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Items: 1 to 20 of 50

1.

Structure and Functions of Microtubule Associated Proteins Tau and MAP2c: Similarities and Differences.

Melková K, Zapletal V, Narasimhan S, Jansen S, Hritz J, Škrabana R, Zweckstetter M, Ringkjøbing Jensen M, Blackledge M, Žídek L.

Biomolecules. 2019 Mar 16;9(3). pii: E105. doi: 10.3390/biom9030105. Review.

2.

Functionally specific binding regions of microtubule-associated protein 2c exhibit distinct conformations and dynamics.

Melková K, Zapletal V, Jansen S, Nomilner E, Zachrdla M, Hritz J, Nováček J, Zweckstetter M, Jensen MR, Blackledge M, Žídek L.

J Biol Chem. 2018 Aug 24;293(34):13297-13309. doi: 10.1074/jbc.RA118.001769. Epub 2018 Jun 20.

PMID:
29925592
3.

Protein environment affects the water-tryptophan binding mode. MD, QM/MM, and NMR studies of engrailed homeodomain mutants.

Špačková N, Trošanová Z, Šebesta F, Jansen S, Burda JV, Srb P, Zachrdla M, Žídek L, Kozelka J.

Phys Chem Chem Phys. 2018 May 9;20(18):12664-12677. doi: 10.1039/c7cp08623g.

PMID:
29696277
4.

Triple resonance ¹⁵Ν NMR relaxation experiments for studies of intrinsically disordered proteins.

Srb P, Nováček J, Kadeřávek P, Rabatinová A, Krásný L, Žídková J, Bobálová J, Sklenář V, Žídek L.

J Biomol NMR. 2017 Nov;69(3):133-146. doi: 10.1007/s10858-017-0138-1. Epub 2017 Oct 25.

PMID:
29071460
5.

Conformational dynamics are a key factor in signaling mediated by the receiver domain of a sensor histidine kinase from Arabidopsis thaliana.

Otrusinová O, Demo G, Padrta P, Jaseňáková Z, Pekárová B, Gelová Z, Szmitkowska A, Kadeřávek P, Jansen S, Zachrdla M, Klumpler T, Marek J, Hritz J, Janda L, Iwaï H, Wimmerová M, Hejátko J, Žídek L.

J Biol Chem. 2017 Oct 20;292(42):17525-17540. doi: 10.1074/jbc.M117.790212. Epub 2017 Aug 31.

6.

Role of SH3b binding domain in a natural deletion mutant of Kayvirus endolysin LysF1 with a broad range of lytic activity.

Benešík M, Nováček J, Janda L, Dopitová R, Pernisová M, Melková K, Tišáková L, Doškař J, Žídek L, Hejátko J, Pantůček R.

Virus Genes. 2018 Feb;54(1):130-139. doi: 10.1007/s11262-017-1507-2. Epub 2017 Aug 29.

PMID:
28852930
7.

Conformational Entropy from Slowly Relaxing Local Structure Analysis of 15N-H Relaxation in Proteins: Application to Pheromone Binding to MUP-I in the 283-308 K Temperature Range.

Žídek L, Meirovitch E.

J Phys Chem B. 2017 Sep 21;121(37):8684-8692. doi: 10.1021/acs.jpcb.7b06049. Epub 2017 Sep 8.

PMID:
28825833
8.

Quantitative mapping of microtubule-associated protein 2c (MAP2c) phosphorylation and regulatory protein 14-3-3ζ-binding sites reveals key differences between MAP2c and its homolog Tau.

Jansen S, Melková K, Trošanová Z, Hanáková K, Zachrdla M, Nováček J, Župa E, Zdráhal Z, Hritz J, Žídek L.

J Biol Chem. 2017 Jun 16;292(24):10316. doi: 10.1074/jbc.A116.771097. No abstract available.

9.

Solution structure of domain 1.1 of the σA factor from Bacillus subtilis is preformed for binding to the RNA polymerase core.

Zachrdla M, Padrta P, Rabatinová A, Šanderová H, Barvík I, Krásný L, Žídek L.

J Biol Chem. 2017 Jul 14;292(28):11610-11617. doi: 10.1074/jbc.M117.784074. Epub 2017 May 24.

10.

Quantitative mapping of microtubule-associated protein 2c (MAP2c) phosphorylation and regulatory protein 14-3-3ζ-binding sites reveals key differences between MAP2c and its homolog Tau.

Jansen S, Melková K, Trošanová Z, Hanáková K, Zachrdla M, Nováček J, Župa E, Zdráhal Z, Hritz J, Žídek L.

J Biol Chem. 2017 Apr 21;292(16):6715-6727. doi: 10.1074/jbc.M116.771097. Epub 2017 Mar 3. Erratum in: J Biol Chem. 2017 Jun 16;292(24):10316.

11.

The Eighth Central European Conference "Chemistry towards Biology": Snapshot.

Perczel A, Atanasov AG, Sklenář V, Nováček J, Papoušková V, Kadeřávek P, Žídek L, Kozłowski H, Wątły J, Hecel A, Kołkowska P, Koča J, Svobodová-Vařeková R, Pravda L, Sehnal D, Horský V, Geidl S, Enriz RD, Matějka P, Jeništová A, Dendisová M, Kokaislová A, Weissig V, Olsen M, Coffey A, Ajuebor J, Keary R, Sanz-Gaitero M, van Raaij MJ, McAuliffe O, Waltenberger B, Mocan A, Šmejkal K, Heiss EH, Diederich M, Musioł R, Košmrlj J, Polański J, Jampílek J.

Molecules. 2016 Oct 17;21(10). pii: E1381.

12.

Spectral density mapping at multiple magnetic fields suitable for (13)C NMR relaxation studies.

Kadeřávek P, Zapletal V, Fiala R, Srb P, Padrta P, Přecechtělová JP, Šoltésová M, Kowalewski J, Widmalm G, Chmelík J, Sklenář V, Žídek L.

J Magn Reson. 2016 May;266:23-40. doi: 10.1016/j.jmr.2016.02.016. Epub 2016 Mar 8.

PMID:
27003380
13.

The influence of Mg2+ coordination on 13C and 15N chemical shifts in CKI1RD protein domain from experiment and molecular dynamics/density functional theory calculations.

Vícha J, Babinský M, Demo G, Otrusinová O, Jansen S, Pekárová B, Žídek L, Munzarová ML.

Proteins. 2016 May;84(5):686-99. doi: 10.1002/prot.25019. Epub 2016 Mar 10.

PMID:
26879585
14.

Structural Aspects of Multistep Phosphorelay-Mediated Signaling in Plants.

Pekárová B, Szmitkowska A, Dopitová R, Degtjarik O, Žídek L, Hejátko J.

Mol Plant. 2016 Jan 4;9(1):71-85. doi: 10.1016/j.molp.2015.11.008. Epub 2015 Nov 26. Review.

15.

Cross-correlated relaxation measurements under adiabatic sweeps: determination of local order in proteins.

Kadeřávek P, Grutsch S, Salvi N, Tollinger M, Žídek L, Bodenhausen G, Ferrage F.

J Biomol NMR. 2015 Dec;63(4):353-365. doi: 10.1007/s10858-015-9994-8. Epub 2015 Oct 28.

16.

NMR assignment of intrinsically disordered self-processing module of the FrpC protein of Neisseria meningitidis.

Kubáň V, Nováček J, Bumba L, Žídek L.

Biomol NMR Assign. 2015 Oct;9(2):435-40. doi: 10.1007/s12104-015-9625-z. Epub 2015 Jul 3.

PMID:
26138689
17.

Conformational dynamics and antigenicity in the disordered malaria antigen merozoite surface protein 2.

MacRaild CA, Zachrdla M, Andrew D, Krishnarjuna B, Nováček J, Žídek L, Sklenář V, Richards JS, Beeson JG, Anders RF, Norton RS.

PLoS One. 2015 Mar 5;10(3):e0119899. doi: 10.1371/journal.pone.0119899. eCollection 2015.

18.

Stabilization of the β-hairpin in Mason-Pfizer monkey virus capsid protein- a critical step for infectivity.

Obr M, Hadravová R, DoleŽal M, KříŽová I, Papoušková V, Zídek L, Hrabal R, Ruml T, Rumlová M.

Retrovirology. 2014 Oct 30;11:94. doi: 10.1186/s12977-014-0094-8.

19.

Retro operation on the Trp-cage miniprotein sequence produces an unstructured molecule capable of folding similar to the original only upon 2,2,2-trifluoroethanol addition.

Vymětal J, Bathula SR, Cerný J, Chaloupková R, Zídek L, Sklenář V, Vondrášek J.

Protein Eng Des Sel. 2014 Dec;27(12):463-72. doi: 10.1093/protein/gzu046. Epub 2014 Oct 24.

PMID:
25344682
20.

X-ray vs. NMR structure of N-terminal domain of δ-subunit of RNA polymerase.

Demo G, Papoušková V, Komárek J, Kadeřávek P, Otrusinová O, Srb P, Rabatinová A, Krásný L, Žídek L, Sklenář V, Wimmerová M.

J Struct Biol. 2014 Aug;187(2):174-186. doi: 10.1016/j.jsb.2014.06.001. Epub 2014 Jun 14.

PMID:
24937760

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