Affinity Of Analogues Research Articles

Appraising the mitogenicity of insulin analogues relative to human insulin—response to: Weinstein D, Simon M, Yehezkel E, Laron Z, Werner H. Insulin analogues display IGF‐I‐like mitogenic and anti‐apoptotic activity in cultured cancer cells. Diabetes Metab Res Rev 2009; 25(1): 41–9

Interest in mitogenic and potentially carcinogenic effects of insulin and insulin analogues has been renewed by several recent publications that have examined the relationship between cancer and insulin analogues. Actions mediated through the insulin-like growth factor-I receptor in a hyperinsulinaemic state have been implicated mechanistically. Both type 2 diabetes and endogenously elevated insulin-like growth factor-I have been epidemiologically linked to malignancies. Therefore, in vitro mitogenic effects and binding affinities of the various analogues have been analysed. A recent publication by Weinstein et al. studied the in vitro mitogenic and anti-apoptotic activities of insulin analogues, and their conclusion asserts that insulins glargine, detemir, and lispro displayed proliferative and anti-apoptotic effects in a number of malignant cell lines. However, their conclusions are not supported by the data which are not complete and lack clear statistical significance. This data should be interpreted cautiously in light of all other presently available scientific evidence. Prospective, randomized clinical trials will best address any direct relationship between insulin analogues and cancer. Until those studies are designed and completed, clinicians should consider the demonstrated strong benefit of glycaemic control in balance with any alleged risk.

Structure and Ligand Binding Properties of the Epoxidase Component of Styrene Monooxygenase,

Styrene monooxygenase (SMO) is a two-component flavoprotein monooxygenase that transforms styrene to styrene oxide in the first step of the styrene catabolic and detoxification pathway of Pseudomonas putida S12. The crystal structure of the N-terminally histidine-tagged epoxidase component of this system, NSMOA, determined to 2.3 A resolution, indicates the enzyme exists as a homodimer in which each monomer forms two distinct domains. The overall architecture is most similar to that of p-hydroxybenzoate hydroxylase (PHBH), although there are some significant differences in secondary structure. Structural comparisons suggest that a large cavity open to the surface forms the FAD binding site. At the base of this pocket is another cavity that likely represents the styrene binding site. Flavin binding and redox equilibria are tightly coupled such that reduced FAD binds apo NSMOA approximately 8000 times more tightly than the oxidized coenzyme. Equilibrium fluorescence and isothermal titration calorimetry data using benzene as a substrate analogue indicate that the oxidized flavin and substrate analogue binding equilibria of NSMOA are linked such that the binding affinity of each is increased by 60-fold when the enzyme is saturated with the other. A much weaker approximately 2-fold positive cooperative interaction is observed for the linked binding equilibria of benzene and reduced FAD. The low affinity of the substrate analogue for the reduced FAD complex of NSMOA is consistent with a preferred reaction order in which flavin reduction and reaction with oxygen precede the binding of styrene, identifying the apoenzyme structure as the key catalytic resting state of NSMOA poised to bind reduced FAD and initiate the oxygen reaction.

Synthesis and structure–activity relationships of N3-pyridylpyrazinones as corticotropin-releasing factor-1 (CRF 1) receptor antagonists

A series of N 3-pyridylpyrazinones was investigated as corticotropin-releasing factor-1 receptor antagonists. It was observed that the binding affinity of analogues containing a pyridyl group was influenced not only by the substitution pattern on the pyridyl group, but also by the p K a of the pyridyl nitrogen. Analogues containing a novel 6-(difluoromethoxy)-2,5-dimethylpyridin-3-amine group were among the most potent N 3-pyridylpyrazinones synthesized. The synthesis and SAR of N 3-pyridylpyrazinones is described herein.

Synthesis and NMDA receptor affinity of dexoxadrol analogues with modifications in position 4 of the piperidine ring

A series of dexoxadrol (3) analogues with various substituents at position 4 of the piperidine ring has been synthesized and pharmacologically evaluated. Key steps in the synthesis are a hetero-Diels–Alder reaction of the dioxolane-derived imine 10 with Danishefsky's diene 11 and replacement of the p-methoxybenzyl protective group by a Cbz group. All possible diastereomers were synthesized, respectively. It was shown that like-configuration of the ring junction (position 2 of the piperidine ring and position 4 of the dioxolane ring) and axial orientation of the C-4 substituent are crucial for high NMDA receptor affinity. 2-(2,2-Diphenyl-1,3-dioxolan-4-yl)piperidine with a hydroxy moiety at position 4 (17d, WMS-2508, Ki = 44 nM) represents the most potent NMDA antagonist with high selectivity against σ1 and σ2 receptors, and the polyamine binding site of the NMDA receptor. The high sensitivity of the receptor ligand interaction became evident since methyl ethers with unlike-configuration of the ring junction (19a, 19b) prefer the σ1 receptor with high selectivity.

A Fluorescent GTP Analogue as a Single Molecule Fluorescence Label of Microtubules

Microtubules are cytoskeletal polymers which play a role in cell division, cell mechanics, and intracellular transport. Dynamic studies of microtubule function make use of fluorescent labels via antibodies, paclitaxel, and direct attachment to the tubulin protein. However, these labels suffer from drawbacks such as transient labeling, occlusion of functional sites on the microtubule surface, or structural non-specificity. Here we report a new, complementary fluorescent labeling technique that avoids these drawbacks. A fluorescently modified GTP analogue is used to polymerize microtubules from tubulin dimers. This GTP analogue binds selectively to the exchangeable GTP-binding site (E-site) on the tubulin dimer, which is available only during polymerization. The E-site affinity of this GTP analogue is about 100 fold weaker than that of GTP. Because this labeling technique places a bright fluorophore at a defined location within the microtubule lattice, it may facilitate observations of microtubule dynamics with increased precision.

Parabolic Character Sheaves, III

The main purpose of this paper is to define a class of sim- ple perverse sheaves (called character sheaves) on certain ind-varieties associated to a loop group. This has applications to a geometric con- struction of certain affine Hecke algebras with unequal parameters (an affine analogue ofanother construction by the author), as will be shown elsewhere.

Linear interaction energy approximation for binding affinities of nevirapine and HEPT analogues with HIV-1 reverse transcriptase

The binding affinities and binding mechanism of nevirapine and HEPT analogues with HIV-1 reverse transcriptase (HIV-1RT) have been studied in this paper with a recently proposed linear interaction energy method based on a surface generalised Born continuum solvent model (LIE–SGB). Various LIE–SGB fitting schemes are presented and discussed on this relatively large binding set, consisting of a total of more than 50 ligands. For a training subset of 40 ligands (20 nevirapine and 20 HEPT analogues), the LIE–SGB method gives an RMS error (RMSE) of 0.89 kcal/mol with a correlation coefficient of 0.74. The leave-one-out cross validation results also show an encouraging RMSE of 1.00 kcal/mol, with a correlation coefficient of 0.69. The further blind tests on seven mostly high-potent candidates (not originally in the training subset) also show reasonable accuracies. The binding mechanism of this HIV-1RT binding set is found to be mainly driven by van der Waals interactions (i.e. a good geometrical fit is important) and the net loss of ligand cavity energies (i.e. the burial of solvent accessible surface area is favourable). The net electrostatic interactions, however, are found to be anti-binding. A secondary amide indicator is found to be necessary for nevirapine analogues to account for the deficiencies in quantum partial charges, and it is also shown that it represents a critical -type hydrogen bond between the secondary amide fragment of nevirapine analogues and the phenyl ring of Tyr188A residue, which explains their otherwise surprising binding affinities. More quantum charge fittings, with the protein environment included, gave similar results, indicating that an out-of-plane polarisability might be needed to fully capture this -type hydrogen bond in classical force fields. Finally, six new ligands are designed for optimal binding based on our predictions for further experimental validations.

Uptake of 3-[125I]iodo-α-methyl-l-tyrosine into colon cancer DLD-1 cells: characterization and inhibitory effect of natural amino acids and amino acid-like drugs

We examined 3-[(123)I]iodo-alpha-methyl-L-tyrosine ([(123)I]IMT) uptake and inhibition by amino acids and amino acid-like drugs in the human DLD-1 colon cancer cell line, to discuss correlation between the inhibition effect and structure. Expression of relevant neutral amino acid transporters was examined by real-time PCR with DLD-1 cells. The time course of [(125)I]IMT uptake, contributions of transport systems, concentration dependence and inhibition effects by amino acids and amino acid-like drugs (1 mM) on [(125)I]IMT uptake were examined. Expression of system L (4F2hc, LAT1 and LAT2), system A (ATA1, ATA2) and system ASC (ASCT1) was strongly detected; system L (LAT3, LAT4) and MCT8 were weakly detected; and B(0)AT was not detected. [(125)I]IMT uptake in DLD-1 cells involved Na(+)-independent system L primarily and Na(+)-dependent system(s). Uptake of [(125)I]IMT in Na(+)-free buffer followed Michaelis-Menten kinetics, with a K(m) of 78 microM and V(max) of 333 pmol/10(6) cells per minute. Neutral D- and L-amino acids with branched or aromatic large side chains inhibited [(125)I]IMT uptake. Tyrosine analogues, tryptophan analogues, L-phenylalanine and p-halogeno-L-phenylalanines, and gamma amino acids [including 3,4-dihydroxy-L-phenylalanine (L-DOPA), DL-threo-beta-(3,4-dihydroxyphenyl)serine (DOPS), 4-[bis(2-chloroethyl)amino]-L-phenylalanine and 1-(aminomethyl)-cyclohexaneacetic acid] strongly inhibited [(125)I]IMT uptake, but L-tyrosine methyl ester and R(+)/S(-)-baclofen weakly inhibited uptake. The substrates of system ASC and A did not inhibit [(125)I]IMT uptake except L-serine and D/L-cysteine. [(125)I]IMT uptake in DLD-1 cells involves mostly LAT1 and its substrates' (including amino acid-like drugs derived from tyrosine, tryptophan and phenylalanine) affinity to transport via LAT1. Whether transport of gamma amino acid analogues is involved in LAT1 depends on the structure of the group corresponding to the amino acid residue. Beta-hydroxylation may confer reduction of transport affinity of tyrosine analogues via LAT1.

Docking of sialic acid analogues against influenza A hemagglutinin: a correlational study between experimentally measured and computationally estimated affinities

A molecular docking tool of AutoDock3.05 was evaluated for its ability to reproduce experimentally determined affinities of various sialic acid analogues toward hemagglutinin of influenza A virus. With the exception of those with a C6-modified glycerol side chain, the experimental binding affinities of most sialic acid analogues (C2, C4 and C5-substituted) determined by viral hemadsorption inhibition assay, hemagglutination inhibition assay and nuclear magnetic resonance correlated well with the computationally estimated free energy of binding. Sialic acid analogues with modified glycerol side chains showed only poor correlation between the experimentally determined hemagglutinin inhibitor affinities and AutoDock3.05 scores, suggesting high mobility of the glutamic acid side chain at the glycerol binding pocket, which is difficult to simulate using a flexi-rigid molecular docking approach. In conclusion, except for some glycerol-substituted sialic acid analogues, the results showed the effectiveness of AutoDock3.05 searching and scoring functions in estimating affinities of sialic acid analogues toward influenza A hemagglutinin, making it a reliable tool for screening a database of virtually designed sialic acid analogues for hemagglutinin inhibitors.

Localization of g-modules on the affine Grassmannian

We consider the category of modules over the affine Kac-Moody algebra ĝ of critical level with regular central character. In our previous paper we conjectured that this category is equivalent to the category of Hecke eigen-D-modules on the affine Grassmannian G((t))/G[[t]]. This conjecture was motivated by our proposal for a local geometric Langlands correspondence. In this paper we prove this conjecture for the corresponding I 0 equivariant categories, where I 0 is the radical of the Iwahori subgroup of G((t)). Our result may be viewed as an affine analogue of the equivalence of categories of g-modules and D-modules on the flag variety G/B, due to Beilinson-Bernstein and Brylinski-Kashiwara.

Structural basis of the affinity for oligomannosides and analogs displayed by BC2L-A, a Burkholderia cenocepacia soluble lectin

The opportunistic pathogen Burkholderia cenocepacia contains three soluble carbohydrate-binding proteins, related to the fucose-binding lectin PA-IIL from Pseudomonas aeruginosa. All contain a PA-IIL-like domain and two of them have an additional N-terminal domain that displays no sequence similarities with known proteins. Printed arrays screening performed on the shortest one, B. cenocepacia lectin A (BC2L-A), demonstrated the strict specificity for oligomannose-type N-glycan structures (Lameignere E, Malinovská L, Sláviková M, Duchaud E, Mitchell EP, Varrot A, Sedo O, Imberty A, Wimmerová M. 2008. Structural basis for mannose recognition by a lectin from opportunistic bacteria Burkholderia cenocepacia. Biochem J. 411:307-318.). The disaccharides alphaMan1-2Man, alphaMan1-3Man, and alphaMan1-6Man and the trisaccharide alphaMan1-3(alphaMan1-6)Man were tested by titration microcalorimetry in order to evaluate their affinity for BC2L-A in solution and to characterize the thermodynamics of the binding. Oligomannose analogs presenting two mannoside residues separated by either flexible or rigid spacer were also tested. Only the rigid one yields to high affinity binding with a fast kinetics of clustering, while the flexible analog and the trimannoside display moderate affinities and no clustering effect on short time scale. The crystal structures of BC2L-A have been obtained in complex with alphaMan1-3Man disaccharide and alphaMan1(alphaMan1-6)-3Man trisaccharide. The lengthy time required for the co-crystallization with the trisaccharide allowed for the formation of cluster since in the BC2L-A-trimannose complex solved at 1.1 A resolution, the sugar creates a bridge between two adjacent dimers, yielding to molecular strings. AFM experiments were performed in order to visualize the filaments formed in solution by this type of interaction.

Role of Intramembrane Polar Residues in the YgfO Xanthine Permease: HIS-31 AND ASN-93 ARE CRUCIAL FOR AFFINITY AND SPECIFICITY, AND ASP-304 AND GLU-272 ARE IRREPLACEABLE

Using the YgfO xanthine permease of Escherichia coli as a bacterial model for the study of the evolutionarily ubiquitous nucleobase-ascorbate transporter (NAT/NCS2) family, we performed a systematic Cys-scanning and site-directed mutagenesis of 14 putatively charged (Asp, Glu, His, Lys, or Arg) and 7 highly polar (Gln or Asn) residues that are predicted to lie in transmembrane helices (TMs). Of 21 single-Cys mutants engineered in the background of a functional YgfO devoid of Cys residues (C-less), only four are inactive or have marginal activity (H31C, N93C, E272C, D304C). The 4 residues are conserved throughout the family in TM1 (His-31), TM3 (Asn-93/Ser/Thr), TM8 (Glu-272), and putative TM9a (Asp-304/Asn/Glu). Extensive site-directed mutagenesis in wild-type background showed that H31N and H31Q have high activity and affinity for xanthine but H31Q recognizes novel purine bases and analogues, whereas H31C and H31L have impaired affinity for xanthine and analogues, and H31K or H31R impairs expression in the membrane. N93S and N93A are highly active but more promiscuous for recognition of analogues at the imidazole moiety of substrate, N93D has low activity, N93T has low affinity for xanthine or analogues, and N93Q or N93C is inactive. All mutants replacing Glu-272 or Asp-304, including E272D, E272Q, D304E, and D304N, are inactive, although expressed to high levels in the membrane. Finally, one of the 17 assayable single-Cys mutants, Q258C, was sensitive to inactivation by N-ethylmaleimide. The findings suggest that polar residues important for the function of YgfO cluster in TMs 1, 3, 8 and 9a.

Analysis of the mechanism by which tryptophan analogs inhibit human myeloperoxidase

Myeloperoxidase (MPO) catalyzes the formation of oxidants that have been implicated in the pathogenesis of various diseases, including cardiovascular and pulmonary diseases and cancer. Inhibition of MPO oxidant-generating activity represents an attractive target for preventing the progression of inflammatory conditions. Peroxidation and chlorination catalytic activity were utilized to screen for the most effective tryptophan analog that inhibits MPO. Rapid kinetic measurements were performed to determine the mechanisms through which these compounds inhibit the catalytic activity of MPO. Substituents on the amino and carboxyl termini of tryptophan enhance its affinity toward MPO compared to a substituent on the indole ring. Hydrogen-bond donor capabilities and a positive charge on the amino group are not required for MPO inhibition. Hydroxyl-containing indoles did not inhibit MPO H 2O 2-consumption activity. Elimination of the negative charge from the carboxyl terminus by introducing a hydrophobic character significantly enhanced tryptophan analog affinity for MPO and improved its inhibitory properties. Further mechanistic studies indicated that indole compounds inhibited MPO activity through the accumulation of compound II, an inactive MPO intermediate. Our results show that specific structural features of tryptophan analogs are involved in increasing the affinity for MPO and providing a significantly greater inhibition of MPO's catalytic activities.

Interactions of the Escherichia coli DnaB-DnaC protein complex with nucleotide cofactors. 1. Allosteric conformational transitions of the complex.

Interactions of nucleotide cofactors with both protein components of the Escherichia coli DnaB helicase complex with the replication factor, the DnaC protein, have been examined using MANT-nucleotide analogues. At saturation, in all examined stationary complexes, including the binary, DnaB-DnaC, and tertiary, DnaB-DnaC-ssDNA, complexes, the helicase binds six cofactor molecules. Thus, protein-protein and protein-DNA interactions do not affect the maximum stoichiometry of the helicase-nucleotide interactions. The single-stranded DNA dramatically increases the ATP analogue affinity, while it has little effect on the affinity of the NDP analogues, indicating that stationary complexes reflect allosteric interactions between the DNA- and NTP-binding site prior to the cofactor hydrolysis step and subsequent to product release. In the binary complex, the DnaC protein diminishes the intrinsic affinity and increases the negative cooperativity in the cofactor binding to the helicase; an opposite effect of the protein on the cofactor-helicase interactions occurs in the tertiary complex. The DnaC protein retains its nucleotide binding capability in the binary and tertiary complexes with the helicase. Surprisingly, the DnaC protein-nucleotide interactions, in the binary and tertiary complexes, are characterized by positive cooperativity. The DnaC assembles on the helicase as a hexamer, which exists in two conformational states and undergoes an allosteric transition, induced by the cofactor. Cooperativity of the allosteric transition depends on the structure of the phosphate group of the nucleotide. The significance of the results for the DnaB-DnaC complex activities is discussed.

Towards Coleoptera-specific high-throughput screening systems for compounds with ecdysone activity: development of EcR reporter assays using weevil ( Anthonomus grandis)-derived cell lines and in silico analysis of ligand binding to A. grandis EcR ligand-binding pocket

Molting in insects is regulated by ecdysteroids and juvenile hormones. Several synthetic non-steroidal ecdysone agonists are on the market as insecticides. These ecdysone agonists are dibenzoylhydrazine (DBH) analogue compounds that manifest their toxicity via interaction with the ecdysone receptor (EcR). Of the four commercial available ecdysone agonists, three (tebufenozide, methoxyfenozide and chromafenozide) are highly lepidopteran specific, one (halofenozide) is used to control coleopteran and lepidopteran insects in turf and ornamentals. However, compared to the very high binding affinity of these DBH analogues to lepidopteran EcRs, halofenozide has a low binding affinity for coleopteran EcRs. For the discovery of ecdysone agonists that target non-lepidopteran insect groups, efficient screening systems that are based on the activation of the EcR are needed. We report here the development and evaluation of two coleopteran-specific reporter-based screening systems to discover and evaluate ecdysone agonists. The screening systems are based on the cell lines BRL-AG-3A and BRL-AG-3C that are derived from the weevil Anthonomus grandis, which can be efficiently transduced with an EcR reporter cassette for evaluation of induction of reporter activity by ecdysone agonists. We also cloned the almost full length coding sequence of EcR expressed in the cell line BRL-AG-3C and used it to make an initial in silico 3D-model of its ligand-binding pocket docked with ponasterone A and tebufenozide.

On a robust and efficient maximum depth estimator

The best breakdown point robustness is one of the most outstanding features of the univariate median. For this robustness property, the median, however, has to pay the price of a low efficiency at normal and other light-tailed models. Affine equivariant multivariate analogues of the univariate median with high breakdown points were constructed in the past two decades. For the high breakdown robustness, most of them also have to sacrifice their efficiency at normal and other models, nevertheless. The affine equivariant maximum depth estimator proposed and studied in this paper turns out to be an exception. Like the univariate median, it also possesses a highest breakdown point among all its multivariate competitors. Unlike the univariate median, it is also highly efficient relative to the sample mean at normal and various other distributions, overcoming the vital low-efficiency shortcoming of the univariate and other multivariate generalized medians. The paper also studies the asymptotics of the estimator and establishes its limit distribution without symmetry and other strong assumptions that are typically imposed on the underlying distribution.

Bone mineral affinity influences the distribution of a bisphosphonate and a lower affinity analogue in vivo

Bone mineral affinity influences the distribution of a bisphosphonate and a lower affinity analogue in vivo

Membrane binding and insertion of the GRP1 PH and Epsin ENTH domains

Phosphoinositide (PI)‐binding domains recruit a variety of signaling and trafficking proteins to the distinct intracellular membranes. In the plasma membrane, PtdIns(4,5)P2 and PtdIns(3,4,5)P3 lipids are recognized by the PH (pleckstrin homology) and ENTH (Epsin N‐terminal homology) domains. Here, the molecular basis of membrane anchoring and penetration by the PH domain of general receptor for phosphoinositides isoform 1 (GRP1) and Epsin ENTH domain is detailed. The specificities and binding affinities for PI‐containing SUVs and soluble metabolically‐stabilized analogues of PIs, insertion into monolayers and bilayers, and regulation of the lipid binding and membrane penetration by pH are investigated using nuclear magnetic resonance spectroscopy, surface plasmon resonance, liposome‐binding and surface tension experiments. The significance of the pH sensitivity and the effect of the acidic and basic media on the PI recognition, hydrophobic insertion and non‐specific electrostatic contacts is established.

Application of the linear interaction energy method for rational design of artemisinin analogues as haeme polymerisation inhibitors

The anti-malarial activity of artemisinin-derived drugs appears to be mediated by an interaction of the drug's endoperoxide bridge with intra-parasitic haeme. The binding affinity of artemisinin analogues with haeme were computed using linear interaction energy with a surface generalised Born (LIE-SGB) continuum solvation model. Low levels of root mean square error (0.348 and 0.415 kcal/mol) as well as significant correlation coefficients (r 2 = 0.868 and 0.892) between the experimental and predicted free energy of binding (FEB) based on molecular dynamics and hybrid Monte Carlo sampling techniques establish the SGB-LIE method as an efficient tool for generating more potent inhibitors of haeme polymerisation inhibition.

From precursor to peptide: Evidence for endomorphin biosynthesis?

Event Abstract Back to Event From precursor to peptide: Evidence for endomorphin biosynthesis? Jayapalreddy Mallareddy1, Balazs Csibrany1, Attila Keresztes1 and Géza Tóth1* 1 Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Hungary Because of their high affinity, selectivity and agonist properties, endomorphins were proposed to be the endogenous ligands of the -opioid receptors. In spite of recent advances, the biosynthetic pathway of endomorphins is still unclear. Recent findings suggested that endomorphin-2 may be produced from a human sulfate transporter protein in consecutive enzymatic reactions. Many biologically active neuropeptides and peptide hormones were shown to be synthesized from inactive glycine-extended precursors, which require a carboxy-terminal posttranslational amidation for biological activity. This reaction is catalyzed by a consecutive action of peptidylglycine-α-hydroxylating monooxygenase (PHM) and peptidylamidoglycolate lyase (PAL). These two enzymes are part of the peptidylglycine α-amidating monooxygenase (PAM), a bifunctional, integral membrane-bound enzyme machinery. In attempt to elicit the hypothesis that endomorphin-2 may be produced from the sulfate transporter precursor protein by the activation of the PAM enzyme system we designed and performed a series of biochemical experiments. Biological matrices, serum and brain homogenates were prepared for the in vitro metabolic studies. Endomorphin-2, Gly5-extended endomorphin-2 as well as their Dmt1-containing analogs were synthesized using SPPS methods. The biodegradation of the Gly5-extended endomorphin-2 was monitored by RP-HPLC and MALDI-TOF mass spectroscopy. Additionally, the -and -opioid receptor binding affinities of the aforementioned analogs were tested. Conference: 12th Meeting of the Hungarian Neuroscience Society, Budapest, Hungary, 22 Jan - 24 Jan, 2009. Presentation Type: Poster Presentation Topic: Developmental neurobiology and subcortical functions Citation: Mallareddy J, Csibrany B, Keresztes A and Tóth G (2009). From precursor to peptide: Evidence for endomorphin biosynthesis?. Front. Syst. Neurosci. Conference Abstract: 12th Meeting of the Hungarian Neuroscience Society. doi: 10.3389/conf.neuro.01.2009.04.245 Copyright: The abstracts in this collection have not been subject to any Frontiers peer review or checks, and are not endorsed by Frontiers. They are made available through the Frontiers publishing platform as a service to conference organizers and presenters. The copyright in the individual abstracts is owned by the author of each abstract or his/her employer unless otherwise stated. Each abstract, as well as the collection of abstracts, are published under a Creative Commons CC-BY 4.0 (attribution) licence (https://creativecommons.org/licenses/by/4.0/) and may thus be reproduced, translated, adapted and be the subject of derivative works provided the authors and Frontiers are attributed. For Frontiers’ terms and conditions please see https://www.frontiersin.org/legal/terms-and-conditions. Received: 13 Mar 2009; Published Online: 13 Mar 2009. * Correspondence: Géza Tóth, Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary, geza@brc.hu Login Required This action requires you to be registered with Frontiers and logged in. To register or login click here. Abstract Info Abstract The Authors in Frontiers Jayapalreddy Mallareddy Balazs Csibrany Attila Keresztes Géza Tóth Google Jayapalreddy Mallareddy Balazs Csibrany Attila Keresztes Géza Tóth Google Scholar Jayapalreddy Mallareddy Balazs Csibrany Attila Keresztes Géza Tóth PubMed Jayapalreddy Mallareddy Balazs Csibrany Attila Keresztes Géza Tóth Related Article in Frontiers Google Scholar PubMed Abstract Close Back to top Javascript is disabled. Please enable Javascript in your browser settings in order to see all the content on this page.