Search results for "Point Mutation"

showing 10 items of 199 documents

Novel alpha-galactosidase A mutation in a female with recurrent strokes.

2012

Abstract Anderson–Fabry disease (AFD) is an X-linked inborn error of glycosphingolipid catabolism resulting from the deficient activity of the lysosomal exoglycohydrolase, a-galactosidase A. The complete genomic and cDNA sequences of the human alpha-galactosidase A gene have been determined and to date, several disease-causing alpha-galactosidase A mutations have been identified, including missense mutations, small deletions/insertions, splice mutations, and large gene rearrangements We report a case of a 56-year-old woman with recurrent cryptogenic strokes. Ophthalmological examination revealed whorled opacities of the cornea (cornea verticillata) and dilated tortuous conjunctival vessels.…

Pathologymedicine.medical_specialtyHeterozygoteClinical BiochemistryMolecular Sequence DataMutation MissenseBiologymedicine.disease_causeExonRecurrencemedicineMissense mutationHumansCornea verticillataAmino Acid SequenceGeneMutationBase SequencePoint mutationGeneral MedicineSequence Analysis DNAMiddle Agedmedicine.diseaseFabry diseaseMolecular biologyAngiokeratomaPedigreeStrokealpha-GalactosidaseFabry DiseaseFemalemedicine.symptomClinical biochemistry
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Single amino acids in the lumenal loop domain influence the stability of the major light-harvesting chlorophyll a/b complex.

2004

The major light-harvesting complex of photosystem II (LHCIIb) is one of the most abundant integral membrane proteins. It greatly enhances the efficiency of photosynthesis in green plants by binding a large number of accessory pigments that absorb light energy and conduct it toward the photosynthetic reaction centers. Most of these pigments are associated with the three transmembrane and one amphiphilic alpha helices of the protein. Less is known about the significance of the loop domains connecting the alpha helices for pigment binding. Therefore, we randomly exchanged single amino acids in the lumenal loop domain of the bacterially expressed apoprotein Lhcb1 and then reconstituted the muta…

Photosynthetic reaction centreProtein FoldingPhotosystem IIPigment bindingDNA Mutational AnalysisLight-Harvesting Protein ComplexesPeasPhotosystem II Protein ComplexBiologyBiochemistryTransmembrane proteinProtein Structure SecondaryProtein Structure TertiaryB vitaminsBiochemistryAmino Acid SubstitutionMutant proteinMutagenesis Site-DirectedPoint MutationAmino AcidsIntegral membrane proteinAccessory pigmentGene LibraryPlant ProteinsBiochemistry
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Effectiveness of screening for known mutations in Sicilian patients with "probable" familial hypercholesterolemia.

2002

Background and Aim: More than 750 mutations in the low-density lipoprotein (LDL) receptor gene are currently known to cause familial hypercholesterolemia (FH), but the array of mutations varies considerably in different populations. The definition of essentially all the LDL receptor gene mutations in a population is therefore a prerequisite for the implementation of nation-wide genetic testing for FH. Methods and Results: In this study, a screening strategy based on PCR-enzymatic digestion and PCR-allele specific hybridisation procedures was used to evaluate the frequency distributions of 11 known mutations in a cohort of 214 unrelated subjects meeting the diagnostic criteria of "probable" …

Point mutationNutrition and DieteticsSettore MED/09 - Medicina InternaEndocrinology Diabetes and MetabolismMedicine (miscellaneous)ExonsPolymerase Chain ReactionFHCohort StudiesHyperlipoproteinemia Type IIGene FrequencyReceptors LDLMutationScreeningHumansGenetic TestingCardiology and Cardiovascular MedicineSicilyFood Science
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The distribution of fitness effects caused by single-nucleotide substitutions in an RNA virus.

2004

6 pages, 3 figures.-- PMID: 15159545 [PubMed].-- PMCID: PMC420405.-- Supporting information (Table 3: Relevant information about each single-nucleotide substation mutant created) available at: http://www.pnas.org/content/101/22/8396/suppl/DC1

PopulationMutantMutagenesis (molecular biology technique)Evolutionary biologyVesicular stomatitis Indiana virusSingle-nucleotide substitutionsGenetic variationAnimalsPoint MutationMutational fitness effectseducationGeneticseducation.field_of_studyMultidisciplinarybiologyPoint mutationRNAGenetic VariationRNA virusRNA viral genomesBiological Sciencesbiology.organism_classificationBiological EvolutionGenetics PopulationVesicular stomatitis virusMutagenesis Site-DirectedProceedings of the National Academy of Sciences of the United States of America
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Rapid screening of the LDL receptor point mutation FH-Genoa/Palermo

1999

The LDL-receptor gene point mutation FH-Genoa/Palermo is the most frequent mutation responsible for Familial Hypercholesterolemia in Sicily. The mutation does not introduce or abolish any useful restriction site. We establish a GeneComb™-based strategy to identify this mutation in a population of Sicilian unrelated clinically diagnosed FH probands. The method was very sensitive and specific; 12 out of 90 (13.3%) unrelated FH probands were found to carry the FH-Genoa/Palermo mutation. According to these results, the FH-Genoa/Palermo is the more frequent LDL-receptor gene mutation among the Sicilian FH patients. Moreover FH-Genoa/Palermo is the mutation cluster to date more represented in Sou…

ProbandGeneticseducation.field_of_studyPoint mutationPopulationFamilial hypercholesterolemiaGene mutationBiologymedicine.diseaseRestriction siteMutation (genetic algorithm)LDL receptorGeneticsmedicineeducationGenetics (clinical)Human Mutation
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Inheritance and variable expression in Rubinstein-Taybi syndrome.

2010

Familial Rubinstein-Taybi syndrome (RTS) is very rare. Here we report on the 6th and 7th case of inherited RTS. Family 1 presents with incomplete or mild RTS over three generations; a 13-year-old girl (proband 1) with mild but typical facial features and learning disabilities, her very mildly affected mother (proband 2), and the maternal grandmother (proband 3). Family 2 includes three females with classical RTS (probands 4-6) and their father (proband 7) with broad thumbs and halluces. Proband 5 also had a brain tumor (ganglioglioma) at the age of 3 years. In probands 1-3, direct sequencing identified a novel CREBBP missense mutation, c.2728A > G (predicting p.Thr910Ala), that was absent i…

ProbandMaleRiskAdolescentDNA Mutational AnalysisMutation MissenseBiologyVariable ExpressionGenetic HeterogeneityGeneticsmedicineMissense mutationHumansPoint MutationFamilyAlleleGenetics (clinical)GeneticsRubinstein-Taybi SyndromeRubinstein–Taybi syndromeGenetic heterogeneityMosaicismPoint mutationmedicine.diseaseCREB-Binding ProteinPedigreePhenotypeChild PreschoolMutation (genetic algorithm)FemaleAmerican journal of medical genetics. Part A
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Thermal Isomerization Mechanism in Dronpa and Its Mutants.

2016

The photoswitching speed of the reversibly switchable fluorescent proteins (RSFPs) from the family of green fluorescent proteins (GFPs) changes upon mutation which is of direct importance for various high-resolution techniques. Dronpa is one of the most used RSFPs. Its point mutants rsFastLime (Dronpa V157G) and rsKame (Dronpa V157L) exhibit a striking difference in their photoswitching speed. Here the QM/MM on-the-fly string method is used in order to explore the details of the thermal isomerization mechanism. The four principal ways in which isomerization may occur have been scrutinized for each of the three proteins. It has been shown that thermal isomerization occurs via a one-bond-flip…

Protein Conformation alpha-HelicalMutantGreen Fluorescent ProteinsGlycineMolecular Dynamics Simulation010402 general chemistryPhotochemistry01 natural sciencesQM/MMDronpaIsomerismLeucine0103 physical sciencesThermalMaterials ChemistryPoint MutationPhysical and Theoretical Chemistrychemistry.chemical_classification010304 chemical physicsChemistryTemperatureValineChromophoreFluorescence0104 chemical sciencesSurfaces Coatings and FilmsAmino acidKineticsThermodynamicsIsomerizationThe journal of physical chemistry. B
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High affinity agonistic metal ion binding sites within the melanocortin 4 receptor illustrate conformational change of transmembrane region 3.

2003

We created a molecular model of the human melanocortin 4 receptor (MC4R) and introduced a series of His residues into the receptor protein to form metal ion binding sites. We were able to insert micromolar affinity binding sites for zinc between transmembrane region (TM) 2 and TM3 where the metal ion alone was able to activate this peptide binding G-protein-coupled receptor. The exact conformation of the metal ion interactions allowed us to predict the orientation of the helices, and remodeling of the receptor protein indicated that Glu100 and Ile104 in TM2 and Asp122 and Ile125 in TM3 are directed toward a putative area of activation of the receptor. The molecular model suggests that a rot…

Protein ConformationAmino Acid MotifsPeptide bindingPlasma protein bindingTransfectionBiochemistryCell LineReceptors G-Protein-CoupledProtein structureCyclic AMPHumansPoint MutationBinding siteReceptorMolecular BiologyBinding SitesChemistryMembrane ProteinsCell BiologyMelanocortin 4 receptorCytosolic partZincBiochemistryBiophysicsReceptor Melanocortin Type 4MelanocortinProtein BindingThe Journal of biological chemistry
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Combining two mutations of human interleukin-6 that affect gp130 activation results in a potent interleukin-6 receptor antagonist on human myeloma ce…

1995

The pleiotropic cytokine interleukin-6 (IL-6) interacts with the specific ligand binding subunit (IL-6R alpha) of the IL-6 receptor, and this complex associates with the signal-transducing subunit gp130 (IL-6R beta). Human IL-6 acts on human and murine cells, whereas murine IL-6 is only active on murine cells. The construction of a set of chimeric human/murine IL-6 proteins has recently allowed us to define a region (residues 43-55) within the human IL-6 protein, which is important for the interaction with gp130. Subdividing this region shows that mainly residues 50-55 of the human IL-6 are necessary for this interaction. Recently, another human IL-6 double mutant (Q159E and T162P) showed r…

Protein ConformationProtein subunitmedicine.medical_treatmentMutantMolecular Sequence DataBiologyBiochemistryMiceAntigenAntigens CDmedicineCytokine Receptor gp130Tumor Cells CulturedAnimalsHumansPoint MutationInterleukin 6ReceptorMolecular BiologyMembrane GlycoproteinsBase SequenceInterleukin-6Wild typeCell BiologyReceptors InterleukinGlycoprotein 130Molecular biologyReceptors Interleukin-6CytokineOligodeoxyribonucleotidesbiology.proteinMultiple MyelomaThe Journal of biological chemistry
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Identification of Single Amino Acid Residues of Human IL-6 Involved in Receptor Binding and Signal Initiation

1996

The pleiotropic cytokine interleukin-6 (IL-6) has been predicted to be a protein with four antiparallel alpha-helices. On target cells, IL-6 interacts with a specific ligand binding receptor subunit (IL-6R), and this complex associates with the signal-transducing subunit gp130. Human IL-6 acts on human and murine cells, whereas murine IL-6 is only active on murine cells. The construction of chimeric human/murine IL-6 proteins has allowed us to define a region (residues 77-95, region 2c) within the human IL-6 protein that is important for IL-6R binding and a region (residues 50-55, region 2a2) that is important for IL-6R dependent gp130 interaction. Guided by sequence alignment and molecular…

Protein ConformationRecombinant Fusion ProteinsProtein subunitMolecular Sequence DataImmunologySequence alignmentPlasma protein bindingBiologyLigandsMiceStructure-Activity RelationshipProtein structureAntigens CDVirologyCytokine Receptor gp130AnimalsHumansPoint MutationAmino Acid SequenceAmino AcidsReceptorPeptide sequenceMembrane GlycoproteinsInterleukin-6Receptors InterleukinCell BiologyGlycoprotein 130Receptors Interleukin-6BiochemistryMutagenesis Site-DirectedSignal transductionSequence AlignmentProtein BindingSignal TransductionJournal of Interferon & Cytokine Research
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