2011
Molecular definitions of cell death subroutines: recommendations of the Nomenclature Committee on Cell Death 2012
Galluzzi L, Vitale I, Abrams J, Alnemri E, Baehrecke E, Blagosklonny M, Dawson T, Dawson V, El-Deiry W, Fulda S, Gottlieb E, Green D, Hengartner M, Kepp O, Knight R, Kumar S, Lipton S, Lu X, Madeo F, Malorni W, Mehlen P, Nuñez G, Peter M, Piacentini M, Rubinsztein D, Shi Y, Simon H, Vandenabeele P, White E, Yuan J, Zhivotovsky B, Melino G, Kroemer G. Molecular definitions of cell death subroutines: recommendations of the Nomenclature Committee on Cell Death 2012. Cell Death & Differentiation 2011, 19: 107-120. PMID: 21760595, PMCID: PMC3252826, DOI: 10.1038/cdd.2011.96.Peer-Reviewed Original ResearchConceptsCell death subroutinesCell death modalitiesCell deathDeath modalitiesMitotic catastropheMolecular definitionCell death morphologyAutophagic cell deathUtility of expressionNomenclature CommitteeExtrinsic apoptosisDeath morphologyRegulated necrosisIntrinsic apoptosisGenetic explorationFunctional classificationApoptosisBiochemical featuresVivo settingsSubstantial progressExpressionDeath
2010
Dealing with Misfolded Proteins: Examining the Neuroprotective Role of Molecular Chaperones in Neurodegeneration
Ali YO, Kitay BM, Zhai RG. Dealing with Misfolded Proteins: Examining the Neuroprotective Role of Molecular Chaperones in Neurodegeneration. Molecules 2010, 15: 6859-6887. PMID: 20938400, PMCID: PMC3133442, DOI: 10.3390/molecules15106859.Peer-Reviewed Original ResearchConceptsMolecular chaperonesMisfolded proteinsNormal protein homeostasisRepair of proteinsProtein-protein interactionsHuman neurodegenerative diseasesNeurodegenerative diseasesNascent proteinsProtein homeostasisNetwork of moleculesCellular functionsConformational diseasesProteolytic machineryProtein speciesCellular stressChaperonesClearance of proteinsNormal proteinProteinFunctional classificationSuch diseasesFoldingEnvironmental factorsWide arrayTherapeutic potential
2004
Human disorders of ubiquitination and proteasomal degradation
Jiang YH, Beaudet AL. Human disorders of ubiquitination and proteasomal degradation. Current Opinion In Pediatrics 2004, 16: 419-426. PMID: 15273504, DOI: 10.1097/01.mop.0000133634.79661.cd.Peer-Reviewed Original ResearchMeSH KeywordsAlzheimer DiseaseAngelman SyndromeAnimalsFanconi AnemiaGenetic Diseases, InbornGenetic Predisposition to DiseaseHumansNF-kappa BPolyendocrinopathies, AutoimmuneProteasome Endopeptidase ComplexUbiquitin-Activating EnzymesUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesUbiquitinsvon Hippel-Lindau DiseaseConceptsProteasomal degradationProteasomal subunitsAdditional functional classesUbiquitin E3 ligaseAutosomal recessive juvenile Parkinson's diseaseUbiquitin signalingE3 ligasesUbiquitin pathwayGenetic inborn errorsUbiquitin genesE3 ligaseSubcellular localizationUbiquitinationRelated proteinsMultiple functional defectsRelevant genesHuman disordersCongenital polycythemiaRegulatory signalingFanconi anemiaGenetic classesOvarian cancer susceptibilityFunctional classificationProteolytic degradationUbiquitin
2003
Genome-wide Analyses of Carboxyl-terminal Sequences*
Chung JJ, Yang H, Li M. Genome-wide Analyses of Carboxyl-terminal Sequences*. Molecular & Cellular Proteomics 2003, 2: 173-181. PMID: 12682279, DOI: 10.1074/mcp.m300008-mcp200.Peer-Reviewed Original ResearchConceptsCarboxyl-terminal sequenceBiological functionsYeast open reading framesTerminal sequenceGenome-wide analysisProtein carboxyl terminusCarboxyl-terminal signalUnknown biological functionEndoplasmic reticulum retentionSpecific biological functionsOpen reading frameHDEL sequenceProteome levelSequence motifsEntire proteomeProteome databaseReading frameCarboxyl terminusRecognition signatureBiochemical processesFunctional classificationProteomeSequenceDetermination of proteinProtein
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