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Wyszukujesz frazę "membrane receptor" wg kryterium: Temat


Wyświetlanie 1-10 z 10
Tytuł:
Sensitivity analysis of mathematical models of signalling pathways
Autorzy:
Charzynska, A.
Nalecz, A.
Rybinski, M.
Gambin, A.
Powiązania:
https://bibliotekanauki.pl/articles/80205.pdf
Data publikacji:
2012
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Tematy:
membrane receptor
differential equation
stochastic model
modelling
sensitivity analysis
mathematical model
signalling pathway
dynamic behaviour
Źródło:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2012, 93, 3
0860-7796
Pojawia się w:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Regulation of steroidogenic function of mouse Leydig cells: G-coupled membrane estrogen receptor and peroxisome proliferator-activated receptor partnership
Autorzy:
Gorowska-Wojtowicz, E.
Dutka, P.
Kudrycka, M.
Pawlicki, P.
Milon, A.
Plachno, B.J.
Tworzydlo, W.
Pardyak, L.
Kaminska, A.
Hejmej, A.
Bilinska, B.
Kotula-Balak, M.
Powiązania:
https://bibliotekanauki.pl/articles/70604.pdf
Data publikacji:
2018
Wydawca:
Polskie Towarzystwo Fizjologiczne
Tematy:
Leydig cell
steroidogenic function
mice
mouse
G-coupled membrane estrogen receptor
peroxisome proliferator-activated receptor
lutropin
cholesterol level
steroidogenesis
Źródło:
Journal of Physiology and Pharmacology; 2018, 69, 3
0867-5910
Pojawia się w:
Journal of Physiology and Pharmacology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Transmembrane segment M2 of glycine receptor as a model system for the pore-forming structure of ion channels.
Autorzy:
Bednarczyk, Piotr
Szewczyk, Adam
Dołowy, Krzysztof
Powiązania:
https://bibliotekanauki.pl/articles/1043689.pdf
Data publikacji:
2002
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
black lipid membrane
ion channels
glycine receptor
Opis:
The glycine receptor belongs to the ligand-gated ion channel superfamily. It is a chloride conducting channel composed of four transmembrane domains. It was previously shown that the second transmembrane domain (M2) of the glycine receptor forms an ion conduction pathway throught lipid bilayers. The amino-acid sequence of the transmembrane segment M2 of the glycine receptor has a high homology to all receptors of the ligand-gated ion channel superfamily. In our report, we have used a synthetic M2 peptide. It was incorporated into a planar membrane of known lipid composition and currents induced by M2 were measured by the Black Lipid Membrane technique. When the planar lipid bilayer was composed of 75% phosphatidylethanolamine and 25% phosphatidylserine, the reversal potential measured in a 150/600 mM KCl (cis/trans) gradient was -19 mV suggesting that the examined pore was preferential to anions, PK/PCl = 0.25. In contrast, when 75% phosphatidylserine and 25% phosphatidylethanolamine was used, the reversal potential was +20 mV and the pore was preferential to cations, PK/PCl = 4.36. Single-channel currents were recorded with two predominant amplitudes corresponding to the main-conductance and sub-conductance states. Both conductance states (about 12 pS and 30 pS) were measured in a symmetric solution of 50 mM KCl. The observed single-channel properties suggest that the selectivity and conductance of the pore formed by the M2 peptide of the glycine receptor depend on the lipid composition of the planar bilayer.
Źródło:
Acta Biochimica Polonica; 2002, 49, 4; 869-875
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Targets for majority of drugs: G protein-coupled receptors - their structure and interaction with bioligands
Autorzy:
Ciarkowski, J.
Czaplewski, C.
Pasenkiewicz-Gierula, M.
Powiązania:
https://bibliotekanauki.pl/articles/1953953.pdf
Data publikacji:
1998
Wydawca:
Politechnika Gdańska
Tematy:
G protein-coupled receptor
molecular modelling
GPCR/bioligand interaction
molecular dynamics
membrane
Opis:
G protein-coupled receptors (GPCRs) are the most frequent targets for many drugs. They form the largest superfamily of integral membrane proteins, of which more than 1000 members have the following common features: (i) All GPCRs form 7 hydrophobic a-helices of length ~38A (25 amino acids, 7 turns) along a single chain. The consecutive helices alternatively cross the membrane, starting from the extracellular side, so that they form a heptahelical transmembrane domain interwoven with 6 loops, of which the even ones plus the N-terminus create the receptor's extracellular domain while the odd ones plus the C-terminus form its intracellular domain. (ii) All GPCRs are stimulated by diverse extracellular (primary) signals. (iii) Stimulated GPCRs convey the primary signals via their transmembrane and intracellular domains to the cytosolic peripheral heterotrimeric GTP-binding proteins (G proteins), mediating the signal's further transduction to various cellular second messenger systems. A current status of structural studies on GPCRs, consisting of low ~7.5A resolution experimental structures and supplementary molecular modeling, is outlined. Subsequently, some results of authors' own work on studying essential interactions of the V2 vasopressin renal receptor (V2R) with its agonist [Arg8]Vasopressin (AVP) and selected antagonists are presented, as well as their possible impact on the biological signal transduction is discussed. Finally, perspectives for future developments are sketched.
Źródło:
TASK Quarterly. Scientific Bulletin of Academic Computer Centre in Gdansk; 1998, 2, 4; 583-599
1428-6394
Pojawia się w:
TASK Quarterly. Scientific Bulletin of Academic Computer Centre in Gdansk
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The retromer: a multiprotein complex mediating multiple functions
Autorzy:
Bayle, V.
Zelazny, E.
Miege, C.
Fobis-Loisy, I.
Jaillais, Y.
Gaude, T.
Powiązania:
https://bibliotekanauki.pl/articles/80162.pdf
Data publikacji:
2013
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Tematy:
conference
multicellular organism
signalling molecule
hormone receptor
ion channel
retromer
protein complex
membrane
Źródło:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2013, 94, 3
0860-7796
Pojawia się w:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Guarding the gates: stomatal responses to pathogens
Autorzy:
Bourdais, G.
Zhou, J.
Robatzek, S.
Powiązania:
https://bibliotekanauki.pl/articles/79964.pdf
Data publikacji:
2013
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Tematy:
conference
stomatal response
pathogen
plasma membrane
FLS2 receptor
plant immunity
flagellin
stomatal immunity
Źródło:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2013, 94, 2
0860-7796
Pojawia się w:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Age dependent changes of insulin receptors in rat tissues
Autorzy:
Torlinska, T.
Mackowiak, P.
Nogowski, L.
Hryniewiecki, T.
Witmanowski, H.
Perz, M.
Madry, E.
Nowak, K.M.
Powiązania:
https://bibliotekanauki.pl/articles/69323.pdf
Data publikacji:
2000
Wydawca:
Polskie Towarzystwo Fizjologiczne
Tematy:
plasma membrane
hyperglycemia
hyperinsulinemia
aging
heart
insulin receptor
liver
rat
tissue
skeletal muscle
hormone
Źródło:
Journal of Physiology and Pharmacology; 2000, 51, 4,2
0867-5910
Pojawia się w:
Journal of Physiology and Pharmacology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
A brief overview of the process of the elucidation of GnRH structure (1971)
Autorzy:
Kochman, K.
Powiązania:
https://bibliotekanauki.pl/articles/80024.pdf
Data publikacji:
2012
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Tematy:
luteinizing hormone
follicle stimulating hormone
receptor protein
protein G
cell membrane
hypothalamic peptide
adrenocorticotrophin
radioimmunoassay
central nervous system
gonadotrophin releasing hormone
receptor
neuroendocrinology
Źródło:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2012, 93, 4
0860-7796
Pojawia się w:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Effect of hypothermia on the insulin - receptor interaction in adipose plasma membranes
Autorzy:
Torlinska, T
Mackowiak, P.
Nogowski, L.
Kozlik, J.
Powiązania:
https://bibliotekanauki.pl/articles/70049.pdf
Data publikacji:
1995
Wydawca:
Polskie Towarzystwo Fizjologiczne
Tematy:
lipolysis
receptor
insulin
hypothermia
fat cell
lipid metabolism
epididymal adipose tissue
carbohydrate
rat
normothermia
hypoinsulinemia
adipose plasma membrane
Źródło:
Journal of Physiology and Pharmacology; 1995, 46, 3
0867-5910
Pojawia się w:
Journal of Physiology and Pharmacology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Binding of Aedes aegypti trypsin modulating oostatic factor [Aea-TMOF] to its receptor stimulates phosphorylation and protease processing of gut-membrane proteins
Autorzy:
Borovsky, D.
Hamdaoui, A.
Powiązania:
https://bibliotekanauki.pl/articles/55079.pdf
Data publikacji:
2008
Wydawca:
Sieć Badawcza Łukasiewicz - Instytut Przemysłu Organicznego
Tematy:
protease processing
Aedes aegypti
electrophoresis
trypsin modulating oostatic factor
phosphorylation
mosquito
insect
larva
gut-membrane protein
fluorography
gut receptor
Opis:
The binding of TMOF to its gut receptor was followed by incubating guts removed from male and female Aedes aegypti. TMOF at physiological concentrations, in the presence of [γ32P]ATP, causes phosphorylation and release of gut-membrane protein (45 kDa) that is further processed by proteolysis. In the presence of protease inhibitors only the 45 kDa protein was released. The phosphorylation and processing of the 45 kDa protein does not happen in the absence of TMOF. Both larvae and adult guts release the protein in the presence of TMOF. Male Ae. aegypti do not synthesize trypsin in their gut and do not release the 45 kDa protein in the presence of TMOF because a TMOF receptor is probably absent. Homogenized guts do not release the 45 kDa protein, indicating that the protease processing or the ecto-protein kinase activity is probably reduced after breaking the tissue. The 45 kDa phosphorylated protein can be dephosphorylated by alkaline phosphatase and protein phosphatase, indicating that the phosphate group is covalently linked to either a serine or a tyrosine moiety. This is the first report that shows that in insects, binding of a peptide hormone activates its receptor by proteolysis.
Źródło:
Pestycydy; 2008, 1-2; 13-25
0208-8703
Pojawia się w:
Pestycydy
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-10 z 10

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