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Items: 31

1.
2.

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.

3.

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
4.

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
5.

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.

6.

Multiple fuzzy interactions in the moonlighting function of thymosin-β4.

Tantos A, Szabo B, Lang A, Varga Z, Tsylonok M, Bokor M, Verebelyi T, Kamasa P, Tompa K, Perczel A, Buday L, Lee SH, Choo Y, Han KH, Tompa P.

Intrinsically Disord Proteins. 2013 Sep 11;1(1):e26204. doi: 10.4161/idp.26204. eCollection 2013 Jan-Dec.

7.

Hydrogen skeleton, mobility and protein architecture.

Tompa K, Bokor M, Han KH, Tompa P.

Intrinsically Disord Proteins. 2013 Apr 1;1(1):e25767. doi: 10.4161/idp.25767. eCollection 2013 Jan-Dec.

8.

Structural disorder and local order of hNopp140.

Tantos A, Szrnka K, Szabo B, Bokor M, Kamasa P, Matus P, Bekesi A, Tompa K, Han KH, Tompa P.

Biochim Biophys Acta. 2013 Jan;1834(1):342-50. doi: 10.1016/j.bbapap.2012.08.005. Epub 2012 Aug 11.

PMID:
22906532
9.

Wide-line NMR and protein hydration.

Tompa K, Bokor M, Tompa P.

Methods Mol Biol. 2012;895:167-96. doi: 10.1007/978-1-61779-927-3_13.

PMID:
22760320
10.

Distinct hydration properties of wild-type and familial point mutant A53T of α-synuclein associated with Parkinson's disease.

Hazy E, Bokor M, Kalmar L, Gelencser A, Kamasa P, Han KH, Tompa K, Tompa P.

Biophys J. 2011 Nov 2;101(9):2260-6. doi: 10.1016/j.bpj.2011.08.052. Epub 2011 Nov 1.

11.

Hydration water/interfacial water in crystalline lens.

Tompa K, Bánki P, Bokor M, Kamasa P, Rácz P, Tompa P.

Exp Eye Res. 2010 Jul;91(1):76-84. doi: 10.1016/j.exer.2010.04.005. Epub 2010 Apr 20.

PMID:
20412792
12.

High levels of structural disorder in scaffold proteins as exemplified by a novel neuronal protein, CASK-interactive protein1.

Balázs A, Csizmok V, Buday L, Rakács M, Kiss R, Bokor M, Udupa R, Tompa K, Tompa P.

FEBS J. 2009 Jul;276(14):3744-56. doi: 10.1111/j.1742-4658.2009.07090.x. Epub 2009 Jun 11.

13.

Interfacial water at protein surfaces: wide-line NMR and DSC characterization of hydration in ubiquitin solutions.

Tompa K, Bánki P, Bokor M, Kamasa P, Lasanda G, Tompa P.

Biophys J. 2009 Apr 8;96(7):2789-98. doi: 10.1016/j.bpj.2008.11.038.

14.

Intrinsic structural disorder of DF31, a Drosophila protein of chromatin decondensation and remodeling activities.

Szollosi E, Bokor M, Bodor A, Perczel A, Klement E, Medzihradszky KF, Tompa K, Tompa P.

J Proteome Res. 2008 Jun;7(6):2291-9. doi: 10.1021/pr700720c. Epub 2008 May 17.

PMID:
18484763
15.

Protein-water and protein-buffer interactions in the aqueous solution of an intrinsically unstructured plant dehydrin: NMR intensity and DSC aspects.

Tompa P, Bánki P, Bokor M, Kamasa P, Kovács D, Lasanda G, Tompa K.

Biophys J. 2006 Sep 15;91(6):2243-9. Epub 2006 Jun 23.

16.

Ion-selective supported liquid membranes placed under steady-state diffusion control.

Tompa K, Birbaum K, Malon A, Vigassy T, Bakker E, Pretsch E.

Anal Chem. 2005 Dec 1;77(23):7801-9.

PMID:
16316191
17.

Rotor-stator molecular crystals of fullerenes with cubane.

Pekker S, Kováts E, Oszlányi G, Bényei G, Klupp G, Bortel G, Jalsovszky I, Jakab E, Borondics F, Kamarás K, Bokor M, Kriza G, Tompa K, Faigel G.

Nat Mater. 2005 Oct;4(10):764-7. Epub 2005 Sep 4.

PMID:
16142242
18.

Primary contact sites in intrinsically unstructured proteins: the case of calpastatin and microtubule-associated protein 2.

Csizmók V, Bokor M, Bánki P, Klement E, Medzihradszky KF, Friedrich P, Tompa K, Tompa P.

Biochemistry. 2005 Mar 15;44(10):3955-64.

PMID:
15751971
19.

NMR relaxation studies on the hydrate layer of intrinsically unstructured proteins.

Bokor M, Csizmók V, Kovács D, Bánki P, Friedrich P, Tompa P, Tompa K.

Biophys J. 2005 Mar;88(3):2030-7. Epub 2004 Dec 21.

20.

1H spin-spin relaxation in normal and cataractous human, normal fish and bird eye lenses.

Rácz P, Hargitai C, Alföldy B, Bánki P, Tompa K.

Exp Eye Res. 2000 Apr;70(4):529-36.

PMID:
10866001
21.

Photoemission investigation of the electronic-structure changes in Zr-Ni-Cu metallic glasses upon hydrogenation.

Petohuml G, Bakonyi I I, Tompa K, Guczi L.

Phys Rev B Condens Matter. 1995 Sep 1;52(10):7151-7158. No abstract available.

PMID:
9979656
22.

Variability of magnetic resonance parameters in pituitary adenomas at low temperature.

Pócsik I, Kenyeres M, Pásztor E, Tompa K.

Physiol Chem Phys Med NMR. 1993;25(2):137-44.

PMID:
8378440
23.
24.

In vitro assessment of MR relaxation properties of pituitary adenomas.

Pasztor E, Kemeny AA, Tompa K, Furó I, Pócsik I, Fedina L.

J Comput Assist Tomogr. 1987 May-Jun;11(3):378-83.

PMID:
3571577
25.

1H nuclear magnetic resonance study of intervertebral discs. A preliminary report.

Bobest M, Furó I, Tompa K, Pócsik I, Kuncz A.

Spine (Phila Pa 1976). 1986 Sep;11(7):709-11.

PMID:
3787343
26.

Knight shift and spin-lattice relaxation for 63Cu and 31P in amorphous Ni-Cu-P alloys.

Bakonyi I I, Schone HE, Varga LK, Tompa K, P Lovas A.

Phys Rev B Condens Matter. 1986 Apr 1;33(7):5030-5033. No abstract available.

PMID:
9938975
27.

In vitro 1H NMR "mapping" of human intervertebral discs.

Furó I, Bobest M, Pócsik I, Tompa K.

Magn Reson Med. 1986 Feb;3(1):146-9.

PMID:
3959880
28.

Combined 1H-NMR and vacuum dehydration study of rat muscles.

Pócsik I, Furó I, Tompa K, Neumark T, Takács J.

Biochim Biophys Acta. 1986 Jan 15;880(1):1-9.

PMID:
3942777
29.

Water fractions in normal and senile cataractous eye lenses studied by NMR.

Rácz P, Tompa K, Pócsik I, Bánki P.

Exp Eye Res. 1983 May;36(5):663-9.

PMID:
6852140
30.

The state of water in normal human, bird and fish eye lenses.

Rácz P, Tompa K, Pócsik I.

Exp Eye Res. 1979 Dec;29(6):601-8. No abstract available.

PMID:
544279
31.

The state of water in normal and senile cataractous lenses studied by nuclear magnetic resonance.

Rácz P, Tompa K, Pócsik I.

Exp Eye Res. 1979 Feb;28(2):129-35. No abstract available.

PMID:
446557

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