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Items: 1 to 50 of 199

1.

Intrinsically Disordered Linkers Impart Processivity on Enzymes by Spatial Confinement of Binding Domains.

Szabo B, Horvath T, Schad E, Murvai N, Tantos A, Kalmar L, Chemes LB, Han KH, Tompa P.

Int J Mol Sci. 2019 Apr 29;20(9). pii: E2119. doi: 10.3390/ijms20092119.

2.

Dynamic anticipation by Cdk2/Cyclin A-bound p27 mediates signal integration in cell cycle regulation.

Tsytlonok M, Sanabria H, Wang Y, Felekyan S, Hemmen K, Phillips AH, Yun MK, Waddell MB, Park CG, Vaithiyalingam S, Iconaru L, White SW, Tompa P, Seidel CAM, Kriwacki R.

Nat Commun. 2019 Apr 11;10(1):1676. doi: 10.1038/s41467-019-09446-w.

3.

Spontaneous driving forces give rise to protein-RNA condensates with coexisting phases and complex material properties.

Boeynaems S, Holehouse AS, Weinhardt V, Kovacs D, Van Lindt J, Larabell C, Van Den Bosch L, Das R, Tompa PS, Pappu RV, Gitler AD.

Proc Natl Acad Sci U S A. 2019 Apr 16;116(16):7889-7898. doi: 10.1073/pnas.1821038116. Epub 2019 Mar 29.

4.

The Balancing Act of Intrinsically Disordered Proteins: Enabling Functional Diversity while Minimizing Promiscuity.

Macossay-Castillo M, Marvelli G, Guharoy M, Jain A, Kihara D, Tompa P, Wodak SJ.

J Mol Biol. 2019 Apr 5;431(8):1650-1670. doi: 10.1016/j.jmb.2019.03.008. Epub 2019 Mar 13.

5.

Emergent functions of proteins in non-stoichiometric supramolecular assemblies.

Pancsa R, Schad E, Tantos A, Tompa P.

Biochim Biophys Acta Proteins Proteom. 2019 Feb 28. pii: S1570-9639(19)30043-3. doi: 10.1016/j.bbapap.2019.02.007. [Epub ahead of print] Review.

PMID:
30826453
6.

Calpain Purification Through Calpastatin and Calcium: Strategy and Procedures.

Nguyen HH, Tompa P, Pauwels K.

Methods Mol Biol. 2019;1929:233-244. doi: 10.1007/978-1-4939-9030-6_15.

PMID:
30710277
7.

Misprediction of Structural Disorder in Halophiles.

Pancsa R, Kovacs D, Tompa P.

Molecules. 2019 Jan 29;24(3). pii: E479. doi: 10.3390/molecules24030479.

8.

Does Intrinsic Disorder in Proteins Favor Their Interaction with Lipids?

Deryusheva E, Nemashkalova E, Galloux M, Richard CA, Eléouët JF, Kovacs D, Van Belle K, Tompa P, Uversky V, Permyakov S.

Proteomics. 2019 Mar;19(6):e1800098. doi: 10.1002/pmic.201800098. Epub 2019 Jan 25.

PMID:
30592560
9.

Challenges in the Structural-Functional Characterization of Multidomain, Partially Disordered Proteins CBP and p300: Preparing Native Proteins and Developing Nanobody Tools.

Bekesi A, Abdellaoui S, Holroyd N, Van Delm W, Pardon E, Pauwels J, Gevaert K, Steyaert J, Derveaux S, Borysik A, Tompa P.

Methods Enzymol. 2018;611:607-675. doi: 10.1016/bs.mie.2018.09.032. Epub 2018 Nov 3.

PMID:
30471702
10.

The Melting Diagram of Protein Solutions and Its Thermodynamic Interpretation.

Tompa K, Bokor M, Tompa P.

Int J Mol Sci. 2018 Nov 12;19(11). pii: E3571. doi: 10.3390/ijms19113571.

11.

Co-Evolution of Intrinsically Disordered Proteins with Folded Partners Witnessed by Evolutionary Couplings.

Pancsa R, Zsolyomi F, Tompa P.

Int J Mol Sci. 2018 Oct 25;19(11). pii: E3315. doi: 10.3390/ijms19113315.

12.

Quantification of Intrinsically Disordered Proteins: A Problem Not Fully Appreciated.

Contreras-Martos S, Nguyen HH, Nguyen PN, Hristozova N, Macossay-Castillo M, Kovacs D, Bekesi A, Oemig JS, Maes D, Pauwels K, Tompa P, Lebrun P.

Front Mol Biosci. 2018 Sep 4;5:83. doi: 10.3389/fmolb.2018.00083. eCollection 2018.

13.

Unique Physicochemical Patterns of Residues in Protein-Protein Interfaces.

Lazar T, Guharoy M, Schad E, Tompa P.

J Chem Inf Model. 2018 Oct 22;58(10):2164-2173. doi: 10.1021/acs.jcim.8b00270. Epub 2018 Oct 3.

PMID:
30212197
14.

Disordered Substrates of the 20S Proteasome Link Degradation with Phase Separation.

Guharoy M, Lazar T, Tompa P.

Proteomics. 2018 Nov;18(21-22):e1800276. doi: 10.1002/pmic.201800276. Epub 2018 Aug 20.

PMID:
30070766
15.

Protein Phase Separation: A New Phase in Cell Biology.

Boeynaems S, Alberti S, Fawzi NL, Mittag T, Polymenidou M, Rousseau F, Schymkowitz J, Shorter J, Wolozin B, Van Den Bosch L, Tompa P, Fuxreiter M.

Trends Cell Biol. 2018 Jun;28(6):420-435. doi: 10.1016/j.tcb.2018.02.004. Epub 2018 Mar 27. Review.

16.

Phasing in on the cell cycle.

Boeynaems S, Tompa P, Van Den Bosch L.

Cell Div. 2018 Jan 25;13:1. doi: 10.1186/s13008-018-0034-4. eCollection 2018. Review.

17.

In vivo biotinylated calpastatin improves the affinity purification of human m-calpain.

Nguyen HH, Volkov AN, Vandenbussche G, Tompa P, Pauwels K.

Protein Expr Purif. 2018 May;145:77-84. doi: 10.1016/j.pep.2018.01.002. Epub 2018 Jan 13.

18.

Molecular Motions and Interactions in Aqueous Solutions of Thymosin-β4 , Stabilin C-Terminal Domain (CTD) and Their 1:1 Complex Studied by 1 H NMR Spectroscopy.

Bokor M, Tantos Á, Mészáros A, Jenei B, Haminda R, Tompa P, Tompa K.

Chemphyschem. 2018 Apr 5;19(7):848-856. doi: 10.1002/cphc.201701187. Epub 2018 Feb 16.

PMID:
29274195
19.

Chemical shift assignments of the partially deuterated Fyn SH2-SH3 domain.

Kieken F, Loth K, van Nuland N, Tompa P, Lenaerts T.

Biomol NMR Assign. 2018 Apr;12(1):117-122. doi: 10.1007/s12104-017-9792-1. Epub 2017 Dec 9.

PMID:
29224116
20.

MobiDB 3.0: more annotations for intrinsic disorder, conformational diversity and interactions in proteins.

Piovesan D, Tabaro F, Paladin L, Necci M, Micetic I, Camilloni C, Davey N, Dosztányi Z, Mészáros B, Monzon AM, Parisi G, Schad E, Sormanni P, Tompa P, Vendruscolo M, Vranken WF, Tosatto SCE.

Nucleic Acids Res. 2018 Jan 4;46(D1):D471-D476. doi: 10.1093/nar/gkx1071.

21.

AmyPro: a database of proteins with validated amyloidogenic regions.

Varadi M, De Baets G, Vranken WF, Tompa P, Pancsa R.

Nucleic Acids Res. 2018 Jan 4;46(D1):D387-D392. doi: 10.1093/nar/gkx950.

22.

Fructose-1,6-bisphosphate couples glycolytic flux to activation of Ras.

Peeters K, Van Leemputte F, Fischer B, Bonini BM, Quezada H, Tsytlonok M, Haesen D, Vanthienen W, Bernardes N, Gonzalez-Blas CB, Janssens V, Tompa P, Versées W, Thevelein JM.

Nat Commun. 2017 Oct 13;8(1):922. doi: 10.1038/s41467-017-01019-z.

23.

A comprehensive assessment of long intrinsic protein disorder from the DisProt database.

Necci M, Piovesan D, Dosztányi Z, Tompa P, Tosatto SCE.

Bioinformatics. 2018 Feb 1;34(3):445-452. doi: 10.1093/bioinformatics/btx590.

PMID:
28968848
24.

Linking functions: an additional role for an intrinsically disordered linker domain in the transcriptional coactivator CBP.

Contreras-Martos S, Piai A, Kosol S, Varadi M, Bekesi A, Lebrun P, Volkov AN, Gevaert K, Pierattelli R, Felli IC, Tompa P.

Sci Rep. 2017 Jul 5;7(1):4676. doi: 10.1038/s41598-017-04611-x.

25.

To be disordered or not to be disordered: is that still a question for proteins in the cell?

Pauwels K, Lebrun P, Tompa P.

Cell Mol Life Sci. 2017 Sep;74(17):3185-3204. doi: 10.1007/s00018-017-2561-6. Epub 2017 Jun 13. Review.

PMID:
28612216
26.

Protein Delivery into Plant Cells: Toward In vivo Structural Biology.

Cedeño C, Pauwels K, Tompa P.

Front Plant Sci. 2017 Apr 19;8:519. doi: 10.3389/fpls.2017.00519. eCollection 2017.

27.

Simultaneous quantification of protein order and disorder.

Sormanni P, Piovesan D, Heller GT, Bonomi M, Kukic P, Camilloni C, Fuxreiter M, Dosztanyi Z, Pappu RV, Babu MM, Longhi S, Tompa P, Dunker AK, Uversky VN, Tosatto SC, Vendruscolo M.

Nat Chem Biol. 2017 Mar 22;13(4):339-342. doi: 10.1038/nchembio.2331. No abstract available.

PMID:
28328918
28.

Affinity purification of human m-calpain through an intrinsically disordered inhibitor, calpastatin.

Nguyen HH, Varadi M, Tompa P, Pauwels K.

PLoS One. 2017 Mar 20;12(3):e0174125. doi: 10.1371/journal.pone.0174125. eCollection 2017.

29.

Phase Separation of C9orf72 Dipeptide Repeats Perturbs Stress Granule Dynamics.

Boeynaems S, Bogaert E, Kovacs D, Konijnenberg A, Timmerman E, Volkov A, Guharoy M, De Decker M, Jaspers T, Ryan VH, Janke AM, Baatsen P, Vercruysse T, Kolaitis RM, Daelemans D, Taylor JP, Kedersha N, Anderson P, Impens F, Sobott F, Schymkowitz J, Rousseau F, Fawzi NL, Robberecht W, Van Damme P, Tompa P, Van Den Bosch L.

Mol Cell. 2017 Mar 16;65(6):1044-1055.e5. doi: 10.1016/j.molcel.2017.02.013.

30.

1H, 15N, 13C resonance assignment of plant dehydrin early response to dehydration 10 (ERD10).

Cedeño C, Żerko S, Tompa P, Koźmiński W.

Biomol NMR Assign. 2017 Oct;11(2):127-131. doi: 10.1007/s12104-017-9732-0. Epub 2017 Mar 8.

PMID:
28275980
31.

Hydrogen Mobility and Protein-Water Interactions in Proteins in the Solid State.

Tompa K, Bokor M, Ágner D, Iván D, Kovács D, Verebélyi T, Tompa P.

Chemphyschem. 2017 Mar 17;18(6):677-682. doi: 10.1002/cphc.201601136. Epub 2017 Feb 7.

PMID:
28066974
32.

DisProt 7.0: a major update of the database of disordered proteins.

Piovesan D, Tabaro F, Mičetić I, Necci M, Quaglia F, Oldfield CJ, Aspromonte MC, Davey NE, Davidović R, Dosztányi Z, Elofsson A, Gasparini A, Hatos A, Kajava AV, Kalmar L, Leonardi E, Lazar T, Macedo-Ribeiro S, Macossay-Castillo M, Meszaros A, Minervini G, Murvai N, Pujols J, Roche DB, Salladini E, Schad E, Schramm A, Szabo B, Tantos A, Tonello F, Tsirigos KD, Veljković N, Ventura S, Vranken W, Warholm P, Uversky VN, Dunker AK, Longhi S, Tompa P, Tosatto SC.

Nucleic Acids Res. 2017 Jan 4;45(D1):D1123-D1124. doi: 10.1093/nar/gkw1279. Epub 2016 Dec 13. No abstract available.

33.

DisProt 7.0: a major update of the database of disordered proteins.

Piovesan D, Tabaro F, Mičetić I, Necci M, Quaglia F, Oldfield CJ, Aspromonte MC, Davey NE, Davidović R, Dosztányi Z, Elofsson A, Gasparini A, Hatos A, Kajava AV, Kalmar L, Leonardi E, Lazar T, Macedo-Ribeiro S, Macossay-Castillo M, Meszaros A, Minervini G, Murvai N, Pujols J, Roche DB, Salladini E, Schad E, Schramm A, Szabo B, Tantos A, Tonello F, Tsirigos KD, Veljković N, Ventura S, Vranken W, Warholm P, Uversky VN, Dunker AK, Longhi S, Tompa P, Tosatto SC.

Nucleic Acids Res. 2017 Jan 4;45(D1):D219-D227. doi: 10.1093/nar/gkw1056. Epub 2016 Nov 28. Erratum in: Nucleic Acids Res. 2017 Jan 4;45(D1):D1123-D1124.

34.

Phosphorylation of MAP65-1 by Arabidopsis Aurora Kinases Is Required for Efficient Cell Cycle Progression.

Boruc J, Weimer AK, Stoppin-Mellet V, Mylle E, Kosetsu K, Cedeño C, Jaquinod M, Njo M, De Milde L, Tompa P, Gonzalez N, Inzé D, Beeckman T, Vantard M, Van Damme D.

Plant Physiol. 2017 Jan;173(1):582-599. doi: 10.1104/pp.16.01602. Epub 2016 Nov 22.

35.

Coding Regions of Intrinsic Disorder Accommodate Parallel Functions.

Pancsa R, Tompa P.

Trends Biochem Sci. 2016 Nov;41(11):898-906. doi: 10.1016/j.tibs.2016.08.009. Epub 2016 Sep 16. Review.

PMID:
27647212
36.

Essential functions linked with structural disorder in organisms of minimal genome.

Pancsa R, Tompa P.

Biol Direct. 2016 Sep 8;11:45. doi: 10.1186/s13062-016-0149-y.

37.

A Novel Method for Assessing the Chaperone Activity of Proteins.

Hristozova N, Tompa P, Kovacs D.

PLoS One. 2016 Aug 26;11(8):e0161970. doi: 10.1371/journal.pone.0161970. eCollection 2016.

38.

Computational analysis of translational readthrough proteins in Drosophila and yeast reveals parallels to alternative splicing.

Pancsa R, Macossay-Castillo M, Kosol S, Tompa P.

Sci Rep. 2016 Aug 26;6:32142. doi: 10.1038/srep32142.

39.

Molecular Mechanism of SSR128129E, an Extracellularly Acting, Small-Molecule, Allosteric Inhibitor of FGF Receptor Signaling.

Herbert C, Schieborr U, Saxena K, Juraszek J, De Smet F, Alcouffe C, Bianciotto M, Saladino G, Sibrac D, Kudlinzki D, Sreeramulu S, Brown A, Rigon P, Herault JP, Lassalle G, Blundell TL, Rousseau F, Gils A, Schymkowitz J, Tompa P, Herbert JM, Carmeliet P, Gervasio FL, Schwalbe H, Bono F.

Cancer Cell. 2016 Jul 11;30(1):176-178. doi: 10.1016/j.ccell.2016.06.015. Epub 2016 Jul 11. No abstract available.

40.

Editorial: Function and Flexibility: Friend or Foe?

Pauwels K, Tompa P.

Front Mol Biosci. 2016 Jul 7;3:31. doi: 10.3389/fmolb.2016.00031. eCollection 2016. No abstract available.

41.

Wide-line NMR and DSC studies on intrinsically disordered p53 transactivation domain and its helically pre-structured segment.

Tompa P, Han KH, Bokor M, Kamasa P, Tantos Á, Fritz B, Kim DH, Lee C, Verebélyi T, Tompa K.

BMB Rep. 2016 Sep;49(9):497-501.

42.

Numerous proteins with unique characteristics are degraded by the 26S proteasome following monoubiquitination.

Braten O, Livneh I, Ziv T, Admon A, Kehat I, Caspi LH, Gonen H, Bercovich B, Godzik A, Jahandideh S, Jaroszewski L, Sommer T, Kwon YT, Guharoy M, Tompa P, Ciechanover A.

Proc Natl Acad Sci U S A. 2016 Aug 9;113(32):E4639-47. doi: 10.1073/pnas.1608644113. Epub 2016 Jul 6.

43.

Intrinsic protein disorder in histone lysine methylation.

Lazar T, Schad E, Szabo B, Horvath T, Meszaros A, Tompa P, Tantos A.

Biol Direct. 2016 Jun 30;11:30. doi: 10.1186/s13062-016-0129-2.

44.

The principle of conformational signaling.

Tompa P.

Chem Soc Rev. 2016 Jul 25;45(15):4252-84. doi: 10.1039/c6cs00011h. Review.

PMID:
27242242
45.

Three reasons protein disorder analysis makes more sense in the light of collagen.

Smithers B, Oates ME, Tompa P, Gough J.

Protein Sci. 2016 May;25(5):1030-6. doi: 10.1002/pro.2913. Epub 2016 Apr 19.

46.

Design Principles Involving Protein Disorder Facilitate Specific Substrate Selection and Degradation by the Ubiquitin-Proteasome System.

Guharoy M, Bhowmick P, Tompa P.

J Biol Chem. 2016 Mar 25;291(13):6723-31. doi: 10.1074/jbc.R115.692665. Epub 2016 Feb 5. Review.

47.

Just a Flexible Linker? The Structural and Dynamic Properties of CBP-ID4 Revealed by NMR Spectroscopy.

Piai A, Calçada EO, Tarenzi T, Grande AD, Varadi M, Tompa P, Felli IC, Pierattelli R.

Biophys J. 2016 Jan 19;110(2):372-381. doi: 10.1016/j.bpj.2015.11.3516.

48.

Tripartite degrons confer diversity and specificity on regulated protein degradation in the ubiquitin-proteasome system.

Guharoy M, Bhowmick P, Sallam M, Tompa P.

Nat Commun. 2016 Jan 6;7:10239. doi: 10.1038/ncomms10239.

49.

Start2Fold: a database of hydrogen/deuterium exchange data on protein folding and stability.

Pancsa R, Varadi M, Tompa P, Vranken WF.

Nucleic Acids Res. 2016 Jan 4;44(D1):D429-34. doi: 10.1093/nar/gkv1185. Epub 2015 Nov 17.

50.

Redefining the BH3 Death Domain as a 'Short Linear Motif'.

Aouacheria A, Combet C, Tompa P, Hardwick JM.

Trends Biochem Sci. 2015 Dec;40(12):736-748. doi: 10.1016/j.tibs.2015.09.007. Epub 2015 Nov 3. Review.

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