0000000000373061

AUTHOR

Rosa Aligué

showing 4 related works from this author

The structural plasticity of the C terminus of p21Cip1 is a determinant for target protein recognition.

2003

The cyclin-dependent kinase inhibitory protein p21(Cip1) might play multiple roles in cell-cycle regulation through interaction of its C-terminal domain with a defined set of cellular proteins such as proliferating cell nuclear antigen (PCNA), calmodulin (CaM), and the oncoprotein SET. p21(Cip1) could be described as an intrinsically unstructured protein in solution although the C-terminal domain adopts a well-defined extended conformation when bound to PCNA. However, the molecular mechanism of the interaction with CaM and the oncoprotein SET is not well understood, partly because of the lack of structural information. In this work, a peptide derived from the C-terminal domain of p21(Cip1) …

Cyclin-Dependent Kinase Inhibitor p21Models MolecularMagnetic Resonance SpectroscopyCalmodulinChromosomal Proteins Non-HistoneProtein ConformationPeptideBiologyLigandsBiochemistryBinding CompetitiveDomain (software engineering)Molecular recognitionCalmodulinCyclinsProliferating Cell Nuclear AntigenEscherichia coliHumansHistone ChaperonesMolecular Biologychemistry.chemical_classificationC-terminusCircular DichroismOrganic ChemistryCell CycleProteinsPeptide FragmentsCell biologyDNA-Binding ProteinschemistryBiochemistrybiology.proteinMolecular MedicineTarget proteinAlpha helixBinding domainTranscription FactorsChembiochem : a European journal of chemical biology
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p27Kip1 regulates alpha-synuclein expression

2018

Alpha-synuclein (α-SYN) is the main component of anomalous protein aggregates (Lewy bodies) that play a crucial role in several neurodegenerative diseases (synucleinopathies) like Parkinson’s disease and multiple system atrophy. However, the mechanisms involved in its transcriptional regulation are poorly understood. We investigated here the role of the cyclin-dependent kinase (Cdk) inhibitor and transcriptional regulator p27Kip1 (p27) in the regulation of α-SYN expression. We observed that selective deletion of p27 by CRISPR/Cas9 technology in neural cells resulted in increased levels of α-SYN. Knock-down of the member of the same family p21Cip1 (p21) also led to increased α-SYN levels, in…

0301 basic medicinep27Kip1[SDV]Life Sciences [q-bio]03 medical and health scienceschemistry.chemical_compound0302 clinical medicineCyclin-dependent kinaseTranscriptional regulationalpha synucleinAlpha synucleinPsychological repressionE2F4Alpha-synucleinSynucleinopathiesbiologyPromoterEnzyme inhibitorsMolecular biologyExpressió gènica3. Good healthnervous system diseases030104 developmental biologyOncologychemistryInhibidors enzimàticsnervous systemE2F4biology.proteinGene expressionTranscription Factor E2F4transcriptionp21Cip1Transcription030217 neurology & neurosurgeryResearch Paper
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Novel, potent calmodulin antagonists derived from an all-dhexapeptide combinatorial library that inhibitin vivocell proliferation: activity and struc…

2000

: Calmodulin is known to bind to various amphipathic helical peptide sequences, and the calmodulin–peptide binding surface has been shown to be remarkably tolerant sterically. d-Amino acid peptides, therefore, represent potential non-hydrolysable intracellular antagonists of calmodulin. In the present study, synthetic combinatorial libraries have been used to develop novel d-amino acid hexapeptide antagonists to calmodulin-regulated phosphodiesterase activity. Five hexapeptides were identified from a library containing over 52 million sequences. These peptides inhibited cell proliferation both in cell culture using normal rat kidney cells and by injection via the femoral vein following part…

chemistry.chemical_classificationCircular dichroismCalmodulinbiologyCell growthChemistryPeptideNuclear magnetic resonance spectroscopyBiochemistryEndocrinologyBiochemistryIn vivoAmphiphilebiology.proteinIntracellularThe Journal of Peptide Research
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Role of p27Kip1 as a transcriptional regulator

2018

The protein p27Kip1 is a member of the Cip/Kip family of cyclin-dependent kinase (Cdk) inhibitors. It interacts with both the catalytic and the regulatory subunit (cyclin) and introduces a region into the catalytic cleave of the Cdk inducing its inactivation. Its inhibitory capacity can be modulated by specific tyrosine phosphorylations. p27Kip1 also behaves as a transcriptional regulator. It associates with specific chromatin domains through different transcription factors. ChIP on chip, ChIP-seq and expression microarray analysis allowed the identification of the transcriptional programs regulated by p27Kip1. Thus, important cellular functions as cell division cycle, respiration, RNA proc…

0301 basic medicinep27Kip1Review03 medical and health sciencesTranscriptional regulationCyclin-dependent kinaseTranscription (biology)Gene expressionTranscriptional regulationcancertranscriptional regulationNeurodegenerationCàncerTranscription factorE2F4CancerbiologyChemistryMalalties neurodegenerativesneurodegenerationNeurodegenerative DiseasesChIP-on-chipExpressió gènicaCell biologyChromatin030104 developmental biologyOncologybiology.proteinGene expressionOncotarget
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