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Modeling of the phospholipid vesicular nanostructure formation process

100%

Avdieieva L., Chunikhin O.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

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2019

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tom 100

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nr 4

2

Lecithin - pharmaceutical applications expanded beyond liposomes

100%

Sznitowska M.

Cellular and Molecular Biology Letters

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2005

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tom 10

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nr Suppl.

3

Brain spectrin interacts with membrane phospholipids

100%

Diakowski W., Sikorski A. F.

Acta Biochimica Polonica

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1994

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tom 41

|

nr 2

4

Effect of thyrotropin on phospholipid composition in thyroid plasma membranes

100%

Stelmach H., Mosko P., Jaroszewicz L.

Journal of Physiology and Pharmacology

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1993

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tom 44

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nr 2

5

Ankyrin shares a binding site with phospholipid vesicles on erythrocyte spectrin

100%

Bialkowska K., Zembron A., Sikorski A. F.

Acta Biochimica Polonica

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1994

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tom 41

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nr 2

6

Annexins-multifunctional, calcium-dependent, phospholipid-binding proteins

100%

Bandorowicz J., Pikula S.

Acta Biochimica Polonica

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1993

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tom 40

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nr 3

7

Conformational transitions in phospholipid bilayers: effect of packing forces and hydration

100%

Bruzik K. S.

Cellular and Molecular Biology Letters

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1999

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tom 04

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nr 2

8

The influence of melanin on the process of lipid peroxidation. Part 1. The influence of melanin on photo-induced lipid peroxidation

88%

Ezzahir A.

Applied Biology Communications. Lublin Scientific Center

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1991

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tom 01

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nr 6

9

The hydration of lipids and what it can tell us

88%

Jendrasiak G. L.

Cellular and Molecular Biology Letters

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1999

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tom 04

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nr 2

10

Role of leukotrienes and platelet activating factor in gastric mucosal damage and repair

75%

Konturek S. J., Brzozowski T.

Journal of Physiology and Pharmacology

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1991

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tom 42

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nr 2

Gastric mucosal integrity depends upon the balance between „aggressive” factors and „defensive” mechanisms. The formation of mucosal lesions results from the disruption of defense lines, including the breaking of unstirred mucus layer, the reduction of surface hydrophobicity, extensive exfoliation of surface epithelium, penetration of offending agents deeply into the mucosa and damage to the microvessels. The release of proinflam- matory and vasoactive mediators such as leukotrienes (LT), thromboxanes, platelet activating factor (PAP), endothelins and others has been thought to be involved in the pathomechanism of mucosal injury, especially damage to the micro vascular endothelium, increased vascular permeability, reduction in mucosal blood flow, vascular stasis, tissue ischemia and glandular cell necrosis. This paper reviews the mechanisms and possible pathogenetic implication of two related compounds, LT and PAP in acute mucosal injury by topical irritants such as ethanol, aspirin, bile salts and by stress. LT and PAP arise from similar membrane phospholipids and may regulate the biosynthesis of one another in the damaged mucosa. Although pharmacological studies have clearly demonstrated the noxious effects of cysteinyl LT and PAP on the mucosa, especially when exposed to topical irritants, recent publications have challenged the primary role of these mediators in the pathogenesis of mucosal lesions and ulcerations because the treatment with agents that selectively antagonize their biosynthesis or the receptor sites at the target cells did not always interrupt the chain of events leading to mucosal injury. The role of these mediators in the mucosal repair processes has been little studied but both cysteinyl LT and PAP seem to delay the restitution and healing of the mucosa. Further studies are necessary to clarify to what extent the biosynthesis of LT and PAP and the pharmacological inhibition of their action on the target tissues is related to noxious, protective and reparative events in the mucosa exposed to mild irritants and ulcerogens.

11

Annexin VI, a novel ATP-dependent protein. Alterations of phospholipid binding properties of annexin VI by nucleotides

75%

Danieluk M., Sikorski A. F., Pikula S., Bandorowicz-Pikula J.

Cellular and Molecular Biology Letters

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1999

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tom 04

|

nr 2

12

Changes of C18 fatty acids content in phospholipids of synchronously cultured Chlorella vulgaris

75%

Mazurek U.

Acta Biochimica Polonica

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1993

|

tom 40

|

nr 1

13

Membrane fluidity as affected by the organophosphorus insecticide menthylbromfenvinfos

75%

Blasiak J.

Polish Journal of Environmental Studies

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1996

|

tom 05

|

nr 1

The interaction of methylbromfenvinfos with model and native membranes was investigated using fluorescence anisotropy of 1,6-diphenyl-1,3,5-hexatriene (DPH), a probe located in the hydrophobic core of the bilayer and l,3-bis-(l-pyrene) propane, a probe distributed in the outer region of the bilayer. DPH reported a broadening of the transition profile and solidifying effects in the fluid phase of liposomes formed from dimyristoyl (DMPC), dipalmitoyl (DPPC), and distearoyl (DSPC) phosphatidylcholine in the presence of 50 μM of the insecticide. Py(3)Py detected an ordering effect of the insecticide in the fluid state of the lipids and abolished pretransition in DPPC and DSPC vesicles. Cholesterol added to DMPC decreased the influence of the insecticide. The effect of methylbromfenvinfos on the fluidity of some native membranes, namely erythrocytes, lymphocytes, brain microsomes, and sarcoplasmic reticulum, depended on the cholesterol content of these membranes.

14

In vitro culture of human peritoneal mesothelium for investigation of mesothelial dysfunction during peritoneal dialysis

75%

Witowski J., Breborowicz A., Knapowski J., Oreopoulos D.

Journal of Physiology and Pharmacology

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1994

|

tom 45

|

nr 2

15

Heat induced changes in absorbancy of cytochrome oxidase entrapped in asolectin - decan - water system

75%

Stanicova J.

Biophysics of Membrane Transport

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1994

|

tom 12

|

nr 2

16

Magnetic field effects on biological membranes and tissues

75%

Hong F. T.

Biophysics of Membrane Transport

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1994

|

tom 12

|

nr 1

17

The ultraviolet studies on protein-lipid interaction of a protein kinase C-gamma phorbol-binding domain

75%

Kowara R., Gryckiewicz E., Matecki A., Pawelczyk T.

Acta Biochimica Polonica

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1999

|

tom 46

|

nr 2

Family of protein kinase C (PKC) isozymes play a key role in transducing a vast number of signals into the cells. The members of classical PKC family are activated by binding of various lipid ligands to one of the several cysteine-rich domains of the enzyme. Second cysteine-rich (Cys2) domain of PKC-γ was expressed in Escherichia coli as a fusion protein with glutathione-S-transferase (GST) using the cDNA sequence from rat brain. The Cys2 protein after cleavage from GST was purified to homogeneity using glutathione-agarose and Mono-S cation exchanger column. In order to investigate the interaction of lipids and calcium with Cys2 protein we used UV spectroscopy. The UV spectrum of Cys2 protein exhibited a maximum at 205 nm. Exposition of Cys2 protein to phosphatidylserine (PS) vesicles resulted in significant decrease in the absorbance in the 210 nm region. Changes in UV spectrum of Cys2 protein induced by phorbol 12,13-dibutyrate (PDB) were smaller than those induced by PS, and addition of PDB with PS had no effect on the PS induced changes in UV spectrum of Cys2. Neither phosphatidylcholine (PC) nor phosphatidylethanolamine (PE) affected UV spectrum of Cys2 but in the presence of phosphatidylinositol 4,5-bisphosphate (PIP2) or phosphatidylinositol 4-phosphate (PIP) vesicles some changes were observed. Calcium ions alone or in the presence of PS had no effect on the UV spectrum of Cys2 protein. These data indicate that PS comparing to PDB, interacts with a larger area of Cys2 protein, and that the binding sites for these two molecules are at least overlapping. The site of PIP and PIP2 interaction with PKC-γ is distinct from that of phorbol ester binding site.

18

Functional role of interaction of spectrins with membrane phospholipids

75%

Sikorski A. F.

Cellular and Molecular Biology Letters

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2002

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tom 07

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nr Suppl.

19

Ankyrin inhibits interaction of erythrocyte spectrin with phospholipids

75%

Bialkowska K., Sikorski A. F.

Biophysics of Membrane Transport

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1994

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tom 12

|

nr 2

20

Annexin VI, a novel ATP-dependent, phospholipid-binding protein

75%

Danieluk M., Sikorski A. F., Pikula S., Bandorowicz-Pikula J.

Cellular and Molecular Biology Letters

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1999

|

tom 04

|

nr 4

The determination of surface pressure (π) of a phosphatidylserine (PS) monolayer is used to study the interactions between specific phospholipid classes and various proteins. In the present study we show that ATP, but not ADP, in milimolar concentration ranges stimulate the increase of Δπ in a PS monolayer evoked by annexin VI (AnxVI)/Ca2+ at a moderate initial π (~11 mN/m). The obtained results are consistent with ATP being a functional ligand for AnxVI. To further study the ATP binding site of AnxVI, we have used fluorescein 5’-isothiocyanate (FITC). This is useful in the characterization of nucleotide-binding sites of many membrane integral and cytosolic proteins. Under our experimental conditions FITC did not affect the binding of AnxVI to membranes but abolished the interaction of the protein with ATP insolubilized on agarose. This observation can be interpreted in terms of AnxVI possessing an ATP-binding site functionally similar to nucleotide-binding domains characterized in other ATP-dependent proteins. We also provide evidence that two AnxVI isoforms are expressed constitutively in porcine liver differ from each other in respect to their ATP binding properties.

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