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Items: 1 to 20 of 116

1.

Off-pathway 3D-structure provides protection against spontaneous Asn/Asp isomerization: shielding proteins Achilles heel.

Láng A, Jákli I, Enyedi KN, Mező G, Menyhárd DK, Perczel A.

Q Rev Biophys. 2020 Jan 31;53:e2. doi: 10.1017/S003358351900009X.

PMID:
32000865
2.

The Route from the Folded to the Amyloid State: Exploring the Potential Energy Surface of a Drug-Like Miniprotein.

Taricska N, Horváth D, Menyhárd DK, Ákontz-Kiss H, Noji M, So M, Goto Y, Fujiwara T, Perczel A.

Chemistry. 2020 Feb 11;26(9):1893. doi: 10.1002/chem.201905181. Epub 2020 Jan 21.

PMID:
31961031
3.

[Allele-specific inhibitors of mutant KRAS are in the focus of RASopathy consortium].

Nyíri K, Koppány G, Pálfy G, Vida I, Tóth S, Orgován Z, Ranđelović I, Baranyi M, Molnár E, Keserû MG, Tóvári J, Perczel A, Vértessy BG, Tímár J.

Magy Onkol. 2019 Dec 9;63(4):310-323. Epub 2019 Nov 25. Hungarian.

4.

The Route from the Folded to the Amyloid State: Exploring the Potential Energy Surface of a Drug-Like Miniprotein.

Taricska N, Horváth D, Menyhárd DK, Ákontz-Kiss H, Noji M, So M, Goto Y, Fujiwara T, Perczel A.

Chemistry. 2020 Feb 11;26(9):1968-1978. doi: 10.1002/chem.201903826. Epub 2019 Dec 27.

5.

Protein Aggregation in a Nutshell: The Splendid Molecular Architecture of the Dreaded Amyloid Fibrils.

Horváth D, Menyhárd DK, Perczel A.

Curr Protein Pept Sci. 2019;20(11):1077-1088. doi: 10.2174/1389203720666190925102832. Review.

PMID:
31553291
6.

Compactness of Protein Folds Alters Disulfide-Bond Reducibility by Three Orders of Magnitude: A Comprehensive Kinetic Case Study on the Reduction of Differently Sized Tryptophan Cage Model Proteins.

Horváth D, Taricska N, Keszei E, Stráner P, Farkas V, Tóth GK, Perczel A.

Chembiochem. 2020 Mar 2;21(5):681-695. doi: 10.1002/cbic.201900470. Epub 2019 Nov 18.

7.

1H, 15N backbone assignment and comparative analysis of the wild type and G12C, G12D, G12V mutants of K-Ras bound to GDP at physiological pH.

Pálfy G, Vida I, Perczel A.

Biomol NMR Assign. 2020 Apr;14(1):1-7. doi: 10.1007/s12104-019-09909-7. Epub 2019 Aug 29.

8.
9.
10.

DUckCov: a Dynamic Undocking-Based Virtual Screening Protocol for Covalent Binders.

Rachman M, Scarpino A, Bajusz D, Pálfy G, Vida I, Perczel A, Barril X, Keserű GM.

ChemMedChem. 2019 May 17;14(10):1011-1021. doi: 10.1002/cmdc.201900078. Epub 2019 Mar 8.

11.

α/β-Chimera peptide synthesis with cyclic β-sugar amino acids: the efficient coupling protocol.

Nagy A, Goldschmidt Gőz V, Pintér I, Farkas V, Perczel A.

Amino Acids. 2019 Apr;51(4):669-678. doi: 10.1007/s00726-019-02702-9. Epub 2019 Feb 13.

PMID:
30758725
12.

iNEXT: a European facility network to stimulate translational structural biology.

iNEXT Consortium.

FEBS Lett. 2018 Jun;592(12):1909-1917. doi: 10.1002/1873-3468.13062. Epub 2018 May 15. No abstract available.

13.

C-terminal oligomerization of podocin mediates interallelic interactions.

Stráner P, Balogh E, Schay G, Arrondel C, Mikó Á, L'Auné G, Benmerah A, Perczel A, K Menyhárd D, Antignac C, Mollet G, Tory K.

Biochim Biophys Acta Mol Basis Dis. 2018 Jul;1864(7):2448-2457. doi: 10.1016/j.bbadis.2018.04.008. Epub 2018 Apr 13.

14.

The impact of water on the ambivalent behavior and paradoxical phenomenon of the amyloid-β fibril protein.

Vajda T, Perczel A.

Biomol Concepts. 2017 Dec 20;8(5-6):213-220. doi: 10.1515/bmc-2017-0027. Review.

PMID:
29211680
15.

Biochemical and pharmacological characterization of three opioid-nociceptin hybrid peptide ligands reveals substantially differing modes of their actions.

Erdei AI, Borbély A, Magyar A, Taricska N, Perczel A, Zsíros O, Garab G, Szűcs E, Ötvös F, Zádor F, Balogh M, Al-Khrasani M, Benyhe S.

Peptides. 2018 Jan;99:205-216. doi: 10.1016/j.peptides.2017.10.005. Epub 2017 Oct 13.

PMID:
29038035
16.

The Piwi-piRNA pathway: road to immortality.

Sturm Á, Perczel A, Ivics Z, Vellai T.

Aging Cell. 2017 Oct;16(5):906-911. doi: 10.1111/acel.12630. Epub 2017 Jun 27.

17.

Four faces of the interaction between ions and aromatic rings.

Papp D, Rovó P, Jákli I, Császár AG, Perczel A.

J Comput Chem. 2017 Jul 15;38(20):1762-1773. doi: 10.1002/jcc.24816. Epub 2017 May 10.

PMID:
28488267
18.

Predictable Conformational Diversity in Foldamers of Sugar Amino Acids.

Menyhárd DK, Hudáky I, Jákli I, Juhász G, Perczel A.

J Chem Inf Model. 2017 Apr 24;57(4):757-768. doi: 10.1021/acs.jcim.6b00488. Epub 2017 Apr 11.

PMID:
28345931
19.

C-3 epimers of sugar amino acids as foldameric building blocks: improved synthesis, useful derivatives, coupling strategies.

Nagy A, Csordás B, Zsoldos-Mády V, Pintér I, Farkas V, Perczel A.

Amino Acids. 2017 Feb;49(2):223-240. doi: 10.1007/s00726-016-2346-5. Epub 2016 Nov 1.

PMID:
27803987
20.

Origin of problems related to Staudinger reduction in carbopeptoid syntheses.

Csordás B, Nagy A, Harmat V, Zsoldos-Mády V, Leveles I, Pintér I, Farkas V, Perczel A.

Amino Acids. 2016 Nov;48(11):2619-2633. Epub 2016 Jul 20.

PMID:
27438266

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