acids with small side chains, and critical involvement of these small amino acids in dimerization of the transmembrane domain has been sugges…

540 Chemistry and allied sciencesGALLEXGxxxGChemical technologycarbonic anhydrase XIITP1-1185transmembrane domainArticle570 Life sciencessmall amino acidsChemical engineering540 ChemieTP155-156interaction propensity570 Biowissenschaftenhelix–helix interactioninteraction motifMembranes
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Inducible ASABF-Type Antimicrobial Peptide from the Sponge Suberites domuncula: Microbicidal and Hemolytic Activity in Vitro and Toxic Effect on Moll…

2011

Since sponges, as typical filter-feeders, are exposed to a high load of attacking prokaryotic and eukaryotic organisms, they are armed with a wide arsenal of antimicrobial/cytostatic low-molecular-weight, non-proteinaceous bioactive compounds. Here we present the first sponge agent belonging to the group of ASABF-type antimicrobial peptides. The ASABF gene was identified and cloned from the demospongeSuberites domuncula. The mature peptide, with a length of 64 aa residues has a predicted pI of 9.24, and comprises the characteristic CSαβ structural motif. Consequently, the S. domuncula ASABF shares high similarity with the nematode ASABFs ; it is distantly related to the defensins. The recom…

ASABFAntimicrobial peptidesGastropodaMolecular Sequence DataPharmaceutical SciencePeptideMicrobial Sensitivity TestsGram-Positive BacteriaReal-Time Polymerase Chain ReactionArticleMicrobiology03 medical and health sciencesantimicrobial peptidesAnti-Infective AgentsSequence Analysis ProteinDrug DiscoveryAnimalsBittium sp.Structural motiflcsh:QH301-705.5Pharmacology Toxicology and Pharmaceutics (miscellaneous)spongesPhylogeny030304 developmental biologychemistry.chemical_classification0303 health sciencesbiology030306 microbiologyEffectorHemolytic AgentsapoptosisGeologyBittium spsponges; <em>Suberites domuncula</em>; ASABF; antimicrobial peptides; apoptosis; <em>Bittium</em> sp.biology.organism_classificationSuberites domunculasponges ; Suberites domuncula ; ASABF ; antimicrobial peptides ; apoptosis ; Bittium sp.Recombinant ProteinsSuberites domunculaSpongeEnzymelcsh:Biology (General)chemistryMolluscaSuberitesSuberitesAntimicrobial Cationic PeptidesMarine Drugs
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A series of West European patients with severe cardiac and skeletal myopathy associated with a de novo R406W mutation in desmin.

2003

Desminopathy is a familial or sporadic cardiac and skeletal muscular dystrophy associated with mutations in desmin. We have previously characterized a de novo desmin R406W mutation in a patient of European origin with early onset muscle weakness in the lower extremities and atrioventricular conduction block requiring a permanent pacemaker. The disease relentlessly progressed resulting in severe incapacity within 5 years after onset. We have now identified three other patients with early onset rapidly progressive cardiac and skeletal myopathy caused by this same desmin R406W mutation. The mutation was present in each studied patient, but not in their parents or other unaffected family member…

AdultMaleModels Molecularmedicine.medical_specialtyPathologyNeurologyHeart diseaseAdolescentAmino Acid MotifsCardiomyopathymacromolecular substancesDiseaseBiologyProtein Structure SecondaryDesmin03 medical and health sciences0302 clinical medicineMuscular DiseasesmedicineHumansMuscular dystrophyMyopathyMuscle SkeletalConserved Sequence030304 developmental biology0303 health sciencesMuscle WeaknessBase SequenceMyocardiumMuscle weaknessAnatomymedicine.diseasePedigreeEuropeHeart BlockNeurologyAmino Acid SubstitutionMutationDisease ProgressionDesminFemaleNeurology (clinical)medicine.symptomCardiomyopathies030217 neurology & neurosurgeryJournal of neurology
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A rhamnose-binding lectin from sea bass (Dicentrarchus labrax) plasma agglutinates and opsonizes pathogenic bacteria

2014

Abstract The discovery of rhamnose-binding lectins (RBLs) in teleost fish eggs led to the identification of a novel lectin family characterized by a unique sequence motif and a structural fold, and initially proposed to modulate fertilization. Further studies of the RBL tissue localization and gene organization were also suggestive of role(s) in innate immunity. Here we describe the purification, and biochemical and functional characterization of a novel RBL (DlRBL) from sea bass (Dicentrarchus labrax) serum. The purified DlRBL had electrophoretic mobilities corresponding to 24 kDa and 100 kDa under reducing and non-reducing conditions, respectively, suggesting that in plasma the DlRBL is p…

AgglutinationGram-negative bacteriaErythrocytesRhamnoselectin; D. labraxImmunologyAmino Acid MotifsMolecular Sequence DataRhamnoseArticlechemistry.chemical_compoundPlasmaPhagocytosisLectinsEscherichia coliAnimalsAmino Acid SequenceSea bassPeptide sequencePhylogenybiologyD. labraxLectinRhamnose bindingBacterial Infectionsbiology.organism_classificationImmunity InnateProtein Structure TertiaryBiochemistrychemistrybiology.proteinMacrophages PeritoneallectinBassRabbitsProtein MultimerizationSequence motifDevelopmental BiologyHomotetramerProtein Binding
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