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Items: 1 to 50 of 101

1.

Functional interplay between protein domains in a supramodular structure involving the postsynaptic density protein PSD-95.

Laursen L, Karlsson E, Gianni S, Jemth P.

J Biol Chem. 2020 Feb 14;295(7):1992-2000. doi: 10.1074/jbc.RA119.011050. Epub 2019 Dec 12.

PMID:
31831623
2.

Erratum to: Affinity versus specificity in coupled binding and folding reactions.

Gianni S, Jemth P.

Protein Eng Des Sel. 2019 Dec 31;32(4):203. doi: 10.1093/protein/gzz038. No abstract available.

PMID:
31587044
3.

Affinity versus specificity in coupled binding and folding reactions.

Gianni S, Jemth P.

Protein Eng Des Sel. 2019 Dec 31;32(8):355-357. doi: 10.1093/protein/gzz020.

PMID:
31397874
4.

Coupled Binding and Helix Formation Monitored by Synchrotron-Radiation Circular Dichroism.

Karlsson E, Andersson E, Jones NC, Hoffmann SV, Jemth P, Kjaergaard M.

Biophys J. 2019 Aug 20;117(4):729-742. doi: 10.1016/j.bpj.2019.07.014. Epub 2019 Jul 19.

PMID:
31378314
5.

Editorial overview: Folding and binding.

Ivarsson Y, Jemth P.

Curr Opin Struct Biol. 2019 Feb;54:139-140. doi: 10.1016/j.sbi.2019.02.006. Epub 2019 Mar 20. No abstract available.

PMID:
30901729
6.

Seeking allosteric networks in PDZ domains.

Gautier C, Laursen L, Jemth P, Gianni S.

Protein Eng Des Sel. 2018 Oct 1;31(10):367-373. doi: 10.1093/protein/gzy033. Review.

7.

A structurally heterogeneous transition state underlies coupled binding and folding of disordered proteins.

Karlsson E, Andersson E, Dogan J, Gianni S, Jemth P, Camilloni C.

J Biol Chem. 2019 Jan 25;294(4):1230-1239. doi: 10.1074/jbc.RA118.005854. Epub 2018 Dec 4.

8.

Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins.

Jemth P, Karlsson E, Vögeli B, Guzovsky B, Andersson E, Hultqvist G, Dogan J, Güntert P, Riek R, Chi CN.

Sci Adv. 2018 Oct 24;4(10):eaau4130. doi: 10.1126/sciadv.aau4130. eCollection 2018 Oct.

9.

Affinity and specificity of motif-based protein-protein interactions.

Ivarsson Y, Jemth P.

Curr Opin Struct Biol. 2019 Feb;54:26-33. doi: 10.1016/j.sbi.2018.09.009. Epub 2018 Oct 24. Review.

PMID:
30368054
10.

Probing Backbone Hydrogen Bonds in Proteins by Amide-to-Ester Mutations.

Sereikaitė V, Jensen TMT, Bartling CRO, Jemth P, Pless SA, Strømgaard K.

Chembiochem. 2018 Oct 18;19(20):2136-2145. doi: 10.1002/cbic.201800350. Epub 2018 Oct 1. Review.

PMID:
30073762
11.

Binding Kinetics of the Intrinsically Disordered p53 Family Transactivation Domains and MDM2.

Åberg E, Karlsson OA, Andersson E, Jemth P.

J Phys Chem B. 2018 Jul 12;122(27):6899-6905. doi: 10.1021/acs.jpcb.8b03876. Epub 2018 Jun 26.

PMID:
29878773
12.

Addressing the role of the α-helical extension in the folding of the third PDZ domain from PSD-95.

Gautier C, Visconti L, Jemth P, Gianni S.

Sci Rep. 2017 Oct 3;7(1):12593. doi: 10.1038/s41598-017-12827-0.

13.

How Fast Is Protein-Ligand Association?

Gianni S, Jemth P.

Trends Biochem Sci. 2017 Nov;42(11):847-849. doi: 10.1016/j.tibs.2017.08.007. Epub 2017 Sep 13.

PMID:
28917971
14.

Evolution of the p53-MDM2 pathway.

Åberg E, Saccoccia F, Grabherr M, Ore WYJ, Jemth P, Hultqvist G.

BMC Evol Biol. 2017 Aug 3;17(1):177. doi: 10.1186/s12862-017-1023-y.

15.

Emergence and evolution of an interaction between intrinsically disordered proteins.

Hultqvist G, Åberg E, Camilloni C, Sundell GN, Andersson E, Dogan J, Chi CN, Vendruscolo M, Jemth P.

Elife. 2017 Apr 11;6. pii: e16059. doi: 10.7554/eLife.16059.

16.

The evolution of Sex-linked barring alleles in chickens involves both regulatory and coding changes in CDKN2A.

Schwochow Thalmann D, Ring H, Sundström E, Cao X, Larsson M, Kerje S, Höglund A, Fogelholm J, Wright D, Jemth P, Hallböök F, Bed'Hom B, Dorshorst B, Tixier-Boichard M, Andersson L.

PLoS Genet. 2017 Apr 7;13(4):e1006665. doi: 10.1371/journal.pgen.1006665. eCollection 2017 Apr.

17.

Understanding the role of phosphorylation in the binding mechanism of a PDZ domain.

Toto A, Mattei A, Jemth P, Gianni S.

Protein Eng Des Sel. 2017 Jan;30(1):1-5. Epub 2016 Oct 19.

PMID:
27760803
18.

Improved affinity at the cost of decreased specificity: a recurring theme in PDZ-peptide interactions.

Karlsson OA, Sundell GN, Andersson E, Ivarsson Y, Jemth P.

Sci Rep. 2016 Oct 3;6:34269. doi: 10.1038/srep34269.

19.

Activation Barrier-Limited Folding and Conformational Sampling of a Dynamic Protein Domain.

Dogan J, Toto A, Andersson E, Gianni S, Jemth P.

Biochemistry. 2016 Sep 20;55(37):5289-95. doi: 10.1021/acs.biochem.6b00573. Epub 2016 Sep 6.

PMID:
27542287
20.

Protein folding: Vexing debates on a fundamental problem.

Gianni S, Jemth P.

Biophys Chem. 2016 May;212:17-21. doi: 10.1016/j.bpc.2016.03.001. Epub 2016 Mar 17. Review.

PMID:
27018826
21.

Ligand binding to the PDZ domains of postsynaptic density protein 95.

Toto A, Pedersen SW, Karlsson OA, Moran GE, Andersson E, Chi CN, Strømgaard K, Gianni S, Jemth P.

Protein Eng Des Sel. 2016 May;29(5):169-75. doi: 10.1093/protein/gzw004. Epub 2016 Mar 2.

PMID:
26941280
22.

Coupled binding and folding of intrinsically disordered proteins: what can we learn from kinetics?

Gianni S, Dogan J, Jemth P.

Curr Opin Struct Biol. 2016 Feb;36:18-24. doi: 10.1016/j.sbi.2015.11.012. Epub 2015 Dec 22. Review.

PMID:
26720267
23.

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
24.

Deconvoluting Protein (Un)folding Structural Ensembles Using X-Ray Scattering, Nuclear Magnetic Resonance Spectroscopy and Molecular Dynamics Simulation.

Nasedkin A, Marcellini M, Religa TL, Freund SM, Menzel A, Fersht AR, Jemth P, van der Spoel D, Davidsson J.

PLoS One. 2015 May 6;10(5):e0125662. doi: 10.1371/journal.pone.0125662. eCollection 2015.

25.

Design of a PDZbody, a bivalent binder of the E6 protein from human papillomavirus.

Karlsson OA, Ramirez J, Öberg D, Malmqvist T, Engström Å, Friberg M, Chi CN, Widersten M, Travé G, Nilsson MT, Jemth P.

Sci Rep. 2015 Mar 23;5:9382. doi: 10.1038/srep09382.

26.

Targeting protein-protein interactions with trimeric ligands: high affinity inhibitors of the MAGUK protein family.

Nissen KB, Haugaard-Kedström LM, Wilbek TS, Nielsen LS, Åberg E, Kristensen AS, Bach A, Jemth P, Strømgaard K.

PLoS One. 2015 Feb 6;10(2):e0117668. doi: 10.1371/journal.pone.0117668. eCollection 2015.

27.

Deciphering the mechanisms of binding induced folding at nearly atomic resolution: The Φ value analysis applied to IDPs.

Gianni S, Dogan J, Jemth P.

Intrinsically Disord Proteins. 2014 Dec 15;2(1):e970900. doi: 10.4161/idp.28624. eCollection 2014.

28.

Nonequilibrium capture rates induce protein accumulation and enhanced adsorption to solid-state nanopores.

Freedman KJ, Haq SR, Fletcher MR, Foley JP, Jemth P, Edel JB, Kim MJ.

ACS Nano. 2014 Dec 23;8(12):12238-49. doi: 10.1021/nn5062645. Epub 2014 Nov 26.

29.

Only kinetics can prove conformational selection.

Dogan J, Jemth P.

Biophys J. 2014 Oct 21;107(8):1997-1998. doi: 10.1016/j.bpj.2014.08.037. No abstract available.

30.

Rigidified clicked dimeric ligands for studying the dynamics of the PDZ1-2 supramodule of PSD-95.

Eildal JN, Bach A, Dogan J, Ye F, Zhang M, Jemth P, Strømgaard K.

Chembiochem. 2015 Jan 2;16(1):64-9. doi: 10.1002/cbic.201402547. Epub 2014 Nov 18.

PMID:
25407949
31.

Conserved nucleation sites reinforce the significance of Phi value analysis in protein-folding studies.

Gianni S, Jemth P.

IUBMB Life. 2014 Jul;66(7):449-52. doi: 10.1002/iub.1287. Epub 2014 Jul 18.

32.

Thermodynamic aspects of cAMP dependent protein kinase catalytic subunit allostery.

Kivi R, Jemth P, Järv J.

Protein J. 2014 Aug;33(4):386-93. doi: 10.1007/s10930-014-9570-1.

PMID:
24985055
33.

The role of backbone hydrogen bonds in the transition state for protein folding of a PDZ domain.

Pedersen SW, Hultqvist G, Strømgaard K, Jemth P.

PLoS One. 2014 Apr 18;9(4):e95619. doi: 10.1371/journal.pone.0095619. eCollection 2014.

34.

Distinguishing induced fit from conformational selection.

Gianni S, Dogan J, Jemth P.

Biophys Chem. 2014 May;189:33-9. doi: 10.1016/j.bpc.2014.03.003. Epub 2014 Apr 1. Review.

PMID:
24747333
35.

Probing backbone hydrogen bonding in PDZ/ligand interactions by protein amide-to-ester mutations.

Pedersen SW, Pedersen SB, Anker L, Hultqvist G, Kristensen AS, Jemth P, Strømgaard K.

Nat Commun. 2014;5:3215. doi: 10.1038/ncomms4215.

PMID:
24477114
36.

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
37.

A frustrated binding interface for intrinsically disordered proteins.

Jemth P, Mu X, Engström Å, Dogan J.

J Biol Chem. 2014 Feb 28;289(9):5528-33. doi: 10.1074/jbc.M113.537068. Epub 2014 Jan 13.

38.

The binding mechanisms of intrinsically disordered proteins.

Dogan J, Gianni S, Jemth P.

Phys Chem Chem Phys. 2014 Apr 14;16(14):6323-31. doi: 10.1039/c3cp54226b. Epub 2013 Dec 6.

PMID:
24317797
39.

Kinetics of acrylodan-labelled cAMP-dependent protein kinase catalytic subunit denaturation.

Kivi R, Loog M, Jemth P, Järv J.

Protein J. 2013 Oct;32(7):519-25. doi: 10.1007/s10930-013-9511-4.

PMID:
24048767
40.

Energetic pathway sampling in a protein interaction domain.

Hultqvist G, Haq SR, Punekar AS, Chi CN, Engström Å, Bach A, Strømgaard K, Selmer M, Gianni S, Jemth P.

Structure. 2013 Jul 2;21(7):1193-1202.

41.

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.

42.

Probing the role of backbone hydrogen bonds in protein-peptide interactions by amide-to-ester mutations.

Eildal JN, Hultqvist G, Balle T, Stuhr-Hansen N, Padrah S, Gianni S, Strømgaard K, Jemth P.

J Am Chem Soc. 2013 Sep 4;135(35):12998-3007. doi: 10.1021/ja402875h. Epub 2013 Jun 7.

43.

Single molecule unfolding and stretching of protein domains inside a solid-state nanopore by electric field.

Freedman KJ, Haq SR, Edel JB, Jemth P, Kim MJ.

Sci Rep. 2013;3:1638. doi: 10.1038/srep01638.

44.

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
45.

Tolerance of protein folding to a circular permutation in a PDZ domain.

Hultqvist G, Punekar AS, Morrone A, Chi CN, Engström A, Selmer M, Gianni S, Jemth P.

PLoS One. 2012;7(11):e50055. doi: 10.1371/journal.pone.0050055. Epub 2012 Nov 21.

46.

Interactions outside the boundaries of the canonical binding groove of a PDZ domain influence ligand binding.

Chi CN, Haq SR, Rinaldo S, Dogan J, Cutruzzolà F, Engström Å, Gianni S, Lundström P, Jemth P.

Biochemistry. 2012 Nov 6;51(44):8971-9. doi: 10.1021/bi300792h. Epub 2012 Oct 23.

PMID:
23046383
47.

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.

48.

Characterization of the endopeptidase activity of tripeptidyl-peptidase II.

Eklund S, Dogan J, Jemth P, Kalbacher H, Tomkinson B.

Biochem Biophys Res Commun. 2012 Aug 3;424(3):503-7. doi: 10.1016/j.bbrc.2012.06.144. Epub 2012 Jul 4.

PMID:
22771804
49.

Ligand binding by PDZ domains.

Chi CN, Bach A, Strømgaard K, Gianni S, Jemth P.

Biofactors. 2012 Sep-Oct;38(5):338-48. doi: 10.1002/biof.1031. Epub 2012 Jun 7. Review.

PMID:
22674855
50.

Folding pathways of proteins with increasing degree of sequence identities but different structure and function.

Giri R, Morrone A, Travaglini-Allocatelli C, Jemth P, Brunori M, Gianni S.

Proc Natl Acad Sci U S A. 2012 Oct 30;109(44):17772-6. doi: 10.1073/pnas.1201794109. Epub 2012 May 31.

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