Wyniki wyszukiwania

1

Internal force field in selected proteins

100%

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

Acta Biochimica Polonica

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2019

|

tom 66

|

nr 4

2

The formation of soluble heat IgG aggregates for immunological studies

100%

Rybarska J., Piekarska B., Konieczny L., Roterman I.

Archivum Immunologiae et Therapiae Experimentalis

|

1988

|

tom 36

|

nr 5

3

The effect of azo dyes on the formation of immune complexes

100%

Rybarska J., Konieczny L., Roterman I., Piekarska B.

Archivum Immunologiae et Therapiae Experimentalis

|

1991

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tom 39

|

nr 3

4

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

88%

Dulak D., Banach M., Gadzala M., Konieczny L., Roterman I.

Acta Biochimica Polonica

|

2018

|

tom 65

|

nr 4

5

Artykuł dostępny w postaci pełnego tekstu - kliknij by otworzyć plik

The melting of native domain structure in effector activation of IgG studied by using Congo Red as a specific probe

88%

Piekarska B., Roterman I., Rybarska J., Konieczny L., Kaszuba J.

Journal of Physiology and Pharmacology

|

1994

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tom 45

|

nr 1

6

Heat - induced structural changes in the Fab fragment of IgG recognized by molecular dynamics simulation - implications for signal transduction in antibodies

88%

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

Folia Biologica

|

1994

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tom 42

|

nr 3-4

7

Bis-azo dyes interference with efector activation of antibodies

88%

Kaszuba J., Konieczny L., Piekarska B., Roterman I., Rybarska J.

Journal of Physiology and Pharmacology

|

1993

|

tom 44

|

nr 3

8

The detection of specific acute phase serum protein complexes and immune complexes by Congo Red binding

88%

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

Journal of Physiology and Pharmacology

|

1995

|

tom 46

|

nr 2

9

Przeciwciała i nośniki leków w terapii celowanej - postęp i ograniczenia

76%

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

Biotechnologia

|

2001

|

nr 3

10

Tandemly repeated trinucleotides - comparative analysis

76%

Piwowar M., Meus J., Piwowar P., Wisniowski Z., Stefaniak J., Roterman I.

Acta Biochimica Polonica

|

2006

|

tom 53

|

nr 2

Characteristics of 64 possible tandem trinucleotide repeats (TSSR) from Homo sapiens (hs), Mus musculus (mm) and Rattus norvegicus (rn) genomes are presented. Comparative analysis of TSSR frequency depending on their repetitiveness and similarity of the TSSR length distributions is shown. Comparative analysis of TSSR sequence motifs and association between type of motif and its length (n) using ρ-coefficient method (quantitatively measuring the association between variables in contingency tables) is presented. These analyses were carried out in the context of neurodegenerative diseases based on trinucleotide tandems. The length of these tandems and their relation to other TSSR is estimated. It was found that the higher repetitiveness (n) the lower frequency of trinucleotides tandems. Differences between genomes under consideration, especially in longer than n=9 TSSR were discussed. A significantly higher frequency off A- and T-rich tandems is observed in the human genome (as well as in human mRNA). This observation also applies to mm and rn, although lower abundant in proportion to human genomes was found. The origin of elongation (or shortening) of TSSR seems to be neither frequency nor length dependent. The results of TSSR analysis presented in this work suggest that neurodegenerative disease-related microsatellites do not differ versus the other except the lower frequency versus the other TSSR. CAG occurs with relatively high frequency in human mRNA, although there are other TSSR with higher frequency that do not cause comparable disease disorders. It suggests that the mechanism of TSSR instability is not the only origin of neurodegenerative diseases.

11

Bis azo dyes - studies on the mechanism of complex formation with IgG modulated by heating or antigen binding

76%

Roterman I., No K. T., Piekarska B., Kaszuba J., Pawlicki R., Rybarska J., Konieczny L.

Journal of Physiology and Pharmacology

|

1993

|

tom 44

|

nr 3

12

Supramolecularity creates nonstandard protein ligands

76%

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

Acta Biochimica Polonica

|

1999

|

tom 46

|

nr 4

Congo red and a group of structurally related dyes long used to stain amyloid proteins are known to associate in water solutions. The self-association of some dyes belonging to this group appears particularly strong. In water solutions their molecules are arranged in ribbon-like micellar forms with liquid crystalline properties. These compounds have recently been found to form complexeswith some native proteins in a non-standard way. Gaps formed by the local distribution of β-sheets in proteins probably represent the receptor sites for these dye ligands. They may result from higher structural instability in unfolding conditions, but also may appear as long range cooperative fluctuations generated by ligand binding. Immunoglobulins G were chosen as model binding proteins to check the mechanism of binding of these dyes. The sites of structural changes generated by antigen binding in antibodies, believed to act as a signal propagated to distant parts of the molecule, were assumed to be suitable sites for the complexation of liquid-crystalline dyes. This assumption was confirmed by proving that antibodies engaged in immune complexation really do bind these dyes; as expected, this binding affects their function by significantly enhancing antigen binding and simultaneously inhibiting C1q attachment. Binding of these supramolecular dyes by some other native proteins including serpins and their natural complexes was also shown. The strict dependence of the ligation properties on strong self-assembling and the particular arrangement of dye molecules indicate that supramolecularity is the feature that creates non-standard protein ligands, with potential uses in medicine and experimental science.

13

In vivo accumulation of self-assembling dye Congo red in an area marked by specific immune complexes: possible relevance to chemotherapy

76%

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

Folia Histochemica et Cytobiologica

|

2004

|

tom 42

|

nr 2

14

Intramolecular signalling in immunoglobulins - new evidence emerging from the use of supramolecular protein ligands

76%

Piekarska B., Konieczny L., Rybarska J., Stopa B., Spolnik P., Roterman I., Krol M.

Journal of Physiology and Pharmacology

|

2004

|

tom 55

|

nr 3

The postulated intramolecular signaling in immunoglobulins generated by antigen binding has been controversial for years. The high heterogeneity of immune complexes as signaling systems and the requirement of the immobilized antigen form for efficient triggering of effector activity is likely the reason for the lack of clarity. Here we present new evidence supporting the notion of intramolecular signaling, based on the use of supramolecular dyes that bind to signal-derived specific sites in immunoglobulins.

15

Amyloids, Congo red and the apple-green effect

64%

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

Acta Biochimica Polonica

|

2019

|

tom 66

|

nr 1

16

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

64%

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

Acta Biochimica Polonica

|

2017

|

tom 64

|

nr 1

17

Egg yolk platelet proteins from Xenopus laevis are amyloidogenic

64%

Zemanek G., Konieczny L., Piekarska B., Rybarska J., Stopa B., Spolnik P., Urbanowicz B., Nowak M., Krol M., Roterman I.

Folia Histochemica et Cytobiologica

|

2002

|

tom 40

|

nr 3

18

The structure and protein binding of amyloid-specific dye reagents

64%

Stopa B., Piekarska B., Konieczny L., Rybarska J., Spolnik P., Zemanek G., Roterman I., Krol M.

Acta Biochimica Polonica

|

2003

|

tom 50

|

nr 4

The self-assembling tendency and protein complexation capability of dyes related to Congo red and also some dyes of different structure were compared to explain the mechanism of Congo red binding and the reason for its specific affinity for /3-struc- ture. Complexation with proteins was measured directly and expressed as the number of dye molecules bound to heat-aggregated IgG and to two light chains with different structural stability. Binding of dyes to rabbit antibodies was measured indirectly as the enhancement effect of the dye on immune complex formation. Self-assembling was tested using dynamic light scattering to measure the size of the supra- molecular assemblies. In general the results show that the supramolecular form of a dye is the main factor determining its complexation capability. Dyes that in their compact supramolecular organization are ribbon-shaped may adhere to polypeptides of /3-conformation due to the architectural compatibility in this unique structural form. The optimal fit in complexation seems to depend on two contradictory factors involving, on the one hand, the compactness of the non-covalently stabilized supra- molecular ligand, and the dynamic character producing its plasticity on the other. As a result, the highest protein binding capability is shown by dyes with a moderate self-assembling tendency, while those arranging into either very rigid or very unstable supramolecular entities are less able to bind.

19

Bis azo dye liquid crystalline micelles as possible drug carriers in immunotargeting technique

64%

Konieczny L., Piekarska B., Rybarska J., Stopa B., Krzykwa B., Noworolski J., Pawlicki R., Roterman I.

Journal of Physiology and Pharmacology

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1994

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tom 45

|

nr 3

20

The use of Congo Red as a lyotropic liquid crystal to carry strains in a model immunotargeting system - microscopic studies

64%

Konieczny L., Piekarska B., Rybarska J., Skowronek M., Stopa B., Tabor B., Dabros W., Pawlicki R., Roterman I.

Folia Histochemica et Cytobiologica

|

1997

|

tom 35

|

nr 4

Ograniczanie wyników

Internal force field in selected proteins

The formation of soluble heat IgG aggregates for immunological studies

The effect of azo dyes on the formation of immune complexes

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

The melting of native domain structure in effector activation of IgG studied by using Congo Red as a specific probe

Heat - induced structural changes in the Fab fragment of IgG recognized by molecular dynamics simulation - implications for signal transduction in antibodies

Bis-azo dyes interference with efector activation of antibodies

The detection of specific acute phase serum protein complexes and immune complexes by Congo Red binding

Przeciwciała i nośniki leków w terapii celowanej - postęp i ograniczenia

Tandemly repeated trinucleotides - comparative analysis

Bis azo dyes - studies on the mechanism of complex formation with IgG modulated by heating or antigen binding

Supramolecularity creates nonstandard protein ligands

In vivo accumulation of self-assembling dye Congo red in an area marked by specific immune complexes: possible relevance to chemotherapy

Intramolecular signalling in immunoglobulins - new evidence emerging from the use of supramolecular protein ligands

Amyloids, Congo red and the apple-green effect

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

Egg yolk platelet proteins from Xenopus laevis are amyloidogenic

The structure and protein binding of amyloid-specific dye reagents

Bis azo dye liquid crystalline micelles as possible drug carriers in immunotargeting technique

The use of Congo Red as a lyotropic liquid crystal to carry strains in a model immunotargeting system - microscopic studies