Temat: binding protein - Prolib Integro

Skocz do pozycji: 1.

Tytuł:: GcMAF: a polemic or a highly promising molecule?
Autorzy:: Eric Matamoros, Morales
Tematy:: HIV
Vitamin D binding protein-macrophage activating factor
cancer
controversies
neurological disorders
vitamin D binding protein
α-N-acetylgalactosaminidase; Pokaż więcej
Wydawca:: Przedsiębiorstwo Wydawnictw Naukowych Darwin / Scientific Publishing House DARWIN
Powiązania:: https://bibliotekanauki.pl/articles/1182805.pdf Link otwiera się w nowym oknie
Opis:: Vitamin D Binding Protein (DBP) is a multifunctional protein which main role is to carry vitamin D and its metabolites, but it also acts as an actin scavenger and is the precursor of the macrophage activating factor molecule (GcMAF), which has reported highly promising results against cancer, HIV, and neurological disorders including autism, Alzheimer disease, Chronic Fatigue Syndrome (CFS), among others. DBP leads to the formation of GcMAF due to the loss of the O-glycosylated oligosaccharide moiety of the peptide by glycohydrolysis mediated by T and B cells. Some of the current noticed diseases have got increased levels of α-N-acetylgalactosaminidase (Nagalase), a molecule that deglycosylates DBP so it cannot drive to GcMAF, leading to immunosuppression. In this review we take a close look at the state of art strategies and trials using GcMAF as well as the controversies that have emerged during the last decade with this ‘polemic’ molecule.
Dostawca treści:: Biblioteka Nauki

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Tytuł:: Cation binding properties of calretinin, an EF-hand calcium-binding protein.
Autorzy:: Groves, Patrick
Palczewska, Małgorzata
Tematy:: calcium binding protein
S100 protein
EF-hand
calretinin
metal binding; fluorescence; Pokaż więcej
Wydawca:: Polskie Towarzystwo Biochemiczne
Powiązania:: https://bibliotekanauki.pl/articles/1044171.pdf Link otwiera się w nowym oknie
Opis:: Calretinin (CR) is a neuronal EF-hand protein previously characterized as a calcium (micromolar affinity) binding protein. CR-containing neurons are spared in some neurodegenerative diseases, although it is as yet unconfirmed how CR plays an active role in this protection. Higher levels of some metal cations (e.g. copper and zinc) are associated with these diseases. At the same time, metals such as terbium (NMR and fluorescence) cadmium (NMR) and manganese (EPR) serve as useful calcium analogues in the study of EF-hand proteins. We survey the binding of the above-mentioned metal cations that might affect the structure and function of CR. Competitive 45Ca2+-overlay, competitive terbium fluorescence and intrinsic tryptophan fluorescence are used to detect the binding of metal cations to CR. Terbium and copper (half-maximal effect of 15 μM) bind to CR. Terbium has a similar or greater affinity for the calcium-binding sites of CR than calcium. Copper quenches the fluorescence of terbium-bound CR, and CR tryptophan residues and competes weakly for 45Ca2+-binding sites. Cadmium, magnesium, manganese and zinc bind less strongly (half-maximal effects above 0.1 mM). Therefore, only terbium appears to be a suitable analytical calcium analogue in further studies of CR. The principal conclusion of this work is that copper, in addition to calcium, might be a factor in the function of CR and a link between CR and neurodegenerative diseases.
Dostawca treści:: Biblioteka Nauki

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Tytuł:: Expression, purification and functional characterization of recombinant human acyl-CoA-binding protein (ACBP) from erythroid cells
Autorzy:: Augoff, Katarzyna
Kolondra, Adam
Chorzalska, Anna
Lach, Agnieszka
Grabowski, Krzysztof
Sikorski, Aleksander
Tematy:: acyl-CoA-binding protein
PC
DBI
ACBP
phosphatidylcholine; Pokaż więcej
Wydawca:: Polskie Towarzystwo Biochemiczne
Powiązania:: https://bibliotekanauki.pl/articles/1040319.pdf Link otwiera się w nowym oknie
Opis:: Fatty acyl-CoA esters are extremely important in cellular homeostasis. They are intermediates in both lipid metabolism and post-translational protein modifications. Among these modification events, protein palmitoylation seems to be unique by its reversibility which allows dynamic regulation of the protein hydrophobicity. The recent discovery of an enzyme family that catalyze protein palmitoylation has increased the understanding of the enzymology of the covalent attachment of fatty acids to proteins. Despite that, the molecular mechanism of supplying acyl-CoA esters to this reaction is yet to be established. Acyl-coenzyme A-binding proteins are known to bind long-chain acyl-CoA esters with very high affinity. Therefore, they play a significant role in intracellular acyl-CoA transport and pool formation. The purpose of this work is to explore the potential of one of the acyl-CoA-binding proteins to participate in the protein palmitoylation. In this study, a recombinant form of ACBP derived from human erythroid cells was expressed in E. coli, purified, and functionally characterized. We demonstrate that recombinant hACBP effectively binds palmitoyl-CoA in vitro, undergoing a shift from a monomeric to a dimeric state, and that this ligand-binding ability is involved in erythrocytic membrane phosphatidylcholine (PC) remodeling but not in protein acylation.
Dostawca treści:: Biblioteka Nauki

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Tytuł:: Characterization of a novel protein that specifically binds to DNA modified by N-acetoxy-acetylaminofluorene and cis-diamminedichloroplatinum
Autorzy:: Pietrowska, Monika
Widłak, Piotr
Tematy:: damage recognition
cisplatin
damaged DNA-binding protein
acetylaminofluorene; Pokaż więcej
Wydawca:: Polskie Towarzystwo Biochemiczne
Powiązania:: https://bibliotekanauki.pl/articles/1041333.pdf Link otwiera się w nowym oknie
Opis:: Proteins recognizing DNA damaged by the chemical carcinogen N-acetoxy-acetylaminofluorene (AAAF) were analyzed in nuclear extracts from rat tissues, using a 36 bp oligonucleotide as a substrate and electrophoretic mobility shift and Southwestern blot assays. One major damage-recognizing protein was detected, whose amount was estimated as at least 105 copies per cell. Levels of this protein were similar in extracts from brain, kidney and liver, but much lower in extracts from testis. The affinity of the detected protein for DNA damaged by AAAF was about 70-fold higher than for undamaged DNA. DNA damaged by cis-diamminedichloroplatinum (cis-DDP), benzo(a)pyrene diolepoxide (BPDE) or UV-radiation also bound this protein with an increased affinity, the former more strongly and the latter two more weakly as compared to AAAF-damaged DNA. The detected AAAF/DDP-damaged-DNA-binding (AAAF/DDP-DDB) protein had a molecular mass of about 25 kDa and was distinct from histone H1 or HMGB proteins, which are known to have a high affinity for cis-DDP-damaged DNA. The level of this damage-recognizing protein was not affected in rats treated with the carcinogen 2-acetylaminofluorene. The activity of an AAAF/DDP-DDB protein could also be detected in extracts from mouse liver cells but not from the Hep2G human hepatocellular carcinoma.
Dostawca treści:: Biblioteka Nauki

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Tytuł:: Serum galectin-3 and galectin-3 binding protein levels in systemic lupus erythematosus and cutaneous lupus erythematosus
Autorzy:: Jagielski, Paweł
Bienias, Piotr
Kowalewski, Cezary
Gala, Kamila
Kalinska-Bienias, Agnieszka
Kowalczyk, Emilia
Opis:: Introduction: The roles of galectin-3 (Gal-3) and galectin-3 binding protein (G3BP) in systemic lupus erythematosus (SLE) are of ongoing interest, but the data are insufficient due to highly limited available studies. There are no data on cutaneous lupus erythematosus (CLE). Aim: To assess serum Gal-3 and G3BP concentrations in SLE patients with and without LE-specific skin lesions, CLE patients and to correlate levels of proteins with clinical and laboratory parameters. Material and methods: The study included 71 SLE patients with and without LE-specific skin lesions, 23 CLE patients and 40 controls. Gal-3 and G3BP were measured by specific enzyme-linked immunosorbent assays (ELISA). Results: Serum Gal-3 and G3BP concentrations were significantly higher in SLE with and without LE-specific lesions compared to controls, but without differences between SLE groups. Gal-3 and G3BP levels were also elevated in CLE compared to controls (p = 0.001, p = 0.005; respectively). There was a positive correlation between G3BP level and CLASI activity score both in CLE (r = 0.55, p = 0.006) and in SLE patients with LE-specific lesions (r = 0.36, p = 0.02). G3BP and Gal-3 levels did not differ in SLE with LE-specific lesions and CLE. There was a positive correlation between serum G3BP level and the SLEDAI score in SLE patients (r = 0.26, p = 0.03). Conclusions: Our findings indicate that serum G3BP and Gal-3 are elevated in CLE. Additionally, G3BP might be associated with the extent of skin lesions. There are no differences between G3BP and Gal-3 concentrations in SLE with and without LE-specific skin lesions.
Dostawca treści:: Repozytorium Uniwersytetu Jagiellońskiego

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Tytuł:: The two-track investigation of fibronectin binding protein a of Staphylococcus aureus from bovine mastitis as a potential candidate for immunodiagnosis : a pilot study
Autorzy:: Karakulska, Jolanta
Drożdż, Kamil
Michalak, Katarzyna
Brzychczy-Włoch, Monika
Wójcik-Grzybek, Dagmara
Pietras-Ożga, Dorota
Dobrut, Anna
Młodzińska, Agata
Biegun, Katarzyna
Opis:: Bovine mastitis is the most common disease affecting dairy cattle worldwide and it generates substantial losses for cattle breeders. One of the most common pathogens identified in infected milk samples is Staphylococcus aureus. Currently, there is no fast test for recognizing bacteria species on the market. The aim of this study was to bioinformatically and laboratory detect and characterize the fibronectin binding protein A (FnBPA) of S. aureus (SA) in milk samples obtained from cows diagnosed with mastitis. More than 90,000,000 amino acid sequences were subjected to bioinformatic detection in the search for a potential biomarker for bovine SA. The analysis of FnBPA included the detection of signal peptides and nonclassical proteins, antigenicity, and the prediction of epitopes. To confirm the presence of the fnbA gene in four SA isolates, amplification with specific primers was performed. FnBPA was detected by immunoblotting. The immunoreactivity and selectivity were performed with monoclonal anti-FnBPA antibodies and SA-negative serum. The bioinformatic analysis showed that FnBPA is a surface, conservative, immunoreactive, and species-specific protein with antigenic potential. Its presence was confirmed in all of the SA isolates we studied. Immunoblotting proved its immunoreactivity and specificity. Thus, it can be considered a potential biomarker in mastitis immunodiagnostics.
Dostawca treści:: Repozytorium Uniwersytetu Jagiellońskiego

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Tytuł:: Structural basis of chiral wrap and T-segment capture by Escherichia coli DNA gyrase
Autorzy:: Heddle, Jonathan
Liston, Jonathon D.
Ghilarov, Dmitry
Pakosz-Stępień, Zuzanna
Gittins, Olivia
Michalczyk, Elizabeth
Pabiś, Marta
Dostawca treści:: Repozytorium Uniwersytetu Jagiellońskiego

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Tytuł:: Evaluation of riboflavin binding protein domain interaction using differential scanning calorimetry
Autorzy:: Wasylewski, Marcin
Dostawca treści:: Repozytorium Uniwersytetu Jagiellońskiego

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Tytuł:: Study of 53BP1 foci formation dynamics after chromatin damage induced by visible light: dependence on wavelength and dose of light
Badanie dynamiki tworzenia ognisk 53BP1 po uszkodzeniu chromatyny światłem widzialnym: zależność od dawki i długości fali światła
Autorzy:: Wesołowska, Julita
Opis:: DNA damages especially double-strand breaks are highly dangerous for maintenance genome integrity. Mechanism of double-strand DNA damage response is still being prospected, however, it is known that it promotes a number of histone post-tranlational modifications, such as dimethylation of Lys20 of histone 4 (H4k20me2), ubiquitilation of Lys15 of histone H2A (H2AK15ub) or phosphorylations. Such modifications are recognized by 53BP1 (repair factor) domains: Tudor interacts with H4K20me2 and UDR motif binds to H2AK15ub. 53BP1 takes part in choosing of repair pathway in response to DSBs of DNA. DNA damages repair for G1/G0 phase cells are mostly performed by nonhomologous end joining that 53BP1 promotes, by contrast, for S/G2 phase cells it is followed by homologous recombination that the 53BP1 antagonist – BRCA1 promotes. Repair proteins create noticeable foci in experiments that use ionising radiation, UV or visible light to induced DNA damages.The purpose of this master's thesis was to investigate of EGFP-53BP1 foci formation dynamics after local chromatin damage induced by visible light, in particular on wavelenght and dose of light dependence.Experiments were carried on living cells after imposition of plasmid vector to elicit transient expression of EGFP-53BP1 fusion protein. EGFP-53BP1 focus formation in site of damage was observed after chromatin exposure to visible light (488 nm – 594 nm) by laser beam park technique. Focus formation was not observed after usage of 633 nm light wavelenght. 53BP1 exhibits at least two types of foci formation. Maximum values of foci surfaces do not depend on dose of light but the minimal dose of light exist. EGFP-53BP1 focus can be continued untill mitosis and go on after cell division. Photobleaching effect appeared after induction of local chromatin damage by shorter than 561 nm wavelenghs. It could cause activation of fototoxicity of EGFP and could disturb studied system. Because of that side effect, the trial to get plasmid vector with mRFP-53BP1 protein was made.
Uszkodzenia DNA, w szczególności pęknięcia dwuniciowe, są wysoce niebezpieczne dla zachowania ciągłości genomu. Mechanizm odpowiedzi komórkowej na dwuniciowe pęknięcia DNA jest wciąż badany, wiadomo jednak, że niesie on ze sobą szereg potranslacyjnych modyfikacji histonów takich jak metylacja reszty lizyny 20 histonu H4 (H4K20me2), ubikwitynacje lizyny 15 histonu H2A (H2AK15ub) czy fosforylacje. Takie modyfikacje rozpoznawane są przez domeny czynnika naprawczego 53BP1: domena Tudor oddziałuje z H4K20me2 a UDR z H2AK15ub. 53BP1 bierze udział w wyborze drogi naprawczej dwuniciowego uszkodzenia DNA. Naprawa uszkodzeń DNA komórek, będących w fazie G1/G0, odbywa się głównie na drodze łączenia niehomologicznych zakończeń (NHEJ), promowana przez 53BP1, natomiast komórek będących w fazie S i G2 cyklu komórkowego – rekombinacji homologicznej (HR), związanej z antagonistą 53BP1, białkiem BRCA1. Białka naprawcze, w eksperymentach stosujących do wywołania uszkodzenia DNA promieniowanie jonizujące, UV bądź światło widzialne, tworzą wyraźne ogniska (foci) w miejscu uszkodzenia.Celem niniejszej pracy magisterskiej było zbadanie dynamiki powstawania ognisk białka fuzyjnego EGFP-53BP1 po wywołaniu lokalnego uszkodzenia chromatyny za pomocą światła widzialnego, w zależności od długości fali światła oraz od jego dawki.Doświadczenia przeprowadzano na komórkach żywych, po wprowadzeniu do nich wektora plazmidowego, w celu wywołania przejściowej ekspresji białka fuzyjnego EGFP-53BP1. Po ekspozycji chromatyny na światło widzialne (488 nm – 594 nm), techniką parkowania wiązki lasera, zaobserwowano powstawanie ogniska białka fuzyjnego w miejscu uszkodzenia. Nie zaobserwowano gromadzenia białka EGFP-53BP1, po ekspozycji na światło o długości fali 633 nm. Odnotowano, że maksymalne wartości powierzchni focus białka nie zależą od dawki światła lecz istnieje dawka minimalna wywołująca uszkodzenie. Zauważono również, że EGFP-53BP1 wykazuje co najmniej dwa typy tworzenia ogniska. Ognisko EGFP-53BP1 może nie zanikać do mitozy, a nawet trwać w komórkach potomnych. Pokazano również, że po wywołaniu uszkodzenia, za pomocą światła o długościach fali krótszych niż 561 nm, doszło do znacznego fotoblaknięcia fluorescencji EGFP, przez co fototoksyczność białka fluorescencyjnego mogła wywołać zaburzenia układu. Wobec tego postanowiono podjąć próbę skonstruowania nowego wektora plazmidowego niosącego gen mRFP-53BP1, za pomocą klasycznego klonowania molekularnego.
Dostawca treści:: Repozytorium Uniwersytetu Jagiellońskiego

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Tytuł:: Azurocidin - inactive serine proteinase homolog acting as a multifunctional inflammatory mediator.
Autorzy:: Wątorek, Wiesław
Tematy:: heparin-binding protein
azurocidin
cationic antibacterial protein 37kDa (CAP37); Pokaż więcej
Wydawca:: Polskie Towarzystwo Biochemiczne
Powiązania:: https://bibliotekanauki.pl/articles/1043446.pdf Link otwiera się w nowym oknie
Opis:: Azurocidin, also known as cationic antimicrobial protein 37 kDa (CAP37) or heparin-binding protein (HBP) is an inactive homolog of serine proteinases residing in granulocytes. The ability to cleave peptide bond was lost due to replacement of two of the three residues from the conserved catalytic triad characteristic for serine proteinases. Azurocidin has a broad spectrum of antimicrobial activity, mainly against Gram-negative bacteria. It is also recognized as a multifunctional inflammatory mediator for its contracting effects on endothelial cells causing an increase of vascular permeability, capacity to bind endotoxin and ability to attract monocytes to inflammation sites.
Dostawca treści:: Biblioteka Nauki

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