scholarly article | Q13442814 |
P819 | ADS bibcode | 2016PLoSO..1144284I |
P356 | DOI | 10.1371/JOURNAL.PONE.0144284 |
P932 | PMC publication ID | 4712144 |
P698 | PubMed publication ID | 26742101 |
P5875 | ResearchGate publication ID | 289534867 |
P50 | author | Raúl E Ithuralde | Q56963282 |
Adrian Turjanski | Q50264698 | ||
P2093 | author name string | Adrián Gustavo Turjanski | |
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Intrinsically disordered proteins undergo and assist folding transitions in the proteome. | Q38059042 | ||
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Mechanism of coupled folding and binding of an intrinsically disordered protein | Q40210194 | ||
Long-range modulation of chain motions within the intrinsically disordered transactivation domain of tumor suppressor p53. | Q40652796 | ||
On the use of orientational restraints and symmetry corrections in alchemical free energy calculations | Q42106721 | ||
Successful molecular dynamics simulation of the zinc-bound farnesyltransferase using the cationic dummy atom approach. | Q42206822 | ||
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P275 | copyright license | Creative Commons Attribution 4.0 International | Q20007257 |
P6216 | copyright status | copyrighted | Q50423863 |
P433 | issue | 1 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | phosphorylation | Q242736 |
P304 | page(s) | e0144284 | |
P577 | publication date | 2016-01-07 | |
P1433 | published in | PLOS One | Q564954 |
P1476 | title | Phosphorylation Regulates the Bound Structure of an Intrinsically Disordered Protein: The p53-TAZ2 Case | |
P478 | volume | 11 |
Q38974661 | Biosimilars in rheumatic diseases: structural and functional variability that may impact clinical and regulatory decisions |
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Q42717863 | Intrinsic protein disorder could be overlooked in cocrystallization conditions: An SRCD case study |
Q53176995 | Stimulatory effects of curcumin and quercetin on posttranslational modifications of p53 during lung carcinogenesis. |
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