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Items: 1 to 20 of 172


Conserved Helix-Flanking Prolines Modulate Intrinsically Disordered Protein:Target Affinity by Altering the Lifetime of the Bound Complex.

Crabtree MD, Borcherds W, Poosapati A, Shammas SL, Daughdrill GW, Clarke J.

Biochemistry. 2017 May 9;56(18):2379-2384. doi: 10.1021/acs.biochem.7b00179. Epub 2017 Apr 26.


Contribution of proline to the pre-structuring tendency of transient helical secondary structure elements in intrinsically disordered proteins.

Lee C, Kalmar L, Xue B, Tompa P, Daughdrill GW, Uversky VN, Han KH.

Biochim Biophys Acta. 2014 Mar;1840(3):993-1003. doi: 10.1016/j.bbagen.2013.10.042. Epub 2013 Nov 7.


Disorder and residual helicity alter p53-Mdm2 binding affinity and signaling in cells.

Borcherds W, Theillet FX, Katzer A, Finzel A, Mishall KM, Powell AT, Wu H, Manieri W, Dieterich C, Selenko P, Loewer A, Daughdrill GW.

Nat Chem Biol. 2014 Dec;10(12):1000-2. doi: 10.1038/nchembio.1668. Epub 2014 Nov 2.


Structural Basis for the Interaction of a Human Small Heat Shock Protein with the 14-3-3 Universal Signaling Regulator.

Sluchanko NN, Beelen S, Kulikova AA, Weeks SD, Antson AA, Gusev NB, Strelkov SV.

Structure. 2017 Feb 7;25(2):305-316. doi: 10.1016/j.str.2016.12.005. Epub 2017 Jan 12.


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

Ithuralde RE, Turjanski AG.

PLoS One. 2016 Jan 7;11(1):e0144284. doi: 10.1371/journal.pone.0144284. eCollection 2016.


Discovery of short linear motif-mediated interactions through phage display of intrinsically disordered regions of the human proteome.

Davey NE, Seo MH, Yadav VK, Jeon J, Nim S, Krystkowiak I, Blikstad C, Dong D, Markova N, Kim PM, Ivarsson Y.

FEBS J. 2017 Feb;284(3):485-498. doi: 10.1111/febs.13995. Epub 2017 Jan 18.


Alanine and proline content modulate global sensitivity to discrete perturbations in disordered proteins.

Perez RB, Tischer A, Auton M, Whitten ST.

Proteins. 2014 Dec;82(12):3373-84. doi: 10.1002/prot.24692. Epub 2014 Oct 10.


The effect of phosphorylation on the salt-tolerance-related functions of the soybean protein PM18, a member of the group-3 LEA protein family.

Liu Y, Yang M, Cheng H, Sun N, Liu S, Li S, Wang Y, Zheng Y, Uversky VN.

Biochim Biophys Acta Proteins Proteom. 2017 Nov;1865(11 Pt A):1291-1303. doi: 10.1016/j.bbapap.2017.08.020. Epub 2017 Sep 1.


Evolving Catalytic Properties of the MLL Family SET Domain.

Zhang Y, Mittal A, Reid J, Reich S, Gamblin SJ, Wilson JR.

Structure. 2015 Oct 6;23(10):1921-1933. doi: 10.1016/j.str.2015.07.018. Epub 2015 Aug 27.


The Tail That Wags the Dog: How the Disordered C-Terminal Domain Controls the Transcriptional Activities of the p53 Tumor-Suppressor Protein.

Laptenko O, Tong DR, Manfredi J, Prives C.

Trends Biochem Sci. 2016 Dec;41(12):1022-1034. doi: 10.1016/j.tibs.2016.08.011. Epub 2016 Sep 23. Review.


Discovery and characterisation of the automethylation properties of PRDM9.

Koh-Stenta X, Poulsen A, Li R, Wee JL, Kwek PZ, Chew SY, Peng J, Wu L, Guccione E, Joy J, Hill J.

Biochem J. 2017 Mar 7;474(6):971-982. doi: 10.1042/BCJ20161067.


Structured and disordered regions cooperatively mediate DNA-binding autoinhibition of ETS factors ETV1, ETV4 and ETV5.

Currie SL, Lau DKW, Doane JJ, Whitby FG, Okon M, McIntosh LP, Graves BJ.

Nucleic Acids Res. 2017 Mar 17;45(5):2223-2241. doi: 10.1093/nar/gkx068.


The effect of specific proline residues on the kinetic stability of the triosephosphate isomerases of two trypanosomes.

Guzmán-Luna V, Quezada AG, Díaz-Salazar AJ, Cabrera N, Pérez-Montfort R, Costas M.

Proteins. 2017 Apr;85(4):571-579. doi: 10.1002/prot.25231. Epub 2017 Feb 3.


Folding and binding pathways of BH3-only proteins are encoded within their intrinsically disordered sequence, not templated by partner proteins.

Crabtree MD, Mendonça CATF, Bubb QR, Clarke J.

J Biol Chem. 2018 Jun 22;293(25):9718-9723. doi: 10.1074/jbc.RA118.002791. Epub 2018 May 1.


Demonstration of a folding after binding mechanism in the recognition between the measles virus NTAIL and X domains.

Dosnon M, Bonetti D, Morrone A, Erales J, di Silvio E, Longhi S, Gianni S.

ACS Chem Biol. 2015 Mar 20;10(3):795-802. doi: 10.1021/cb5008579. Epub 2014 Dec 22.


A J-modulated protonless NMR experiment characterizes the conformational ensemble of the intrinsically disordered protein WIP.

Rozentur-Shkop E, Goobes G, Chill JH.

J Biomol NMR. 2016 Dec;66(4):243-257. doi: 10.1007/s10858-016-0073-6. Epub 2016 Nov 14.


Mapping the interactions of the p53 transactivation domain with the KIX domain of CBP.

Lee CW, Arai M, Martinez-Yamout MA, Dyson HJ, Wright PE.

Biochemistry. 2009 Mar 17;48(10):2115-24. doi: 10.1021/bi802055v.


Conformational propensities of intrinsically disordered proteins influence the mechanism of binding and folding.

Arai M, Sugase K, Dyson HJ, Wright PE.

Proc Natl Acad Sci U S A. 2015 Aug 4;112(31):9614-9. doi: 10.1073/pnas.1512799112. Epub 2015 Jul 20.


Structural properties of the intrinsically disordered, multiple calcium ion-binding otolith matrix macromolecule-64 (OMM-64).

Poznar M, Hołubowicz R, Wojtas M, Gapiński J, Banachowicz E, Patkowski A, Ożyhar A, Dobryszycki P.

Biochim Biophys Acta Proteins Proteom. 2017 Nov;1865(11 Pt A):1358-1371. doi: 10.1016/j.bbapap.2017.08.019. Epub 2017 Sep 1.


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