Phosphorylation Regulates the Bound Structure of an Intrinsically Disordered Protein: The p53-TAZ2 Case.

scientific article published on 7 January 2016

Phosphorylation Regulates the Bound Structure of an Intrinsically Disordered Protein: The p53-TAZ2 Case. is …
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scholarly articleQ13442814

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P819ADS bibcode2016PLoSO..1144284I
P356DOI10.1371/JOURNAL.PONE.0144284
P932PMC publication ID4712144
P698PubMed publication ID26742101
P5875ResearchGate publication ID289534867

P50authorRaúl E IthuraldeQ56963282
Adrian TurjanskiQ50264698
P2093author name stringAdrián Gustavo Turjanski
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Two distinct motifs within the p53 transactivation domain bind to the Taz2 domain of p300 and are differentially affected by phosphorylationQ33764044
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HTLV-1 HBZ protein deregulates interactions between cellular factors and the KIX domain of p300/CBP.Q35114430
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Deconstructing p53 transcriptional networks in tumor suppressionQ37966330
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Successful molecular dynamics simulation of the zinc-bound farnesyltransferase using the cationic dummy atom approach.Q42206822
Kinetic advantage of intrinsically disordered proteins in coupled folding-binding process: a critical assessment of the "fly-casting" mechanismQ44367549
P275copyright licenseCreative Commons Attribution 4.0 InternationalQ20007257
P6216copyright statuscopyrightedQ50423863
P433issue1
P407language of work or nameEnglishQ1860
P921main subjectphosphorylationQ242736
P304page(s)e0144284
P577publication date2016-01-07
P1433published inPLOS OneQ564954
P1476titlePhosphorylation Regulates the Bound Structure of an Intrinsically Disordered Protein: The p53-TAZ2 Case
P478volume11

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Q90240391Generation of the configurational ensemble of an intrinsically disordered protein from unbiased molecular dynamics simulation
Q42717863Intrinsic protein disorder could be overlooked in cocrystallization conditions: An SRCD case study
Q53176995Stimulatory effects of curcumin and quercetin on posttranslational modifications of p53 during lung carcinogenesis.

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