Search results for "Functional domain"

showing 3 items of 3 documents

Skeletal organic matrices in molluscs: origin, evolution, diagenesis

2017

8 pages; International audience; The mollusc shell comprises a small amount of organic macromolecules, mostly proteins and polysaccharides, which, all together, constitute the skeletal organic matrix (SOM). In the recent years, the study of the SOM of about two dozens of mollusc species via transcriptomics and/or proteomics has led to the identification of hundreds of shell-associated proteins. This rapidly growing set of data allows several comparisons, shedding light on similarities and differences at the primary structure level and on some peculiar evolutionary mechanisms that may have affected SOM proteins. In addition, it constitutes a prerequisite for investigating the SOM repertoires…

0301 basic medicineProteomicsSubfossilProteinBiologyFunctional domainsProteomicsbiology.organism_classificationFossilizationSequencesTridacnaDiagenesisDiagenesis[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM]03 medical and health sciences030104 developmental biology0302 clinical medicineOrder (biology)Evolutionary biologyMollusc shellShellIdentification (biology)14. Life underwaterMollusc030217 neurology & neurosurgery
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Hsp60 chaperonopathies and chaperonotherapy: targets and agents

2014

Hsp60 (Cpn60) assembles into a tetradecamer that interacts with the co-chaperonin Hsp10 (Cpn10) to assist client polypeptides to fold, but it also has other roles, including participation in pathogenic mechanisms.Hsp60 chaperonopathies are pathological conditions, inherited or acquired, in which the chaperone plays a determinant etiologic-pathogenic role. These diseases justify selection of Hsp60 as a target for developing agents that interfere with its pathogenic effects. We provide information on how to proceed.The information available encourages the development of ways to improve Hsp60 activity (positive chaperonotherapy) when deficient or to block it (negative chaperonotherapy) when pa…

InflammationPharmacologyanimal structuresChaperonin 60biologyProtein ConformationfungiClinical BiochemistryChaperonin 60BioinformaticsAutoimmune Diseasesautoimmunity cancer carboranylphenoxyacetanilide chaperonopathies chaperonotherapy chemical compounds Cpn60 electrophilic compounds epolactaene functional domain GroEL Hsp60 inflammation mizoribine structural domainNeoplasmsChaperone (protein)Expert opinionDrug DiscoveryImmunologybiology.proteinAnimalsHumansMolecular MedicineHSP60Cytokine formationA determinantExpert Opinion on Therapeutic Targets
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Hsp60, a Novel Target for Antitumor Therapy: Structure-Function Features and Prospective Drugs Design

2013

Heat shock protein 60 kDa (Hsp60) is a chaperone classically believed to be involved in assisting the correct folding of other mitochondrial proteins. Hsp60 also plays a role in cytoprotection against cell stressors, displaying for example, antiapoptotic potential. Despite the plethora of studies devoted to the mechanism of Hsp60's function, especially in prokaryotes, fundamental issues still remain unexplored, including the definition of its role in cancer. Key questions still unanswered pertain to the differences in structure-function features that might exist between the well-studied prokaryotic GroEL and the largely unexplored eukaryotic Hsp60 proteins. In this article we discuss these …

animal structuresBinding pocketCellAntineoplastic Agentschemical and pharmacologic phenomenaComputational biologyBiologyBioinformaticsFunctional domaincomplex mixturesChaperoninStructure-Activity RelationshipNeoplasmsHeat shock proteinDrug DiscoverymedicineHumansPharmacologyCompound dockingSettore BIO/16 - Anatomia UmanaCell growthfungiSettore CHIM/06 - Chimica OrganicaChaperonin 60Hsp60Settore CHIM/08 - Chimica FarmaceuticaCytoprotectionGroELmedicine.anatomical_structureSettore CHIM/03 - Chimica Generale E InorganicaCancer treatmentDrug DesignChaperone (protein)biology.proteinHSP60Protein foldingEpolactaeneCurrent Pharmaceutical Design
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