Search results for "CONSERVE"

showing 10 items of 127 documents

Key features and clinical variability of COG6-CDG

2015

The conserved oligomeric Golgi (COG) complex consists of eight subunits and plays a crucial role in Golgi trafficking and positioning of glycosylation enzymes. Mutations in all COG subunits, except subunit 3, have been detected in patients with congenital disorders of glycosylation (CDG) of variable severity. So far, 3 families with a total of 10 individuals with biallelic COG6 mutations have been described, showing a broad clinical spectrum. Here we present 7 additional patients with 4 novel COG6 mutations. In spite of clinical variability, we delineate the core features of COG6-CDG i.e. liver involvement (9/10), microcephaly (8/10), developmental disability (8/10), recurrent infections (7…

MaleMicrocephalyGlycosylationAdolescentEndocrinology Diabetes and MetabolismProtein subunitHyperkeratosisMolecular Sequence DataGolgi ApparatusCase ReportsResearch SupportBiochemistryConserved oligomeric Golgi complexYoung AdultEndocrinologyCogCongenital Disorders of GlycosylationGeneticsJournal ArticleMedicineHumansNon-U.S. Gov'tChildMolecular BiologyExome sequencingGenetic Association StudiesGeneticsbusiness.industryConserved oligomeric Golgi complexResearch Support Non-U.S. Gov'tHigh-Throughput Nucleotide SequencingInfantCongenital disorder of glycosylationmedicine.diseasePhenotypeAdaptor Proteins Vesicular TransportPhenotypeCOG6MutationMicrocephalyFemaleCDGbusinessCongenital disorder of glycosylation
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Sequence variation in couch potato and its effects on life-history traits in a northern malt fly, Drosophila montana

2011

Abstract Couch potato ( cpo ) has previously been connected to reproductive diapause in several insect species including Drosophila melanogaster , where it has been suggested to provide a link between the insulin signalling pathway and the hormonal control of diapause. In the first part of the study we sequenced nearly 3.6 kb of this gene in a northern Drosophila species ( Drosophila montana ) with a robust photoperiodically determined diapause and found several types of polymorphisms along the sequenced area. We also found variation among five Drosophila virilis group species in the length of the 5th exon of cpo and in the site of the stop codon at the end of this exon. The second part of …

MalePhysiologyAmino Acid MotifsMolecular Sequence DataPopulationDiapauseExonSpecies SpecificityAnimalsDrosophila ProteinsAmino Acid SequenceeducationGeneConserved SequenceSequence DeletionGeneticseducation.field_of_studyPolymorphism GeneticSequence Homology Amino AcidbiologyWild typeNuclear ProteinsExonsSequence Analysis DNAbiology.organism_classificationIntronsStop codonDrosophila virilisPhenotypeInsect ScienceDrosophilaFemaleDrosophila melanogasterSequence AlignmentJournal of Insect Physiology
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Further Delineation of Duplications of ARX Locus Detected in Male Patients with Varying Degrees of Intellectual Disability

2022

The X-linked gene encoding aristaless-related homeobox (ARX) is a bi-functional transcription factor capable of activating or repressing gene transcription, whose mutations have been found in a wide spectrum of neurodevelopmental disorders (NDDs); these include cortical malformations, paediatric epilepsy, intellectual disability (ID) and autism. In addition to point mutations, duplications of the ARX locus have been detected in male patients with ID. These rearrangements include telencephalon ultraconserved enhancers, whose structural alterations can interfere with the control of ARX expression in the developing brain. Here, we review the structural features of 15 gain copy-number variants …

MaleTranscription FactorUltraconserved enhancersIntellectual disability3D structureCatalysisInorganic ChemistryMiceAnimalsHumansPhysical and Theoretical ChemistryChildMolecular BiologySpectroscopyHomeodomain ProteinsAnimalKDM5C-SYN1 axiOrganic ChemistryKDM5C-SYN1 axisGenes HomeoboxHomeodomain ProteinGeneral MedicineXp21.3 duplicationComputer Science ApplicationsUltraconserved enhancerSettore MED/03 - Genetica MedicaMutationARXHumanTranscription Factors
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A new heterozygous mutation (D196N) in the Gs alpha gene as a cause for pseudohypoparathyroidism type IA in a boy who had gallstones

2011

Background Pseudohypoparathyroidism (PHP) is characterized by hypocalcemia and hyperphosphatemia in association with an increased secretion of parathyroid hormone (PTH) due to decreased target tissue responsiveness to PTH. Patients with PHP type Ia are not only resistant to PTH, but also to other hormones that bind to receptors coupled to stimulatory G protein (Gsalpha). PHP Ia and Albright hereditary osteodystrophy (AHO) are caused by a reduced activity of the Gsalpha protein. Heterozygous inactivating Gs alpha (GNAS) gene mutations have been identified in these patients. Methods We studied a boy with PHP Ia. During follow-up the patient developed elevated liver enzyme serum levels and abd…

Malemusculoskeletal diseasesHeterozygotemedicine.medical_specialtyErythrocytesFoot Deformities CongenitalEndocrinology Diabetes and MetabolismMutation MissenseParathyroid hormoneGallstonesGene mutationHyperphosphatemiaEndocrinologyInternal medicineChromograninsGTP-Binding Protein alpha Subunits GsGNAS complex locusHumansMedicineMissense mutationnatural sciencesAmino Acid SequenceChildConserved SequencePseudohypoparathyroidismBase SequenceSequence Homology Amino Acidbiologybusiness.industryDNAExonsGallstonesmedicine.diseasePedigreeCholesterolEndocrinologyAmino Acid SubstitutionPseudohypoparathyroidismPediatrics Perinatology and Child Healthbiology.proteinbusinessHand Deformities CongenitalHormoneJournal of Pediatric Endocrinology and Metabolism
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Evolutionary conservation of the structural, pharmacological, and genomic characteristics of the melanocortin receptor subtypes

2005

We have cloned melanocortin receptors (MCRs) from several species of fish. The MC4R and MC5R subtypes arose early in vertebrate evolution and their primary structure is remarkably conserved. Expression and pharmacological characterization of the MCRs in fish has revealed that they bind and respond to melanocortin peptides with high potency. Detailed characterization of the binding properties of the different subtypes suggests that MCRs in early vertebrates had preference for adrenocorticotropic hormone (ACTH) peptides, while the high sensitivity for the shorter proopiomelanocortin (POMC) products, such as the alpha-, beta-, and gamma-melanocyte-stimulating hormone (MSH), has appeared later,…

Melanocyte-stimulating hormonePhysiologyMolecular Sequence DataBiochemistryConserved sequenceEvolution MolecularCellular and Molecular NeuroscienceEndocrinologyProopiomelanocortinMelanocortin receptorbiology.animalAnimalsHumansAmino Acid SequenceReceptorConserved SequenceG protein-coupled receptorGeneticsbiologyReceptors MelanocortinVertebrateGenomicsStructural Homology Proteinbiology.proteinMelanocortinhormones hormone substitutes and hormone antagonistsPeptides
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Characterization of the length polymorphism in the A + T-rich region of the Drosophila obscura group species

1993

In the twelve Drosophila obscura group species studied, belonging to the affinis, obscura, and pseudoobscura subgroups, the mitochondrial DNA length ranges from 15.8 to 17.2 kb. This length polymorphism is mainly due to insertions/deletions in the variable region of the A + T-rich region. In addition, one species (D. tristis) possess a tandem duplication of a 470-bp fragment that contains the replication origin. The same duplication has occurred at least twice in the Drosophila evolutionary history due to the fact that the repetition is analogous to repetitions found in the four species of the D. melanogaster complex. By comparing the nucleotide sequence of the conserved region in D. ambigu…

Mitochondrial DNAMolecular Sequence DataRestriction MappingDNA RecombinantDNA MitochondrialConserved sequenceSpecies SpecificityMolecular evolutionDrosophilidaeSequence Homology Nucleic AcidGene duplicationGeneticsAnimalsMolecular BiologyEcology Evolution Behavior and SystematicsGeneticsPolymorphism GeneticbiologyBase SequenceAdenineNucleic acid sequencebiology.organism_classificationNucleic Acid ConformationDrosophilaTandem exon duplicationDrosophila obscuraSequence AlignmentPlasmidsThymidine
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Maintenance of a Protein Structure in the Dynamic Evolution of TIMPs over 600 Million Years

2016

Deciphering the events leading to protein evolution represents a challenge, especially for protein families showing complex evolutionary history. Among them, TIMPs represent an ancient eukaryotic protein family widely distributed in the animal kingdom. They are known to control the turnover of the extracellular matrix and are considered to arise early during metazoan evolution, arguably tuning essential features of tissue and epithelial organization. To probe the structure and molecular evolution of TIMPs within metazoans, we report the mining and structural characterization of a large data set of TIMPs over approximately 600 Myr. The TIMPs repertoire was explored starting from the Cnidaria…

Models Molecular0301 basic medicineTIMPsProtein familyProtein Conformationhomology modelingSettore BIO/11 - Biologia MolecolareSequence alignmentBiologytranscriptome wide analysisConserved sequencecnidariansEvolution MolecularCnidaria03 medical and health sciences0302 clinical medicineProtein structurePhylogeneticsMolecular evolutionGeneticsAnimalsTIMPAmino Acid SequenceHomology modelingcnidarianConserved SequencePhylogenyEcology Evolution Behavior and SystematicsGeneticsmyrTissue Inhibitor of Metalloproteinases030104 developmental biologyEvolutionary biologyTIMPs; cnidarians; homology modeling; transcriptome wide analysisSequence Alignment030217 neurology & neurosurgeryResearch Article
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The death-domain fold of the ASC PYRIN domain, presenting a basis for PYRIN/PYRIN recognition.

2003

The PYRIN domain is a conserved sequence motif identified in more than 20 human proteins with putative functions in apoptotic and inflammatory signalling pathways. The three-dimensional structure of the PYRIN domain from human ASC was determined by NMR spectroscopy. The structure determination reveals close structural similarity to death domains, death effector domains, and caspase activation and recruitment domains, although the structural alignment with these other members of the death-domain superfamily differs from previously predicted amino acid sequence alignments. Two highly positively and negatively charged surfaces in the PYRIN domain of ASC result in a strong electrostatic dipole …

Models MolecularProtein FoldingMagnetic Resonance SpectroscopyCARD Signaling Adaptor ProteinsProtein ConformationProtein domainMolecular Sequence DataStatic ElectricityBiologyPyrin domainProtein Structure SecondaryConserved sequenceProtein structureStructural BiologyAnimalsHumansAmino Acid SequenceCloning MolecularMolecular BiologyPeptide sequenceZebrafishDeath domainGeneticsModels StatisticalSequence Homology Amino AcidProteinsPyrinZebrafish ProteinsCell biologyProtein Structure TertiaryCARD Signaling Adaptor ProteinsCytoskeletal ProteinsSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationProtein foldingProtein BindingSignal TransductionJournal of molecular biology
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Folding and stability of the aquaglyceroporin GlpF: Implications for human aqua(glycero)porin diseases

2015

AbstractAquaporins are highly selective polytopic transmembrane channel proteins that facilitate the permeation of water across cellular membranes in a large diversity of organisms. Defects in aquaporin function are associated with common diseases, such as nephrogenic diabetes insipidus, congenital cataract and certain types of cancer. In general, aquaporins have a highly conserved structure; from prokaryotes to humans. The conserved structure, together with structural dynamics and the structural framework for substrate selectivity is discussed. The folding pathway of aquaporins has been a topic of several studies in recent years. These studies revealed that a conserved protein structure ca…

Models MolecularProtein activityAmino Acid MotifsMolecular Sequence DataBiophysicsGene ExpressionPorinsAquaporinDiabetes Insipidus NephrogenicEndoplasmic-reticulum-associated protein degradationAquaporinsBiochemistryCataractProtein Structure SecondaryProtein structureNeoplasmsEscherichia coliGlpFHumansProtein foldingConserved SequenceProtein StabilityChemistryurogenital systemEscherichia coli ProteinsAquaporinWaterCell BiologyTransmembrane proteinCell biologyFolding (chemistry)Membrane proteinBiochemistryMembrane proteinPorinProtein foldingBiochimica et Biophysica Acta (BBA) - Biomembranes
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Structural Characterization of Set1 RNA Recognition Motifs and their Role in Histone H3 Lysine 4 Methylation

2006

Departament de Bioquimica iBiologia Molecular, Universitatde Valencia, C/Dr Moliner 50,46100, Burjassot, SpainThe yeast Set1 histone H3 lysine 4 (H3K4) methyltransferase contains, inaddition to its catalytic SET domain, a conserved RNA recognition motif(RRM1). We present here the crystal structure and the secondary structureassignment in solution of the Set1 RRM1. Although RRM1 has the expectedβαββαβ RRM-fold, it lacks the typical RNA-binding features of thesemodules. RRM1 is not able to bind RNA by itself in vitro, but a constructcombining RRM1 with a newly identified downstream RRM2 specificallybinds RNA. Invivo,H3K4 methylation isnot affectedbyapoint mutation inRRM2 that preserves Set1 s…

Models MolecularRiboswitchHistone H3 Lysine 4Saccharomyces cerevisiae ProteinsRNA-induced transcriptional silencingSurface Properties[SDV]Life Sciences [q-bio]Molecular Sequence DataSaccharomyces cerevisiae[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]BiologyMethylationHistonesStructure-Activity Relationship03 medical and health sciencesStructural BiologyHistone methylation[SDV.BC.BC] Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]Amino Acid SequenceProtein Structure QuaternaryMolecular BiologyConserved Sequence030304 developmental biology0303 health sciencesRNA recognition motifLysine030302 biochemistry & molecular biologyRNARNA FungalHistone-Lysine N-MethyltransferaseNon-coding RNAMolecular biology[SDV] Life Sciences [q-bio]DNA-Binding ProteinsProtein SubunitsBiochemistryHistone methyltransferaseSequence AlignmentProtein BindingTranscription Factors
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