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Aggregation Propensity of the Human Proteome 英文参考文献
AggregationPropensityoftheHumanProteome
ElodieMonsellier1.,MatteoRamazzotti1.,Niccolo` Taddei1,FabrizioChiti1,2*
1DipartimentodiScienzeBiochimiche,Universita`deglistudidiFirenze,Florence,Italy,2Consorziointeruniversitrio‘‘IstitutoNazionaleBiostruttureeBiosistemi’’(I.N.B.B.),
Rome,Italy
Abstract
Formationofamyloid-likefibrilsisinvolvedinnumeroushumanproteindepositiondiseases,butisalsoanintrinsicproperty
of polypeptide chains in general. Progress achieved recently now allows the aggregation propensity of proteins to be
analyzedoverlargescales.Inthisworkweusedapreviouslydevelopedpredictivealgorithmtoanalyzethepropensityof
the34,180proteinsequencesofthehumanproteometoformamyloid-likefibrils. Weshowthatlongproteins have,on
average,lessintenseaggregationpeaksthanshortones.Humanproteinsinvolvedinproteindepositiondiseasesdonot
differextensivelyfromtherestoftheproteome,furtherdemonstratingthegeneralityofproteinaggregation.Wewerealso
abletoreproducesomeoftheresultsobtainedwithotheralgorithms,demonstratingthattheydonotdependonthetype
ofcomputationaltoolemployed.Forexample,proteinswithdifferentsubcellularlocalizationswerefoundtohavedifferent
aggregation propensities, in relation to the various efficiencies of quality control mechanisms. Membrane proteins,
intrinsicallydisorderedproteins,andfoldedproteinswereconfirmedtohaveverydifferentaggregationpropensities,asa
consequence of their different structures and cellular microenvironments. In addition, gatekeeper residues at strategic
positions of the sequences were found to protect human proteins from aggregation. The results of these comparative
analyseshighlighttheexistenceofintimatelinksbetweenthepropensityofproteinstoformaggregateswithb-structure
andtheirbiology.Inparticular,theyemphasizetheexistenceofanegativeselectionpressurethatfinelymodulatesprotein
sequencesinordertoadapttheiraggregationpropensitytotheirbiologicalcontext.
Citation:MonsellierE,RamazzottiM,TaddeiN,ChitiF(2008)AggregationPropensityoftheHumanProteo
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