Search results for "NIMA-Interacting Peptidylprolyl Isomerase"

showing 4 items of 4 documents

Fine-tuning the extent and dynamics of binding cleft opening as a potential general regulatory mechanism in parvulin-type peptidyl prolyl isomerases

2017

AbstractParvulins or rotamases form a distinct group within peptidyl prolyl cis-trans isomerases. Their exact mode of action as well as the role of conserved residues in the family are still not unambiguously resolved. Using backbone S2 order parameters and NOEs as restraints, we have generated dynamic structural ensembles of three distinct parvulins, SaPrsA, TbPin1 and CsPinA. The resulting ensembles are in good agreement with the experimental data but reveal important differences between the three enzymes. The largest difference can be attributed to the extent of the opening of the substrate binding cleft, along which motional mode the three molecules occupy distinct regions. Comparison w…

0301 basic medicineFine-tuningentsyymitStaphylococcus aureusparvulinsProtein ConformationParvulinenzymesTrypanosoma brucei bruceibinding cleftIsomeraseisomerasesArticleWW domain03 medical and health sciencesHumansAmino Acid SequenceMode of actionta116Multidisciplinary030102 biochemistry & molecular biologybiologyChemistryDynamics (mechanics)ta1182Peptidylprolyl IsomeraseArchaeaNIMA-Interacting Peptidylprolyl Isomerase030104 developmental biologyOrder (biology)PIN1Biophysicsbiology.proteinProtein BindingScientific Reports
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Molecular evidence for the inverse comorbidity between central nervous system disorders and cancers detected by transcriptomic meta-analyses.

2014

There is epidemiological evidence that patients with certain Central Nervous System (CNS) disorders have a lower than expected probability of developing some types of Cancer. We tested here the hypothesis that this inverse comorbidity is driven by molecular processes common to CNS disorders and Cancers, and that are deregulated in opposite directions. We conducted transcriptomic meta-analyses of three CNS disorders (Alzheimer's disease, Parkinson's disease and Schizophrenia) and three Cancer types (Lung, Prostate, Colorectal) previously described with inverse comorbidities. A significant overlap was observed between the genes upregulated in CNS disorders and downregulated in Cancers, as wel…

Central Nervous SystemCancer ResearchGene ExpressionDiseaseComorbidityBioinformaticsProstate cancer0302 clinical medicineNeoplasmsGenetics (clinical)0303 health sciencesWnt signaling pathwayParkinson DiseaseAlzheimer's diseasePeptidylprolyl Isomerase[SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM]3. Good health[SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]Alzheimer's diseaseResearch ArticleSignal Transductionlcsh:QH426-470[SDV.CAN]Life Sciences [q-bio]/CancerProtein degradationBiology03 medical and health sciencesAlzheimer Disease[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]medicineGeneticsCancer GeneticsHumansGene NetworksMolecular BiologyBiologyEcology Evolution Behavior and Systematics030304 developmental biologyPeptidylprolyl isomeraseGene Expression ProfilingCancerComputational Biologymedicine.diseaseColorectal cancerComorbidityMalariaNIMA-Interacting Peptidylprolyl IsomeraseMeta-analysislcsh:GeneticsGene Expression RegulationImmunologySchizophrenia[SDV.SPEE]Life Sciences [q-bio]/Santé publique et épidémiologie030217 neurology & neurosurgery
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Theileria parasites secrete a prolyl isomerase to maintain host leukocyte transformation

2015

Infectious agents develop intricate mechanisms to interact with host cell pathways and hijack their genetic and epigenetic machinery to change host cell phenotypic states. Among the Apicomplexa phylum of obligate intracellular parasites, which cause veterinary and human diseases, Theileria is the only genus that transforms its mammalian host cells. Theileria infection of bovine leukocytes induces proliferative and invasive phenotypes associated with activated signalling pathways, notably JNK and AP-1 (ref. 2). The transformed phenotypes are reversed by treatment with the theilericidal drug buparvaquone. We used comparative genomics to identify a homologue of the peptidyl-prolyl isomerase PI…

Proto-Oncogene Proteins c-jun[SDV]Life Sciences [q-bio]Drug ResistanceparasitesBiologyArticleCell LineHost-Parasite InteractionsmiR-155TheileriaTheileriaLeukocytesProlyl isomeraseAnimalsHumanscancerSecretionNIMA-Interacting Peptidylprolyl IsomeraseZebrafishComputingMilieux_MISCELLANEOUSPeptidylprolyl isomeraseSKP Cullin F-Box Protein LigasesMultidisciplinaryProtein StabilityGeneral CommentaryIntracellular parasiteUbiquitinationPeptidylprolyl Isomerasebiology.organism_classificationXenograft Model Antitumor AssaysMolecular biology3. Good healthCell biologyUbiquitin ligaseNIMA-Interacting Peptidylprolyl IsomeraseTranscription Factor AP-1Cell Transformation NeoplasticSchistosoma haematobiumPIN1biology.proteinMedicineCattleNaphthoquinonesSignal Transduction
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The prolyl-isomerase PIN1 is essential for nuclear Lamin-B structure and function and protects heterochromatin under mechanical stress.

2021

Summary: Chromatin organization plays a crucial role in tissue homeostasis. Heterochromatin relaxation and consequent unscheduled mobilization of transposable elements (TEs) are emerging as key contributors of aging and aging-related pathologies, including Alzheimer’s disease (AD) and cancer. However, the mechanisms governing heterochromatin maintenance or its relaxation in pathological conditions remain poorly understood. Here we show that PIN1, the only phosphorylation-specific cis/trans prolyl isomerase, whose loss is associated with premature aging and AD, is essential to preserve heterochromatin. We demonstrate that this PIN1 function is conserved from Drosophila to humans and prevents…

transposonsNeocortexMiceHeterochromatinProlyl isomeraseDrosophila ProteinsBiology (General)PhosphorylationRNA Small InterferingTissue homeostasisCells CulturedSettore ING-INF/05 - Sistemi Di Elaborazione Delle InformazioniNeuronsLamin Type BChemistryHP1phosphorylationneurodegenerationnuclear envelopePeptidylprolyl IsomeraseCell biologyDrosophila heterochromatin HP1 Lamin mechanical stress neurodegeneration nuclear envelope phosphorylation PIN1 transposonsNuclear laminaDrosophilaRNA InterferencePremature agingQH301-705.5HeterochromatinNuclear EnvelopeDrosophila; heterochromatin; HP1; Lamin; mechanical stress; neurodegeneration; nuclear envelope; phosphorylation; PIN1; transposonsSettore BIO/11 - Biologia MolecolareSettore MED/08 - Anatomia PatologicaGeneral Biochemistry Genetics and Molecular BiologyPIN1Alzheimer DiseaseSettore MED/05 - Patologia ClinicaAnimalsHumansHeterochromatin maintenancemechanical stressheterochromatinmechanical streMice Inbred C57BLNIMA-Interacting Peptidylprolyl IsomeraseChromobox Protein Homolog 5DNA Transposable ElementsHeterochromatin protein 1Stress MechanicalLaminLaminCell reports
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