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Items: 1 to 20 of 414

1.

Synergistic folding of two intrinsically disordered proteins: searching for conformational selection.

Ganguly D, Zhang W, Chen J.

Mol Biosyst. 2012 Jan;8(1):198-209. doi: 10.1039/c1mb05156c. Epub 2011 Jul 18.

PMID:
21766125
2.

Residual structures, conformational fluctuations, and electrostatic interactions in the synergistic folding of two intrinsically disordered proteins.

Zhang W, Ganguly D, Chen J.

PLoS Comput Biol. 2012 Jan;8(1):e1002353. doi: 10.1371/journal.pcbi.1002353. Epub 2012 Jan 12.

3.

Topology-based modeling of intrinsically disordered proteins: balancing intrinsic folding and intermolecular interactions.

Ganguly D, Chen J.

Proteins. 2011 Apr;79(4):1251-66. doi: 10.1002/prot.22960. Epub 2011 Jan 25.

PMID:
21268115
4.

A folded excited state of ligand-free nuclear coactivator binding domain (NCBD) underlies plasticity in ligand recognition.

Kjaergaard M, Andersen L, Nielsen LD, Teilum K.

Biochemistry. 2013 Mar 12;52(10):1686-93. doi: 10.1021/bi4001062. Epub 2013 Mar 1.

PMID:
23373423
5.

Atomistic details of the disordered states of KID and pKID. Implications in coupled binding and folding.

Ganguly D, Chen J.

J Am Chem Soc. 2009 Apr 15;131(14):5214-23. doi: 10.1021/ja808999m.

PMID:
19278259
6.

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.

7.

Reconciling binding mechanisms of intrinsically disordered proteins.

Espinoza-Fonseca LM.

Biochem Biophys Res Commun. 2009 May 8;382(3):479-82. doi: 10.1016/j.bbrc.2009.02.151. Epub 2009 Mar 3. Review.

PMID:
19265676
8.

Mapping unstructured regions and synergistic folding in intrinsically disordered proteins with amide H/D exchange mass spectrometry.

Keppel TR, Howard BA, Weis DD.

Biochemistry. 2011 Oct 11;50(40):8722-32. doi: 10.1021/bi200875p. Epub 2011 Sep 19. Erratum in: Biochemistry. 2012 Oct 2;51(39):7812.

PMID:
21894929
9.

Single-molecule studies of intrinsically disordered proteins using solid-state nanopores.

Japrung D, Dogan J, Freedman KJ, Nadzeyka A, Bauerdick S, Albrecht T, Kim MJ, Jemth P, Edel JB.

Anal Chem. 2013 Feb 19;85(4):2449-56. doi: 10.1021/ac3035025. Epub 2013 Feb 6.

PMID:
23327569
10.

Helical propensity in an intrinsically disordered protein accelerates ligand binding.

Iešmantavičius V, Dogan J, Jemth P, Teilum K, Kjaergaard M.

Angew Chem Int Ed Engl. 2014 Feb 3;53(6):1548-51. doi: 10.1002/anie.201307712. Epub 2014 Jan 21.

PMID:
24449148
11.

Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP.

Kjaergaard M, Teilum K, Poulsen FM.

Proc Natl Acad Sci U S A. 2010 Jul 13;107(28):12535-40. doi: 10.1073/pnas.1001693107. Epub 2010 Jun 24.

12.
13.

Folding propensity of intrinsically disordered proteins by osmotic stress.

Mansouri AL, Grese LN, Rowe EL, Pino JC, Chennubhotla SC, Ramanathan A, O'Neill HM, Berthelier V, Stanley CB.

Mol Biosyst. 2016 Nov 15;12(12):3695-3701.

14.

Mechanism of coupled folding and binding of an intrinsically disordered protein.

Sugase K, Dyson HJ, Wright PE.

Nature. 2007 Jun 21;447(7147):1021-5. Epub 2007 May 23.

PMID:
17522630
15.
16.

Binding Rate Constants Reveal Distinct Features of Disordered Protein Domains.

Dogan J, Jonasson J, Andersson E, Jemth P.

Biochemistry. 2015 Aug 4;54(30):4741-50. doi: 10.1021/acs.biochem.5b00520. Epub 2015 Jul 20.

PMID:
26153298
17.

Backbone conformational preferences of an intrinsically disordered protein in solution.

Espinoza-Fonseca LM, Ilizaliturri-Flores I, Correa-Basurto J.

Mol Biosyst. 2012 Jun;8(6):1798-805. doi: 10.1039/c2mb00004k. Epub 2012 Apr 13.

PMID:
22506277
18.

Fast association and slow transitions in the interaction between two intrinsically disordered protein domains.

Dogan J, Schmidt T, Mu X, Engström Å, Jemth P.

J Biol Chem. 2012 Oct 5;287(41):34316-24. doi: 10.1074/jbc.M112.399436. Epub 2012 Aug 22.

19.

The transition state structure for coupled binding and folding of disordered protein domains.

Dogan J, Mu X, Engström Å, Jemth P.

Sci Rep. 2013;3:2076. doi: 10.1038/srep02076.

20.

Electrostatically accelerated encounter and folding for facile recognition of intrinsically disordered proteins.

Ganguly D, Zhang W, Chen J.

PLoS Comput Biol. 2013;9(11):e1003363. doi: 10.1371/journal.pcbi.1003363. Epub 2013 Nov 21.

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