0000000000925940

AUTHOR

Isabelle Zanella-cléon

showing 28 related works from this author

Characterization of MRNP34, a novel methionine-rich nacre protein from the pearl oysters

2012

9 pages; International audience; Nacre of the Pinctada pearl oyster shells is composed of 98% CaCO(3) and 2% organic matrix. The relationship between the organic matrix and the mechanism of nacre formation currently constitutes the main focus regarding the biomineralization process. In this study, we isolated a new nacre matrix protein in P. margaritifera and P. maxima, we called Pmarg- and Pmax-MRNP34 (methionine-rich nacre protein). MRNP34 is a secreted hydrophobic protein, which is remarkably rich in methionine, and which is specifically localised in mineralizing the epithelium cells of the mantle and in the nacre matrix. The structure of this protein is drastically different from those …

0106 biological sciencesBiomineralizationCalcifying mantleMethionine-richMolecular Sequence DataClinical BiochemistryGene ExpressionBiologyMatrix (biology)engineering.materialProteomics010603 evolutionary biology01 natural sciencesBiochemistryLow complexity03 medical and health sciencesPaleontologychemistry.chemical_compoundCalcification PhysiologicMethionineAnimalsAmino Acid SequencePinctada[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsNacre030304 developmental biology0303 health sciencesMethionineViral matrix proteinOrganic ChemistryProteinsEpithelial Cells[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/Biomaterialsbiology.organism_classificationProtein Structure TertiarychemistryBiochemistryengineeringMolluscMatrix proteinPearlBiomineralizationPinctada
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The skeletal proteome of the coral Acropora millepora: the evolution of calcification by co-option and domain shuffling.

2013

14 pages; International audience; In corals, biocalcification is a major function that may be drastically affected by ocean acidification (OA). Scleractinian corals grow by building up aragonitic exoskeletons that provide support and protection for soft tissues. Although this process has been extensively studied, the molecular basis of biocalcification is poorly understood. Notably lacking is a comprehensive catalog of the skeleton-occluded proteins-the skeletal organic matrix proteins (SOMPs) that are thought to regulate the mineral deposition. Using a combination of proteomics and transcriptomics, we report the first survey of such proteins in the staghorn coral Acropora millepora. The or…

0106 biological sciencesProteomeCoralMolecular Sequence Datacalcium carbonate skeletonProteomics010603 evolutionary biology01 natural sciencesMass SpectrometryCalcium CarbonateEvolution Molecular03 medical and health sciencesAcropora milleporaCalcification PhysiologicproteomicsPhylogeneticsAnthozoa[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]evolutionGeneticsAnimals14. Life underwaterAmino Acid Sequencescleractinian[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsMolecular BiologyEcology Evolution Behavior and SystematicsDiscoveriesPhylogeny030304 developmental biologyStaghorn coral0303 health sciencesbiologySequence Homology Amino AcidEcologyMolecular Sequence Annotationbiology.organism_classification[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/BiomaterialsAnthozoabiomineralizationExtracellular MatrixProtein Structure TertiaryEvolutionary biology[ SDV.BBM.GTP ] Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]ProteomeSequence AlignmentFunction (biology)
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The shell-forming proteome of Lottia gigantea reveals both deep conservations and lineage-specific novelties

2013

19 pages; International audience; Proteins that are occluded within the molluscan shell, the so-called shell matrix proteins (SMPs), are an assemblage of biomolecules attractive to study for several reasons. They increase the fracture resistance of the shell by several orders of magnitude, determine the polymorph of CaCO(3) deposited, and regulate crystal nucleation, growth initiation and termination. In addition, they are thought to control the shell microstructures. Understanding how these proteins have evolved is also likely to provide deep insight into events that supported the diversification and expansion of metazoan life during the Cambrian radiation 543 million years ago. Here, we p…

Glycoside Hydrolasesmedicine.medical_treatmentproteomeGastropodaMolecular Sequence DataBiologyBiochemistrymollusc shell matrix proteinsTranscriptomeCyclophilins03 medical and health sciencesPaleontologyLineage specificAnimal ShellsSequence Analysis ProteinTandem Mass Spectrometry[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]evolutionmedicineAnimalsAmino Acid Sequence14. Life underwaterMantle (mollusc)[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsMolecular BiologyCarbonic Anhydrases030304 developmental biologyExtracellular Matrix Proteins0303 health sciencesProteaseEpidermal Growth FactorSequence Homology Amino AcidLimpet030302 biochemistry & molecular biologyCell Biologybiology.organism_classification[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/BiomaterialsbiomineralizationPeptide FragmentsProtein Structure TertiaryPeroxidasesEvolutionary biology[ SDV.BBM.GTP ] Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]ProteomeLottia giganteaElectrophoresis Polyacrylamide GelmantleBiomineralization
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Pmarg-pearlin is a matrix protein involved in nacre framework formation in the pearl oyster Pinctada margaritifera.

2011

11 pages; International audience; The shell of pearl oysters is organized in multiple layers of CaCO(3) crystallites packed together in an organic matrix. Relationships between the components of the organic matrix and mechanisms of nacre formation currently constitute the main focus of research into biomineralization. In this study, we characterized the pearlin protein from the oyster Pinctada margaritifera (Pmarg); this shares structural features with other members of a matrix protein family, N14/N16/pearlin. Pmarg pearlin exhibits calcium- and chitin-binding properties. Pmarg pearlin transcripts are distinctively localized in the mineralizing tissue responsible for nacre formation. More s…

OysterPteriidaeMolecular Sequence Dataengineering.materialBiologyMatrix (biology)010402 general chemistry01 natural sciencesBiochemistry03 medical and health sciencesProtein structureAnimal Shellsbiology.animalAnimalsAmino Acid SequencePinctadaRNA Messenger[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsMolecular Biologyglycoproteins030304 developmental biologyorganic matrix0303 health sciencesExtracellular Matrix ProteinsEcologyAragoniteOrganic ChemistryPinctada margaritiferabiology.organism_classificationbiomineralization[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/Biomaterials0104 chemical sciencesCell biologyprotein structuresengineeringMolecular Medicinepearl oysterPearlBiomineralization
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Additional file 1 of Transcriptome and proteome analysis of Pinctada margaritifera calcifying mantle and shell: focus on biomineralization

2021

Additional file 1:Table S1: Summary of BlastX results of biomineralization-related protein in the EST P. margaritifera mantle database. A catalogue of 82 P. margaritifera mantle transcripts potentially implicated in the biomineralization process was constructed using BlastX (E-value < 10-3) with selected protein sequences identified from mollusks (bivalvia and gastropoda). (DOC 140 KB)

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Nacre evolution: a proteomic approach.

2009

AbstractFrom an evolutionary viewpoint, the molluscan nacre constitutes a fascinating object. This microstructure appeared early, in the Lower Cambrian period, about 530 million years ago, and since then, has been kept unchanged until today. Nacre is restricted to the conchiferan mollusks, where it occurs in t least three main classes, bivalves, gastropods and cephalopods. The aim of the present study is to investigate whether all nacres are built from the same “macromolecular tools”, proteins of the nacre matrix. To this end, we studied three new nacre models, the freshwater bivalve Unio pictorum, the cephalopod Nautilus macromphalus, and the gastropod Haliotis asinina, to which we applied…

0106 biological sciences0303 health sciencesFreshwater bivalveMaterials sciencebiologyHaliotis asininaUnio pictorumMacroevolutionbiology.organism_classification[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/Biomaterials010603 evolutionary biology01 natural sciencesCephalopod[SDV.IB.BIO] Life Sciences [q-bio]/Bioengineering/Biomaterials03 medical and health sciencesEvolutionary biologyBiophysics14. Life underwaterNautilus macromphalus[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsComputingMilieux_MISCELLANEOUS030304 developmental biology
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Nautilin-63, a novel acidic glycoprotein from the shell nacre of Nautilus macromphalus

2011

In molluscs, and more generally in metazoan organisms, the production of a calcified skeleton is a complex molecular process that is regulated by the secretion of an extracellular organic matrix. This matrix constitutes a cohesive and functional macromolecular assemblage, containing mainly proteins, glycoproteins and polysaccharides that, together, control the biomineral formation. These macromolecules interact with the extruded precursor mineral ions, mainly calcium and bicarbonate, to form complex organo-mineral composites of well-defined microstructures. For several reasons related to its remarkable mechanical properties and to its high value in jewelry, nacre is by far the most studied …

chemistry.chemical_classification0303 health sciences02 engineering and technologyCell BiologyPlasma protein bindingMatrix (biology)Biology021001 nanoscience & nanotechnologyBiochemistryAmino acid03 medical and health scienceschemistry.chemical_compoundchemistryBiochemistryChitin0210 nano-technologyGlycoproteinMolecular BiologyPeptide sequence030304 developmental biologyMacromoleculeBiomineralizationFEBS Journal
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A minimal molecular toolkit for mineral deposition? Biochemistry and proteomics of the test matrix of adult specimens of the sea urchin Paracentrotus…

2016

12 pages; International audience; The sea urchin endoskeleton consists of a magnesium-rich biocalcite comprising a small amount of occluded organic macromolecules. This structure constitutes a key-model for understanding the mineral - organics interplay, and for conceiving in vitro bio-inspired materials with tailored properties. Here we employed a deep-clean technique to purify the occluded proteins from adult Paracentrotus lividus tests. We characterized them by 1- and 2D-electrophoreses, ELISA and immunoblotting, and using liquid chromatography coupled with Mass Spectrometry (nanoLC-MS/MS), we identified two metalloenzymes (carbonic anhydrase and MMP), a set of MSP130 family members, sev…

0301 basic medicineBiomineralizationProteomicsSea urchinBiophysicsMatrix (biology)ProteomicsBiochemistryMineralization (biology)Paracentrotus lividusMass Spectrometry03 medical and health sciences0302 clinical medicinebiology.animal[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]Animals[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsSea urchinExtracellular Matrix ProteinsCarbonic anhydrasebiologyChemistryCalcitebiology.organism_classification[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/BiomaterialsIn vitroExtracellular MatrixCalcifying matrixC-type lectin030104 developmental biologyBiochemistry[ SDV.BBM.GTP ] Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]Paracentrotus030217 neurology & neurosurgeryMacromoleculeBiomineralization
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Proteomic analysis of Parietaria judaica pollen and allergen profiling by an immunoproteomic approach

2010

Parietaria judaica pollen is a common cause of airway allergic disease in the Mediterranean area. Proteome analysis of mature Parietaria judaica pollen by two-dimensional gel electrophoresis (2-DE) and mass spectrometry has established the first reference proteome map of this weed. Proteins involved in a variety of cellular functions as well as the occurrence of allergens were detected. By using 2-DE and immunoblotting with sera from Parietaria judaica allergic patients we obtained a more detailed characterization of Parietaria judaica allergen profile so to improve our comprehension of the pathogenesis of pollen-induced allergic reaction.

ProteomicsAllergyProteomeCellular functionsBioengineeringmedicine.disease_causeProteomicsApplied Microbiology and BiotechnologyAllergenTandem Mass SpectrometryPollenotorhinolaryngologic diseasesmedicineHumansElectrophoresis Gel Two-DimensionalPlant Proteinsbiologyfood and beveragesGeneral MedicineAntigens PlantImmunoglobulin Ebiology.organism_classificationmedicine.diseaseParietariaImmunologyProteomeParietaria judaicaPollenParietaria judaica pollenallergens Parietaria judaica immunoproteome pollenBiotechnologyChromatography Liquid
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Additional file of Transcriptome and proteome analysis of Pinctada margaritifera calcifying mantle and shell: focus on biomineralization

2021

Additional file of Transcriptome and proteome analysis of Pinctada margaritifera calcifying mantle and shell: focus on biomineralization

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Identification of Two Carbonic Anhydrases in the Mantle of the European Abalone Haliotis tuberculata (Gastropoda, Haliotidae): Phylogenetic Implicati…

2012

Carbonic anhydrases (CAs) represent a diversified family of metalloenzymes that reversibly catalyze the hydration of carbon dioxide. They are involved in a wide range of functions, among which is the formation of CaCO(3) skeletons in metazoans. In the shell-forming mantle tissues of mollusks, the location of the CA catalytic activity is elusive and gives birth to contradicting views. In the present paper, using the European abalone Haliotis tuberculata, a key model gastropod in biomineralization studies, we identified and characterized two CAs (htCA1 and htCA2) that are specific of the shell-forming mantle tissue. We analyzed them in a phylogenetic context. Combining various approaches, inc…

0106 biological sciencesfood.ingredientAbalone010603 evolutionary biology01 natural sciences03 medical and health sciencesfoodGastropodaGeneticsPinctada fucata14. Life underwaterHaliotisMantle (mollusc)Ecology Evolution Behavior and Systematics030304 developmental biology0303 health sciencesPhylogenetic treebiologyEcologyUnio pictorumbiology.organism_classificationEvolutionary biologyMolecular MedicineAnimal Science and ZoologyDevelopmental BiologyBiomineralizationJournal of Experimental Zoology Part B: Molecular and Developmental Evolution
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Additional file 3 of Transcriptome and proteome analysis of Pinctada margaritifera calcifying mantle and shell: focus on biomineralization

2021

Authors’ original file for figure 2

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Proteomic analysis of the acid-soluble nacre matrix of the bivalve Unio pictorum: detection of novel carbonic anhydrase and putative protease inhibit…

2010

10 pages; International audience; The matrix extracted from mollusc shell nacre is a mixture of proteins and glycoproteins that is thought to play a major role in controlling biomineral synthesis and in increasing its mechanical properties. We investigated the nacreous shell of the freshwater mussel Unio pictorum, to which we applied a proteomics approach adapted to mollusc shell proteins. On one hand, the acid-soluble nacre matrix was fractionated by SDS-PAGE and the five main protein bands (P95, P50, P29, P16, and P12) were digested with trypsin and analyzed by nanoLC-MS/MS followed by de novo sequencing. On the other hand, the acid-soluble nacre matrix was analyzed in a similar manner, w…

Spectrometry Mass Electrospray IonizationProteomeMolecular Sequence DataBioinformaticsProteomicsBiochemistryHomology (biology)03 medical and health sciencesUnioSequence Analysis ProteinCarbonic anhydraseMollusc shellmedicineAnimalsProtease InhibitorsAmino Acid SequenceDatabases Protein[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsMolecular BiologyCarbonic Anhydrases030304 developmental biologychemistry.chemical_classification0303 health sciencesExpressed sequence tagbiology030302 biochemistry & molecular biologyOrganic ChemistryUnio pictorumTrypsinbiology.organism_classification[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/BiomaterialschemistryBiochemistrybiology.proteinMolecular MedicineGlycoproteinChromatography Liquidmedicine.drug
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The shell matrix of the pulmonate land snail Helix aspersa maxima.

2012

12 pages; International audience; In mollusks, the shell mineralization process is controlled by an array of proteins, glycoproteins and polysaccharides that collectively constitute the shell matrix. In spite of numerous researches, the shell protein content of a limited number of model species has been investigated. This paper presents biochemical data on the common edible land snail Helix aspersa maxima, a model organism for ecotoxicological purposes, which has however been poorly investigated from a biomineralization viewpoint. The shell matrix of this species was extracted and analyzed biochemically for functional in vitro inhibition assay, for amino acid and monosaccharides composition…

0106 biological sciencesBiomineralizationPulmonate snailPhysiology01 natural sciencesBiochemistryMineralization (biology)chemistry.chemical_compoundX-Ray DiffractionTandem Mass SpectrometryElectrophoresis Gel Two-DimensionalHaliotisAmino AcidsComputingMilieux_MISCELLANEOUSchemistry.chemical_classification0303 health sciencesEcologyMonosaccharidesLand snailImmunogold labellingImmunohistochemistryAmino acidBiochemistryElectrophoresis Polyacrylamide GelTerrestrial snail ; biomineralization ; shell ; aragonite ; crossed-lamellar ; protein ; immunogold ; gel electrophoresisFrancefood.ingredientBiology010603 evolutionary biologyCalcium Carbonate03 medical and health sciencesfoodSpecies SpecificityAnimal ShellsShellAnimals14. Life underwater[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsMolecular Biology030304 developmental biologyHelix SnailsProteinsCrossed-lamellarbiology.organism_classification[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/BiomaterialsGel electrophoresis[SDV.BA.ZI]Life Sciences [q-bio]/Animal biology/Invertebrate ZoologyCalcium carbonatechemistryMicroscopy Electron ScanningBiomineralizationPinctadaComparative biochemistry and physiology. Part B, Biochemistrymolecular biology
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Transcriptome and proteome analysis of Pinctada margaritifera calcifying mantle and shell: focus on biomineralization

2010

Abstract Background The shell of the pearl-producing bivalve Pinctada margaritifera is composed of an organic cell-free matrix that plays a key role in the dynamic process of biologically-controlled biomineralization. In order to increase genomic resources and identify shell matrix proteins implicated in biomineralization in P. margaritifera, high-throughput Expressed Sequence Tag (EST) pyrosequencing was undertaken on the calcifying mantle, combined with a proteomic analysis of the shell. Results We report the functional analysis of 276 738 sequences, leading to the constitution of an unprecedented catalog of 82 P. margaritifera biomineralization-related mantle protein sequences. Component…

0106 biological sciencesModels MolecularProteomicsProteome[SDV]Life Sciences [q-bio]Proteomics01 natural sciencesContig MappingMantle (mollusc)MargaritiferaIn Situ HybridizationGeneticsExpressed Sequence Tags0303 health sciencesMineralsbiologyPinctada margaritifera[ SDV.BBM.GTP ] Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]ProteomeBiotechnologyResearch Articlelcsh:QH426-470Sequence analysislcsh:BiotechnologyMolecular Sequence Data010603 evolutionary biology03 medical and health sciencesCalcification Physiologiclcsh:TP248.13-248.65[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]GeneticsAnimals[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyAmino Acid SequencePinctadaRNA Messenger[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/Biomaterials030304 developmental biologyBase SequenceSequence Homology Amino AcidGene Expression ProfilingAnimal StructuresMolecular Sequence AnnotationSequence Analysis DNAbiology.organism_classification[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/Biomaterialslcsh:GeneticsGene Expression RegulationEvolutionary biologyPinctadaBiomineralization
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Comparative Proteome Profiling and Functional Analysis of Chronic Myelogenous Leukemia Cell Lines

2007

The aim of the present study was the molecular profiling of different Ph+ chronic myelogenous leukemia (CML) cell lines (LAMA84, K562, and KCL22) by a proteomic approach. By employing two-dimensional gel electrophoresis combined with mass spectrometry analysis, we have identified 191 protein spots corresponding to 142 different proteins. Among these, 63% were cancer-related proteins and 74% were described for the first time in leukemia cells. Multivariate analysis highlighted significant differences in the global proteomic profile of the three CML cell lines. In particular, the detailed analysis of 35 differentially expressed proteins revealed that LAMA84 cells preferentially expressed prot…

Proteomicschronic myelogenous leukemia cell lineBiologyProteomicsBiochemistrySettore BIO/13 - Biologia ApplicataCell MovementCell Line TumorEthidiumLeukemia Myelogenous Chronic BCR-ABL Positivehemic and lymphatic diseases[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologymedicineHumansElectrophoresis Gel Two-DimensionalNeoplasm InvasivenessGel electrophoresisdrug resistanceProteomic ProfileGene Expression Regulation LeukemicGene Expression ProfilingGeneral Chemistrytumor invasionmedicine.diseasePhenotypeMolecular biologyAcridine OrangeGene expression profilingLeukemiaPhenotypeDrug Resistance Neoplasmproteome profilingMultivariate AnalysisDisease ProgressionK562 CellsChronic myelogenous leukemiaK562 cellsJournal of Proteome Research
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Novel molluskan biomineralization proteins retrieved from proteomics: a case study with upsalin.

2012

12 pages; International audience; The formation of the molluskan shell is regulated by an array of extracellular proteins secreted by the calcifying epithelial cells of the mantle. These proteins remain occluded within the recently formed biominerals. To date, many shell proteins have been retrieved, but only a few of them, such as nacreins, have clearly identified functions. In this particular case, by combining molecular biology and biochemical approaches, we performed the molecular characterization of a novel protein that we named Upsalin, associated with the nacreous shell of the freshwater mussel Unio pictorum. The full sequence of the upsalin transcript was obtained by RT-PCR and 5'/3…

ElectrophoresisMolecular Sequence DataBiologyProteomicsBioinformaticsBiochemistryHomology (biology)03 medical and health sciencesproteomicsGene silencingAnimalsAmino Acid Sequence[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsMolecular BiologyPeptide sequence030304 developmental biology0303 health sciencesMineralsBase Sequence030302 biochemistry & molecular biologyOrganic ChemistrymollusksImmunogold labelling[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/BiomaterialsbiomineralizationIn vitroproteinsfreshwater bivalvesBiochemistryMolluscaMicroscopy Electron ScanningMolecular MedicineTarget proteinBiomineralization
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Characterization of crustacyanin-A2 subunit as a component of the organic matrix of gastroliths from the crayfish Cherax quadricarinatus.

2009

AbstractLike the lobsters, some terrestrial crabs and other crayfishes, the Australian red claw crayfish, Cherax quadricarinatus, elaborates in its stomach wall calcium storage structures called gastroliths. For understanding the cyclic elaboration and stabilization of these amorphous calcified structures, we studied the organic matrix (OM) of these paired biomineralizations. After decalcification with acetic acid, we analysed the proteinaceous components of an acetic acid-insoluble fraction by two-dimensional electrophoresis. Nine spots were digested by trpsin and the tryptic peptides were sequenced by nanoLC-nanoESI-MS/MS mass spectrometry. About 100 peptidic sequences were compared to se…

0303 health sciencesMaterials scienceCrustacyanin A2 subunitbiologyProtein subunit030302 biochemistry & molecular biologybiology.organism_classificationCrayfish[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/BiomaterialsHomology (biology)[SDV.IB.BIO] Life Sciences [q-bio]/Bioengineering/Biomaterials03 medical and health sciencesAcetic acidchemistry.chemical_compoundchemistryBiochemistryHomarus gammarusCherax quadricarinatusOrganic matrix[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsComputingMilieux_MISCELLANEOUS030304 developmental biology
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Additional file 5 of Transcriptome and proteome analysis of Pinctada margaritifera calcifying mantle and shell: focus on biomineralization

2021

Authors’ original file for figure 4

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Additional file of Transcriptome and proteome analysis of Pinctada margaritifera calcifying mantle and shell: focus on biomineralization

2021

Additional file of Transcriptome and proteome analysis of Pinctada margaritifera calcifying mantle and shell: focus on biomineralization

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Additional file 4 of Transcriptome and proteome analysis of Pinctada margaritifera calcifying mantle and shell: focus on biomineralization

2021

Authors’ original file for figure 3

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Additional file 2 of Transcriptome and proteome analysis of Pinctada margaritifera calcifying mantle and shell: focus on biomineralization

2021

Authors’ original file for figure 1

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Additional file 5 of Transcriptome and proteome analysis of Pinctada margaritifera calcifying mantle and shell: focus on biomineralization

2021

Authors’ original file for figure 4

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Additional file of Transcriptome and proteome analysis of Pinctada margaritifera calcifying mantle and shell: focus on biomineralization

2021

Additional file of Transcriptome and proteome analysis of Pinctada margaritifera calcifying mantle and shell: focus on biomineralization

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Additional file 4 of Transcriptome and proteome analysis of Pinctada margaritifera calcifying mantle and shell: focus on biomineralization

2021

Authors’ original file for figure 3

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Additional file of Transcriptome and proteome analysis of Pinctada margaritifera calcifying mantle and shell: focus on biomineralization

2021

Additional file of Transcriptome and proteome analysis of Pinctada margaritifera calcifying mantle and shell: focus on biomineralization

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Additional file of Transcriptome and proteome analysis of Pinctada margaritifera calcifying mantle and shell: focus on biomineralization

2021

Additional file of Transcriptome and proteome analysis of Pinctada margaritifera calcifying mantle and shell: focus on biomineralization

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Additional file 2 of Transcriptome and proteome analysis of Pinctada margaritifera calcifying mantle and shell: focus on biomineralization

2021

Authors’ original file for figure 1

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