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Items: 1 to 20 of 57

1.

The Amyloid as a Ribbon-Like Micelle in Contrast to Spherical Micelles Represented by Globular Proteins.

Banach M, Konieczny L, Roterman I.

Molecules. 2019 Dec 3;24(23). pii: E4395. doi: 10.3390/molecules24234395. Review.

2.

Internal force field in selected proteins.

Ptak-Kaczor M, Banach M, Konieczny L, Roterman I.

Acta Biochim Pol. 2019 Nov 20. doi: 10.18388/abp.2019_2865. [Epub ahead of print]

3.

Different Synergy in Amyloids and Biologically Active Forms of Proteins.

Fabian P, Stapor K, Banach M, Ptak-Kaczor M, Konieczny L, Roterman I.

Int J Mol Sci. 2019 Sep 9;20(18). pii: E4436. doi: 10.3390/ijms20184436.

4.

Supramolecular Congo Red as Specific Ligand of Antibodies Engaged in Immune Complex.

Jagusiak A, Rybarska J, Piekarska B, Stopa B, Konieczny L.

In: Roterman I, Konieczny L, editors. Self-Assembled Molecules – New Kind of Protein Ligands: Supramolecular Ligands [Internet]. Cham (CH): Springer; 2018. Chapter 2.
2017 Nov 4.

5.

Supramolecular Systems as Protein Ligands.

Rybarska J, Piekarska B, Stopa B, Zemanek G, Konieczny L, Roterman I.

In: Roterman I, Konieczny L, editors. Self-Assembled Molecules – New Kind of Protein Ligands: Supramolecular Ligands [Internet]. Cham (CH): Springer; 2018. Chapter 1.
2017 Nov 4.

6.

Possible Mechanism of Amyloidogenesis of V Domains.

Banach M, Kalinowska B, Konieczny L, Roterman I.

In: Roterman I, Konieczny L, editors. Self-Assembled Molecules – New Kind of Protein Ligands: Supramolecular Ligands [Internet]. Cham (CH): Springer; 2018. Chapter 5.
2017 Nov 4.

7.

Metal Ions Introduced to Proteins by Supramolecular Ligands.

Woźnicka O, Rybarska J, Jagusiak A, Konieczny L, Stopa B, Roterman I.

In: Roterman I, Konieczny L, editors. Self-Assembled Molecules – New Kind of Protein Ligands: Supramolecular Ligands [Internet]. Cham (CH): Springer; 2018. Chapter 4.
2017 Nov 4.

8.

Structural analysis of the Aβ(11-42) amyloid fibril based on hydrophobicity distribution.

Roterman I, Dułak D, Gadzała M, Banach M, Konieczny L.

J Comput Aided Mol Des. 2019 Jul;33(7):665-675. doi: 10.1007/s10822-019-00209-9. Epub 2019 Jul 10.

9.

Secondary and Supersecondary Structure of Proteins in Light of the Structure of Hydrophobic Cores.

Banach M, Konieczny L, Roterman I.

Methods Mol Biol. 2019;1958:347-378. doi: 10.1007/978-1-4939-9161-7_19.

PMID:
30945229
10.

Amyloids, Congo red and the apple-green effect.

Jagusiak A, Rybarska J, Konieczny L, Piekarska B, Stopa B, Chłopaś K, Zemanem G, Roterman I.

Acta Biochim Pol. 2019 Mar 14;66(1):39-46. doi: 10.18388/abp.2018_2667.

11.

The aqueous environment as an active participant in the protein folding process.

Gadzała M, Dułak D, Kalinowska B, Baster Z, Bryliński M, Konieczny L, Banach M, Roterman I.

J Mol Graph Model. 2019 Mar;87:227-239. doi: 10.1016/j.jmgm.2018.12.008. Epub 2018 Dec 14.

12.

Structural analysis of the Aβ(15-40) amyloid fibril based on hydrophobicity distribution.

Dułak D, Banach M, Gadzała M, Konieczny L, Roterman I.

Acta Biochim Pol. 2018 Nov 21;65(4):595-604. doi: 10.18388/abp.2018_2647.

13.

Filamentous Aggregates of Tau Proteins Fulfil Standard Amyloid Criteria Provided by the Fuzzy Oil Drop (FOD) Model.

Dułak D, Gadzała M, Banach M, Ptak M, Wiśniowski Z, Konieczny L, Roterman I.

Int J Mol Sci. 2018 Sep 25;19(10). pii: E2910. doi: 10.3390/ijms19102910.

14.

Towards the design of anti-amyloid short peptide helices.

Roterman I, Banach M, Konieczny L.

Bioinformation. 2018 Jan 31;14(1):1-7. doi: 10.6026/97320630014001. eCollection 2018.

15.

Antifreeze proteins.

Roterman I, Banach M, Konieczny L.

Bioinformation. 2017 Dec 31;13(12):400-401. doi: 10.6026/97320630013400. eCollection 2017.

16.

Propagation of Fibrillar Structural Forms in Proteins Stopped by Naturally Occurring Short Polypeptide Chain Fragments.

Roterman I, Banach M, Konieczny L.

Pharmaceuticals (Basel). 2017 Nov 16;10(4). pii: E89. doi: 10.3390/ph10040089.

17.

Is the hydrophobic core a universal structural element in proteins?

Kalinowska B, Banach M, Wiśniowski Z, Konieczny L, Roterman I.

J Mol Model. 2017 Jul;23(7):205. doi: 10.1007/s00894-017-3367-z. Epub 2017 Jun 16.

18.

Dispersion of single-wall carbon nanotubes with supramolecular Congo red - properties of the complexes and mechanism of the interaction.

Jagusiak A, Piekarska B, Pańczyk T, Jemioła-Rzemińska M, Bielańska E, Stopa B, Zemanek G, Rybarska J, Roterman I, Konieczny L.

Beilstein J Nanotechnol. 2017 Mar 16;8:636-648. doi: 10.3762/bjnano.8.68. eCollection 2017.

19.

Silver ions as em marker of congo red ligation sites in amyloids and amyloid-like aggregates.

Rybarska J, Konieczny L, Jagusiak A, Chłopaś K, Zemanek G, Piekarska B, Stopa B, Piwowar P, Woźnicka O, Roterman I.

Acta Biochim Pol. 2017;64(1):161-169. doi: 10.18388/abp.2016_1393. Epub 2016 Dec 19.

20.

Structural Interface Forms and Their Involvement in Stabilization of Multidomain Proteins or Protein Complexes.

Dygut J, Kalinowska B, Banach M, Piwowar M, Konieczny L, Roterman I.

Int J Mol Sci. 2016 Oct 18;17(10). pii: E1741.

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