2013
Paracrine exchanges of molecular signals between alginate-encapsulated pericytes and freely suspended endothelial cells within a 3D protein gel
Andrejecsk JW, Cui J, Chang WG, Devalliere J, Pober JS, Saltzman WM. Paracrine exchanges of molecular signals between alginate-encapsulated pericytes and freely suspended endothelial cells within a 3D protein gel. Biomaterials 2013, 34: 8899-8908. PMID: 23973174, PMCID: PMC3839675, DOI: 10.1016/j.biomaterials.2013.08.008.Peer-Reviewed Original ResearchConceptsHuman umbilical vein endothelial cellsParacrine signalsFunctioning of tissuesProper survivalEndothelial cellsUmbilical vein endothelial cellsMolecular signalsRegulated deliveryVein endothelial cellsVessel-like structuresLiving cellsProtein gelsHepatocyte growth factorTherapeutic proteinsParacrine exchangesGrowth factorMicrovascular pericytesProteinAngiogenic proteinsCellsVascular tissue engineeringHUVEC behaviorTissue constructsPericytesLocal environment
2004
A Dynamic Molecular Link between the Telomere Length Regulator TRF1 and the Chromosome End Protector TRF2
Houghtaling BR, Cuttonaro L, Chang W, Smith S. A Dynamic Molecular Link between the Telomere Length Regulator TRF1 and the Chromosome End Protector TRF2. Current Biology 2004, 14: 1621-1631. PMID: 15380063, DOI: 10.1016/j.cub.2004.08.052.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceBlotting, NorthernCell CycleFluorescent Antibody TechniqueHeLa CellsHumansImmunoprecipitationModels, BiologicalMolecular Sequence DataPlasmidsSequence Analysis, DNAShelterin ComplexTelomereTelomere-Binding ProteinsTelomeric Repeat Binding Protein 1Telomeric Repeat Binding Protein 2Two-Hybrid System TechniquesConceptsTelomerase-mediated telomere elongationTelomere length homeostasisBinding proteins TRF1Telomere length controlLength homeostasisTelomeric chromatinProteins TRF1Chromosome endsTelomere elongationHuman telomeresTankyrase 1TRF1TRF2Negative regulatorMolecular linkMolecular mechanismsCell cycleTelomeresDynamic cross talkTIN2Cross talkLength controlChromatinRegulatorProtein
2003
TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres
Chang W, Dynek JN, Smith S. TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres. Genes & Development 2003, 17: 1328-1333. PMID: 12782650, PMCID: PMC196064, DOI: 10.1101/gad.1077103.Peer-Reviewed Original ResearchConceptsSequential post-translational modificationsAccess of telomeraseDNA-binding proteinsPost-translational modificationsMammalian telomeresTelomeres resultsTranslational modificationsTankyrase 1TRF1Negative regulatorTelomeresADP-ribosylationNovel mechanismUnbound formUbiquitinationTelomere lengthUbiquitinProteasomeTelomeraseRegulatorProteolysisProteinDegradationElongation