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2. Conformational Changes that occur in Heme and Globin upon Temperature Variations and Normobaric Hypoxia

Author

Sergei N. Orlov, L. I. Deev, Georgy V. Maksimov, O. G. Luneva, and O. V. Slatinskaya

Subjects
0301 basic medicine, Hematoporphyrin, 030102 biochemistry & molecular biology, Biophysics, chemistry.chemical_element, Oxygen, 03 medical and health sciences, chemistry.chemical_compound, 030104 developmental biology, chemistry, Globin, Hemoglobin, Heme, Oxygen binding, Histidine, Pyrrole
Abstract

—Using Raman spectroscopy (RS) approach in a spectral range of 1000–3000 cm–1 were used to study the conformational and structural changes that arise in the heme group and globin moiety of hemoglobin in human red blood cells at various temperatures and oxygen contents. In hypoxia, the hemoglobin conformation was shown to change as a result of the increasing contribution of hematoporphyrin pyrrole rings and vibrational motions of vinyl groups. Modifications were additionally detected in the contributions of symmetric and asymmetric vibrations of the CH2 and CH3 radicals of histidine (2850, 2860, and 2900 cm–1) and lysine (2880 and 2860 cm–1) residues. The mechanisms of oxygen binding are discussed for hemoglobin located in the submembrane region and cytoplasm of the cell.

Published
2020
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3. Effect of Dinitrosyl Iron Complex on Albumin Conformation

Author

Elvin S. Allakhverdiev, O. G. Luneva, Georgy V. Maksimov, Aleksey D. Ivanov, Georgy V. Tsoraev, Tamila Martynyuk, Alexander Yusipovich, and O. V. Rodnenkov

Subjects
Adult, Male, Protein Conformation, Iron, Biophysics, Biochemistry, Biochemistry, Genetics and Molecular Biology (miscellaneous), chemistry.chemical_compound, Blood plasma, medicine, Animals, Humans, Bovine serum albumin, Serum Albumin, Aged, biology, Chemistry, Nitrosylation, Tryptophan, Albumin, Electron Spin Resonance Spectroscopy, Serum Albumin, Bovine, General Medicine, Glutathione, Middle Aged, Human serum albumin, Spectrometry, Fluorescence, biology.protein, Cattle, Nitrogen Oxides, Geriatrics and Gerontology, Cysteine, medicine.drug
Abstract

Binding of dinitrosyl iron complex (DNIC) to albumin was studied using time-resolved fluorescence (TRF) and electron spin resonance (ESR) spectroscopy. It was found that the fluorescence lifetime of bovine serum albumin (BSA) and human serum albumin (HSA) decreases with binding and depends on DNIC concentration. The observed biexponential pattern of the BSA tryptophan (Trp) fluorescence decay is explained by the presence of two tryptophan residues in the protein molecule. We believe that DNIC forms stable complexes with the cysteine (Cys34) residue in the domain I of albumin. It was shown that the lifetime of albumin tryptophan fluorescence decreased during co-incubation of BSA with DNICs and glutathione. Effects of DNIC on the binding of specific spin-labeled fatty acids with albumin in human blood plasma were studied in vitro. The presence of DNIC in blood plasma does not change conformation of albumin domains II and III. We suggest that the most possible interaction between DNICs and albumin is the formation of a complex; and nitrosylation of the cysteine residue in the albumin domain I occurs without the changes in albumin conformation.

Published
2021

4. Oxygen radicals and cytoplasm zoning in growing lily pollen tubes

Author

Alexandra Podolyan, Maria Breygina, and O. G. Luneva

Subjects
Membrane potential, chemistry.chemical_compound, Chemistry, Superoxide, Cytoplasm, Organelle, Biophysics, food and beverages, Pollen tube, Depolarization, Tip growth, Membrane transport
Abstract

Recently redox-regulation of tip growth has been extensively studied, but differential sensitivity of growing cells to particular ROS and their subcellular localization is still unclear. Here we used specific dyes to provide mapping of H2O2 and O•2− in short and long pollen tubes. We found apical accumulation of H2O2 and H2O2–producing organelles in the shank that were not colocalized with O•2−-producing mitochondria. Differential modulation of ROS content of the germination medium affected both growth speed and pollen tube morphology. Oxygen radicals affected ionic zoning: membrane potential and pH gradients. OH• caused depolarization all along the tube while O•2− provoked hyperpolarization and cytoplasm alkalinization. O•2− accelerated growth and reduced tube diameter, indicating that this ROS can be considered as pollen tube growth stimulator along with H2O2. Serious structural disturbances were observed upon exposure to OH• and H2O2 and O•2− quencher MnTMPP: pollen tube growth slowed down and ballooned tips formed in both cases, but in the presence of OH• membrane transport and organelle distribution was affected as well. OH•, thus, can be considered as a negative influence on pollen tubes which, presumably, have mechanisms for leveling it. The assumption was confirmed by EPR spectroscopy: pollen tubes actively reduce OH• content in the incubation medium.

Published
2020
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5. Oxygen radicals and cytoplasm zoning in growing lily pollen tubes

Author

Maria Breygina, Ekaterina Klimenko, O. G. Luneva, and Alexandra Podolyan

Subjects
0106 biological sciences, Membrane potential, Cytoplasm, food and beverages, chemistry.chemical_element, Depolarization, Cell Biology, Plant Science, Hydrogen Peroxide, Pollen Tube, Membrane transport, Hyperpolarization (biology), Biology, 01 natural sciences, Oxygen, chemistry, Biophysics, Pollen tube, Tip growth, Lilium, Reactive Oxygen Species, 010606 plant biology & botany
Abstract

Differential modulation of ROS content of the microenvironment (O ¯/MnTMPP/OH·) affects growth speed and morphology in lily pollen tubes. Oxygen radicals influence ionic zoning: membrane potential and pH gradients. Recently, redox-regulation of tip growth has been extensively studied, but differential sensitivity of growing cells to particular ROS and their subcellular localization is still unclear. Here, we used specific dyes to provide mapping of H2O2 and O·2¯ in short and long pollen tubes. We found apical accumulation of H2O2 and H2O2-producing organelles in the shank that were not colocalized with O·2¯-producing mitochondria. Differential modulation of ROS content of the germination medium affected both growth speed and pollen tube morphology. Oxygen radicals affected ionic zoning: membrane potential and pH gradients. OH· caused depolarization all along the tube while O·2¯ provoked hyperpolarization and cytoplasm alkalinization. O·2¯accelerated growth and reduced tube diameter, indicating that this ROS can be considered as pollen tube growth stimulator. Serious structural disturbances were observed upon exposure to OH· and ROS quencher MnTMPP: pollen tube growth slowed down and ballooned tips formed in both cases, but OH· affected membrane transport and organelle distribution as well. OH·, thus, can be considered as a negative regulator of pollen tube growth. Pollen tubes, in turn, are able to reduce OH· concentration, which was assessed by electron paramagnetic resonance spectroscopy (EPR).

Published
2020

6. Proteomics-based identification of hypoxia-sensitive membrane-bound proteins in rat erythrocytes

Author

O. G. Luneva, Ryszard Grygorczyk, Natalya V. Alekseeva, Svetlana V. Sidorenko, Sergei N. Orlov, L. I. Deev, Georgy V. Maksimov, and Rustam H. Ziganshin

Subjects
Male, Proteomics, 0301 basic medicine, Erythrocytes, Proteome, мембраносвязанные белки, Protein subunit, Biophysics, Biochemistry, протеомика, эритроциты, 03 medical and health sciences, 0302 clinical medicine, Tandem Mass Spectrometry, Membrane fluidity, medicine, Animals, гипоксия, Rats, Wistar, Hypoxia, Cytoskeleton, Lipid bilayer, Band 3, biology, Chemistry, Erythrocyte Membrane, Membrane Proteins, Rats, Red blood cell, 030104 developmental biology, medicine.anatomical_structure, Membrane protein, гемолиз, biology.protein, крысы, Hemoglobin, гемоглобин, 030217 neurology & neurosurgery, Chromatography, Liquid
Abstract

This study examines the action of hypoxia on integrity, fluidity and protein composition of red blood cell (RBC) membrane. Twenty-min exposure to oxygen-free environment decreases rat RBC integrity documented by 3-fold elevation of hemoglobin release without any action on the membrane fluidity estimated by electron magnetic resonance spectroscopy of spin-labeled stearic acid analogues. The proteomics technology in combination with relative label free quantification analysis revealed a dozen of membrane-bound proteins, including elevated content of hemoglobin, reproducibly affected by hypoxia. Mapping the identified proteins in the KEGG pathway database we found that the proteins of multi subunit Cullin-Rbx E3 ubiquitin ligase complex are presented in normoxic RBC ghosts but not in the hypoxic samples. Our results suggest that Cullin-Rbx E3 complex, associated with RBC membrane in normoxia, provides detection and deletion of membrane proteins damaged by reactive oxygen species. In hypoxic conditions, deoxy-Hb binds to band 3 protein, resulting in dissociation of Cullin-Rbx E3 complex from RBC membrane and impaired clearance of damaged cytoskeleton proteins. These rearrangements of membrane proteins might be involved in attenuated membrane integrity revealed in hypoxic RBC. Significance This study demonstrate that sustained deoxygenation of rat erythrocytes alters the composition of membrane-bound proteins including elevation of the content of hemoglobin without any changes in the viscosity of erythrocyte membrane lipid bilayer. These results suggest that the changes the composition of membrane proteins result in attenuated membrane integrity and contribute to augment release of hemoglobin seen in hypoxic conditions.

Published
2018
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7. Hemolysis and ATP Release from Human and Rat Erythrocytes under Conditions of Hypoxia: A Comparative Study

Author

Svetlana V. Sidorenko, T. S. Novozhilova, Ryszard Grygorczyk, Georgy V. Maksimov, N. V. Alekseeva, O. V. Rodnenkov, Sergei N. Orlov, L. I. Deev, and O. G. Luneva

Subjects
0301 basic medicine, Chemistry, Biophysics, chemistry.chemical_element, Cell Biology, Pharmacology, Pannexin, medicine.disease, Biochemistry, Oxygen, Hemolysis, Probenecid, 03 medical and health sciences, Red blood cell, 030104 developmental biology, 0302 clinical medicine, medicine.anatomical_structure, Extracellular, medicine, Autoregulation, Hemoglobin, 030217 neurology & neurosurgery, medicine.drug
Abstract

Red blood cells are involved not only in transportation of oxygen and carbon dioxide but also in autoregulation of vascular tone by ATP release in hypoxic conditions. Molecular mechanisms of the ATP release from red blood cells in response to a decrease in partial oxygen pressure still remain to be elucidated. In this work we have studied effects of hypoxia on red blood cell hemolysis in humans and rats and compared the effects of inhibitors of ecto-ATPase and pannexin on the release of ATP and hemoglobin from rat erythrocytes. The 20-min hypoxia at 37°C increased hemolysis of red blood cells in humans and rats 1.5- and 2.5-fold, respectively. In rat erythrocytes a significant increase in hypoxia-induced extracellular ATP level was found only in the presence of ecto-ATPase inhibitor ARL 67156. In these conditions we observed a positive correlation (R2 = 0.5003) between the increase in free hemoglobin concentration and the ATP release. Neither carbenoxolon nor probenecid, the inhibitors of low-selectivity pannexin channels, altered the hypoxia-induced ATP release from rat erythrocytes. The obtained results indicate a key role of hemolysis in the ATP release from red blood cells.

Published
2018
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8. Physical–chemical properties of plasma membrane and function of erythrocytes of cosmonauts after long-term space flight

Author

Georgy V. Maksimov, O. I. Labetskaya, Yu. V. Yarlikova, O. G. Luneva, A. A. Baizhumanov, Ivanova Sm, Nadezda A. Brazhe, E.Y. Parshina, and B. V. Morukov

Subjects
Sodium–hydrogen antiporter, chemistry.chemical_compound, Membrane, Chemistry, Cholesterol, Physical chemical, Echinocyte, Biophysics, Aerospace Engineering, Semipermeable membrane, Hemoglobin, Plasma
Abstract

We studied microfluidity and selective ion permeability of plasma membranes and O2-binding properties of erythrocytes of cosmonauts during early rehabilitation after a long-term space flight (LTSF). Microfluidity of plasma membranes in surface regions was found to undergo a reversible decrease during 13–15 days following LTSF, which was accompanied by a reversible increase in relative cholesterol content. Cosmonauts’ erythrocytes revealed an increased activity of Na/H-exchanger and KCa-channel as well as a decrease in number of discocytes and increase in number of echinocytes, stomatocytes and knizocytes. Total hemoglobin content as well as oxyhemoglobin content were lowered after the LTSF, while the affinity of hemoglobin to O2 was advanced. It is suggested that the changes in Hb properties, microfluidity and selective permeability of plasma membranes following the elevated cholesterol content in the membranes can decrease tissue supply with O2.

Published
2011
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9. New Insight into Erythrocyte through In Vivo Surface-Enhanced Raman Spectroscopy

Author

Salim Abdali, Nadezda A. Brazhe, Olga Sosnovtseva, Georgy V. Maksimov, Nadezda Y. Bryzgalova, Eugenia Y. Parshina, O. G. Luneva, and Alexey R. Brazhe

Subjects
Male, Erythrocytes, Cell Survival, Surface Properties, Resonance Raman spectroscopy, Spectroscopy, Imaging, and Other Techniques, Biophysics, Analytical chemistry, Metal Nanoparticles, Spectrum Analysis, Raman, Silver nanoparticle, Hemoglobins, symbols.namesake, Colloid, Cytosol, In vivo, Animals, Molecule, Rats, Wistar, Chemistry, Signal Processing, Computer-Assisted, Surface-enhanced Raman spectroscopy, Rats, symbols, Gold, Hemoglobin, Raman spectroscopy
Abstract

The article presents a noninvasive approach to the study of erythrocyte properties by means of a comparative analysis of signals obtained by surface-enhanced Raman spectroscopy (SERS) and resonance Raman spectroscopy (RS). We report step-by-step the procedure for preparing experimental samples containing erythrocytes in their normal physiological environment in a mixture of colloid solution with silver nanoparticles and the procedure for the optimization of SERS conditions to achieve high signal enhancement without affecting the properties of living erythrocytes. By means of three independent techniques, we demonstrate that under the proposed conditions a colloid solution of silver nanoparticles does not affect the properties of erythrocytes. For the first time to our knowledge, we describe how to use the SERS-RS approach to study two populations of hemoglobin molecules inside an intact living erythrocyte: submembrane and cytosolic hemoglobin (Hb(sm) and Hb(c)). We show that the conformation of Hb(sm) differs from the conformation of Hb(c). This finding has an important application, as the comparative study of Hb(sm) and Hb(c) could be successfully used in biomedical research and diagnostic tests.

Published
2009
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10. HCO3--Dependent Impact of Na+,K+,2Cl- Cotransport in Vascular Smooth Muscle Excitation-Contraction Coupling

Author

Svetlana V. Koltsova, Georgy V. Maksimov, O. G. Luneva, Julie L. Lavoie, Pavel Hamet, Sergei N. Orlov, and Johanne Tremblay

Subjects
medicine.medical_specialty, Contraction (grammar), Vascular smooth muscle, Physiology, Chemistry, Bicarbonate, Depolarization, chemistry.chemical_compound, Endocrinology, Internal medicine, medicine, Extracellular, Cotransporter, Phenylephrine, Bumetanide, medicine.drug
Abstract

In smooth muscles, inhibition of Na(+),K(+),2Cl(-) cotransport (NKCC) by bumetanide decreased intracellular Cl(-) content ([Cl(-)](i)) and suppressed the contractions triggered by diverse stimuli. This study examines whether or not bicarbonate, a regulator of several Cl(-) transporters, affects the impact of NKCC in excitation-contraction coupling. Addition of 25 mM NaHCO(3) attenuated the inhibitory action of bumetanide on mesenteric artery contractions evoked by 30 mM KCl and phenylephrine (PE) by 5 and 3-fold, respectively. In cultured vascular smooth muscle cells, NaHCO(3) almost completely abolished inhibitory actions of bumetanide on transient depolarization and [Ca(2+)](i) elevation triggered by PE. In bicarbonate-free medium, bumetanide decreased [Cl(-)](i) by approximately 15%; this effect was almost totally abrogated by NaHCO(3). The addition of NaHCO(3) resulted in 2-fold inhibition of NKCC activity and 3-fold attenuation of [Cl(-)](i). These data strongly suggest that extracellular HCO(3)(-) diminishes the NKCC-sensitive component of excitation-contraction coupling via suppression of this carrier.

Published
2009
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11. Deoxygenation affects composition of membrane-bound proteins in human erythrocytes

Author

Sergei N. Orlov, O. G. Luneva, Ryszard Grygorczyk, Natalia V. Alekseeva, Artem M. Tverskoy, Aleksander A. Cherkashin, Georgy V. Maksimov, O. V. Rodnenkov, Svetlana V. Sidorenko, Olga Ponomarchuk, and L. I. Deev

Subjects
Adult, Male, 0301 basic medicine, Time Factors, Erythrocytes, Physiology, Hemolysis, lcsh:Physiology, дезоксигенирование, lcsh:Biochemistry, Hemoglobins, Young Adult, ATP release, 03 medical and health sciences, эритроциты, Adenosine Triphosphate, medicine, Extracellular, Humans, lcsh:QD415-436, Incubation, Deoxygenation, Membrane bound proteins, lcsh:QP1-981, Chemistry, Erythrocyte Membrane, Membrane Proteins, Hypoxia (medical), medicine.disease, Cell Hypoxia, Oxygen, 030104 developmental biology, Membrane, Biochemistry, гемолиз, Linear Models, Human erythrocytes, Electrophoresis, Polyacrylamide Gel, Female, Hemoglobin, medicine.symptom
Abstract

Background/Aims: ATP release from erythrocyte plays a key role in hypoxia-induced elevation of blood flow in systematic circulation. We have previously shown that hemolysis contributes to erythrocyte ATP release triggered by several stimuli, including hypoxia, but the molecular mechanisms of hypoxia-increased membrane fragility remain unknown. Methods: In this study, we compared the action of hypoxia on hemolysis, ATP release and the composition of membrane-bound proteins in human erythrocytes. Results: Twenty minutes incubation of human erythrocytes in the oxygen-free environment increased the content of extracellular hemoglobin by ∼1.5 fold. Paired measurements of hemoglobin and ATP content in the same samples, showed a positive correlation between hemolysis and ATP release. Comparative analysis of SDS-PAGE electrophoresis of erythrocyte ghosts obtained under control and deoxygenated conditions revealed a ∼2-fold elevation of the content of membrane-bound protein with Mr of ∼60 kDa. Conclusion: Deoxygenation of human erythrocytes affects composition of membrane-bound proteins. Additional experiments should be performed to identify the molecular origin of 60 kDa protein and its role in the attenuation of erythrocyte integrity and ATP release in hypoxic conditions.

Published
2016

12. Ion transport, membrane fluidity and haemoglobin conformation in erythrocyte from patients with cardiovascular diseases: Role of augmented plasma cholesterol

Author

Sergei N. Orlov, N. Yu. Bryzgalova, Nadezda A. Brazhe, Andrei B. Rubin, E I Chazov, O. V. Rodnenkov, N. V. Maksimova, O. G. Luneva, E. Yu. Parshina, and Georgy V. Maksimov

Subjects
medicine.medical_specialty, Cholesterol, Hypertriglyceridemia, chemistry.chemical_element, Transporter, Essential hypertension, medicine.disease, Oxygen, Pathology and Forensic Medicine, chemistry.chemical_compound, Endocrinology, Biochemistry, chemistry, Permeability (electromagnetism), Physiology (medical), Internal medicine, medicine, Membrane fluidity, Ion transporter
Abstract

Tissue hypoxia, which plays a key role in the development of renal and vascular complications of cardiovascular diseases (CVD), might be considered a consequence of vascular remodeling and/or attenuated oxygen (O(2)) delivery by erythrocytes. Using Raman spectroscopy (RS), we observed that erythrocytes from patients with CVD exhibit changes in the conformation of haemoglobin (Hb) haemoporphyrin (HP), reflecting its lower O(2) transport capacity. Hypertriglyceridemia and hypercholesterolemia are well-known hallmarks of CVD. This study examined the role of plasma lipids in the regulation of erythrocyte membrane viscosity, oxy-Hb content as well as Na(+)/H(+) exchange and Ca(2+)-ATPase, whose activities are altered in patients with CVD. HP conformation was assessed by RS of blood samples. Membrane fluidity was estimated at depths of 0.6-0.8 and 2.2nm by electron-paramagnetic resonance spectroscopy of erythrocytes loaded with spin-labeled 5-doxylstearic acid and 16-doxylstearic acid, respectively. Ion-selective electrodes were employed for the study of H(+) and Ca(2+) fluxes. Both oxy-Hb content and erythrocyte membrane fluidity were decreased in essential hypertension and coronary artery disease patients and negatively correlated with plasma cholesterol but not triglyceride content. This observation allows us to assume that decreased oxy-Hb content in patients with CVD is caused by high plasma cholesterol via attenuation of erythrocyte membrane fluidity and its permeability to O(2). Plasma cholesterol level correlated positively and negatively with erythrocyte Na(+)/H(+) exchange and Ca(2+)-ATPase, respectively. However, in contrast to membrane fluidity, the impact of these ion transporters in oxy-Hb regulation under baseline conditions seems to be negligible. We propose that decreased oxy-Hb content contributes to the reduced O(2) tissue supply seen in patients with CVD.

Published
2007
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13. Changes in the State of Hemoglobin in Patients with Coronary Heart Disease and Patients with Circulatory Failure

Author

N. A. Braze, O. G. Luneva, O. V. Rodnenkov, Georgy V. Maksimov, E. Yu. Parshina, Churin Aa, and Alexander Yusipovich

Subjects
Adult, Male, medicine.medical_specialty, CIRCULATORY FAILURE, Erythrocytes, Abnormal, chemistry.chemical_element, Coronary Disease, Hematocrit, Oxygen, General Biochemistry, Genetics and Molecular Biology, Hemoglobins, chemistry.chemical_compound, Oxygen Consumption, Internal medicine, medicine, Humans, In patient, Hematoporphyrin, medicine.diagnostic_test, business.industry, Shock, General Medicine, Middle Aged, Coronary heart disease, Hematoporphyrins, chemistry, Laser interference, Cardiology, Hemoglobin, business
Abstract

Morphology of erythrocytes and conformation of hemoglobin-derived hematoporphyrin were studied in patients with coronary heart disease (CHD) and patients with circulatory failure using laser interference microscopy and Raman spectroscopy. Correlation was revealed (r=0.81) between hemoglobin oxygen saturation and oxyhemoglobin fraction in erythrocytes evaluated by Raman spectroscopy. Patients with CHD and patients with circulatory failure showed reduced oxygen-releasing capacity of hemoglobin and hemoglobin content and increased oxygen-binding capacity of hemoglobin, and hemoglobin affinity for oxygen. Significant differences from the control were observed only in patients with circulatory failure. It was found that hemoglobin content, hematocrit, and the shape of erythrocytes during CHD and circulatory failure did not differ from the control, whereas the area of erythrocytes was increased.

Published
2013
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14. Erythrocytes as regulators of blood vessel tone

Author

Georgy V. Maksimov, O. G. Luneva, Svetlana V. Sidorenko, Ryszard Grygorczyk, and Sergei N. Orlov

Subjects
Blood vessel diameter, пуринергическая сигнальная система, biology, Purinergic receptor, Biophysics, Cell Biology, Haemolysis, Biochemistry, Nitric oxide, chemistry.chemical_compound, эритроциты, medicine.anatomical_structure, chemistry, гемолиз, medicine, biology.protein, кровеносные сосуды, Oxygen sensing, Band 3, Intracellular, Blood vessel
Abstract

A drop in oxygen partial pressure results in elevation of blood vessel diameter. It has been demonstrated that isolated vessels exhibit this unique feature only when they are perfused in the presence of erythrocytes. More recently, it was shown that haemoglobin plays a key role in oxygen sensing. Its deoxygenated form interacts with band 3 protein, triggering the cascade of non-identified intracellular signals involved in nitric oxide production and release of ATP interacting with P2Y purinergic receptors in endothelial cells. In this review, we summarize the data on mechanisms of ATP release from erythrocytes, as well as on its physiological and pathophysiological implications.

Published
2015

15. Contributory presentations/posters

Author

N. Manoj, V. R. Srinivas, A. Surolia, M. Vijayan, K. Suguna, R. Ravishankar, R. Schwarzenbacher, K. Zeth, null Diederichs, G. M. Kostner, A. Gries, P. Laggner, R. Prassl, null Madhusudan, Pearl Akamine, Nguyen-huu Xuong, Susan S. Taylor, M. Bidva Sagar, K. Saikrishnan, S. Roy, K. Purnapatre, P. Handa, U. Varshney, B. K. Biswal, N. Sukumar, J. K. Mohana Rao, A. Johnson, Vasantha Pattabhi, S. Sri Krishna, Mira Sastri, H. S. Savithri, M. R. N. Murthy, Bindu Pillai, null Kannan, M. V. Hosur, Mukesh Kumar, Swati Patwardhan, K. K. Kannan, B. Padmanabhaa, S. Sasaki-Sugio, M. Nukaga, T. Matsuzaki, S. Karthikevan, S. Sharma, A. K. Sharma, M. Paramasivam, P. Kumar, J. A. Khan, S. Yadav, A. Srinivasan, T. P. Singh, S. Gourinath, Neelima Alam, A. Srintvasan, Vikas Chandra, Punit Kaur, Ch. Betzel, S. Ghosh, A. K. Bera, S. Bhattacharya, S. Chakraborty, A. K. Pal, B. P. Mukhopadhyay, I. Dey, U. Haldar, Asok Baneriee, Jozef Sevcik, Adriana Solovicova, K. Sekar, M. Sundaralingam, N. Genov, Dong-cai Liang, Tao Jiang, Ji-ping Zhang, Wen-rui Chang, Wolfgang Jahnke, Marcel Blommers, S. C. Panchal, R. V. Hosur, Bindu Pillay, Puniti Mathur, S. Srivatsun, Ratan Mani Joshi, N. R. Jaganathan, V. S. Chauhan, H. S. Atreya, S. C. Sahu, K. V. R. Chary, Girjesh Govil, Elisabeth Adjadj, Éric Quinjou, Nadia Izadi-Pruneyre, Yves Blouquit, Joël Mispelter, Bernadette Heyd, Guilhem Lerat, Philippe Milnard, Michel Desmadreil, Y. Lin, B. D. Nageswara Rao, Vidva Raghunathan, Mei H. Chau, Prashant Pesais, Sudha Srivastava, Evans Coutinho, Anil Saran, Leizl F. Sapico, Jayson Gesme, Herbert Lijima, Raymond Paxton, Thamarapu Srikrishnan, C. R. Grace, G. Nagenagowda, A. M. Lynn, Sudha M. Cowsik, Sarata C. Sahu, S. Chauhan, A. Bhattacharya, G. Govil, Anil Kumar, Maurizio Pellecchia, Erik R. P. Zuiderweg, Keiichi Kawano, Tomoyasu Aizawa, Naoki Fujitani, Yoichi Hayakawa, Atsushi Ohnishi, Tadayasu Ohkubo, Yasuhiro Kumaki, Kunio Hikichi, Katsutoshi Nitta, V. Rani Parvathy, R. M. Kini, Takumi Koshiba, Yoshihiro Kobashigawa, Min Yao, Makoto Demura, Astushi Nakagawa, Isao Tanaka, Kunihiro Kuwajima, Jens Linge, Seán O. Donoghue, Michael Nilges, G. Chakshusmathi, Girish S. Ratnaparkhi, P. K. Madhu, R. Varadarajan, C. Tetreau, M. Tourbez, D. Lavalette, M. Manno, P. L. San Biagio, V. Martorana, A. Emanuele, S. M. Vaiana, D. Bulone, M. B. Palma-Vittorelli, M. U. Palma, V. D. Trivedi, S. F. Cheng, W. J. Chien, S. H. Yang, S. Francis, D. K. Chang, Renn Batra, Michael A. Geeves, Dietmar J. Manstein, Joanna Trvlska, Pawel Grochowski, Maciej Geller, K. Ginalski, P. Grochowski, B. Lesyng, P. Lavalette, Y. Blouquit, D. Roccatano, A. Amadei, A. Di Nola, H. J. C. Berendsen, Bosco Ho, P. M. G. Curmi, H. Berry, D. Lairez, E. Pauthe, J. Pelta, V. Kothekar, Shakti Sahi, M. Srinivasan, Anil K. Singh, Kartha S. Madhusudnan, Fateh S. Nandel, Harpreet Kaur, Balwinder Singh, D. V. S. Jain, K. Anton Feenstra, Herman J. C. Berendsen, F. Tama, Y. -H. Sanejouand, N. Go, Deepak Sharma, Sunita Sharma, Santosh Pasha, Samir K. Brahmachari, R. Viiavaraghavan, Jyoti Makker, Sharmisllia Dey, S. Kumar, G. S. Lakshmikanth, G. Krishnamoorthy, V. M. Mazhul, E. M. Zaitseva, Borys Kierdaszuk, J. Widengren, B. Terry, Ü. Mets, R. Rigler, R. Swaminathan, S. Thamotharan, N. Yathindra, Y. Shibata, H. Chosrowjan, N. Mataga, I. Morisima, Tania Chakraharty, Ming Xiao, Roger Cooke, Paul Selvin, C. Branca, A. Faraone, S. Magazù, G. Maisano, P. Migliardo, V. Villari, Digambar V. Behere, M. Sharique Zahida Waheed Deva, M. Brunori, F. Cutruzzolà, Q. H. Gibson, C. Savino, C. Travaglini-Allocatelli, B. Vallone, Swati Prasad, Shyamalava Mazumdar, Samaresh Mitra, P. Soto, R. Fayad, I. E. Sukovataya, N. A. Tyulkova, Sh. V. Mamedov, B. Aktas, M. Canturk, B. Aksakal, R. Yilgin, K. I. Bogutska, N. S. Miroshnichenko, S. Chacko, M. DiSanto, J. A. Hypolite, Y-M. Zheng, A. J. Wein, M. Wojciechowski, T. Grycuk, J. Antosiewicz, Marc A. Ceruso, Alfredo Di Nola, Subhasis Bandvopadhvay, Bishnu P. Chatterjee, Devapriva Choudhury, Andrew Thompson, Vivian Stojanoff, Jerome Pinkner, Scott Hultgren, Stefan Khight, Delphine Flatters, Julia Goodfellow, Fumi Takazawatt, Minoru Kanehisa, Masaki Sasai, Hironori Nakamura, Wang Bao Han, Yuan Zheng, Wang Zhi Xin, Pan xin Min, Vlnod Bhakuni, Sangeeta Kulkarni, Atta Ahmad, Koodathingal Prakash, Shashi Prajapati, Alexey Surin, Tomoharu Matsumoto, Li Yang, Yuki Nakagawa, Kazumoto Kimura, Yoshiyuki Amemiya, Gennady V. Semisotnov, Hiroshi Kihara, Saad Tayyab, Salman Muzammil, Yogesh Kumar, Vinod Bhakuni, Monica Sundd, Suman Kundu, M. V. Jagannadham, Medicherla V. Jagannadham, Bina Chandani, Ruby Dhar, Lalankumar Sinha, Deepti Warrier, Sonam Mehrotra, Purnima Khandelwal, Subhendu Seth, Y. U. Sasidhar, C. Ratna Prabha, Arun Gidwani, K. P. Madhusudan, Akira R. Kinjo, Ken Nishikawa, Suvobrata Chakravarty, Raghavan Varadarajan, K. Noyelle, P. Haezebrouck, M. Joniau, H. Van Dael, Sheffali Dash, Indra Brata Jha, Rajiv Bhat, Prasanna Mohanty, A. K. Bandyopadhyay, H. M. Sonawat, Ch. Mohan Rao, Siddhartha Datta, K. Rajaraman, B. Raman, T. Ramakrishna, A. Pande, J. Pande, S. Betts, N. Asherie, O. Ogun, J. King, G. Benedek, I. V. Sokolova, G. S. Kalacheva, Masashi Sonoyama, Yasunori Yokoyama, Kunihiro Taira, Shigeki Mitaku, Chicko Nakazawal, Takanori Sasakil, Yuri Mukai, Naoki Kamo, Seema Dalal, Lynne Regan, Shigeki Mituku, Mihir Roychoudhury, Devesh Kumar, Dénes Lőrinczv, Franciska Könczöl, László Farkas, Joseph Belagyi, Christoph Schick, Christy A. Thomson, Vettai S. Ananthanarayanan, E. G. Alirzayeva, S. N. Baba-Zade, M. Michael Gromiha, M. Oobatake, H. Kono, J. An, H. Uedaira, A. Sarai, Kazufumi Takano, Yuriko Yamagata, Katsuhide Yutani, Gouri S. Jas, Victor Muñoz, James Hofrichter, William A. Eaton, Jonathan Penoyar, Philip T. Lo Verde, J. Kardos, Á. Bódi, I. Venekei, P. Závodszky, L. Gráf, András Szilágyi, Péter Závodszky, R. D. Allan, J. Walshaw, D. N. Woolfson, Jun Funahashi, Savan Gupta, M. Mangoni, P. Roccatano, Gosu Ramachandraiah, Nagasuma R. Chandra, Barbara Ciani, Derek N. Woolfson, Usha B. Nair, Kanwal J. Kaur, Dinakar M. Salunke, Chittoor P. Swaminathan, Avadhesha Surolia, A. Pramanik, P. Jonasson, G. Kratz, O. T. Jansson, P. -Å. Nygren, S. Ståhl, K. Ekberg, B. -L. Johansson, S. Uhlén, M. Uhlén, H. Jörnvall, J. Wahren, Karin Welfle, Rolf Misselwitz, Wolfgang Höhne, Heinz Welfle, L. G. Mitskevich, N. V. Fedurkina, B. I. Kurganov, Gotam K. Jarori, Haripada Maity, J. Guharay, B. Sengupta, P. K. Sengupta, K. Sridevi, S. R. Kasturi, S. P. Gupta, Gunjan Agarwal, Suzanne Kwong, Robin W. Briehl, O. I. Ismailova, N, A. Tyulkova, C. Hariharan, D. Pines, E. Pines, M. Zamai, R. Cohen-Luria, A. Yayon, A. H. Parola, M. J. Padya, G. A. Spooner, D. N. Woolfeon, Panchan Bakshi, D. K. Bharadwaj, U. Sharma, N. Srivastava, R. Barthwal, N. R. Jagannathan, Keiko Matsuda, Takaaki Nishioka, Nobuhiro Go, T. Aita, S. Urata, Y. Husimi, Mainak Majumder, Nicola G. A. Abrescia, Lucy Malinina, Juan A. Subirana, Juan Aymami, Ramón Eritxa, Miquel Coll, B. J. Premraj, R. Thenmalarchelvi, P. Satheesh Kumar, N. Gautham, Lou -Sing Kan, null Ming-Hou, Shwu-Bin Lin, Tapas Sana, Kanal B. Roy, N. Bruant, D. Flatters, R. Lavery, D. Genest, Remo Rons, Heinz Sklenar, Richard Lavery, Sudip Kundu, Dhananjay Bhattacharyya, Debashree Bandyopadhyay, Ashoke Ranjan Thakur, Rabi Majumdar, F. Barceló, J. Portugal, Sunita Ramanathan, B. J. Rao, Mahua Gliosli, N. Vinay Kumar, Umesh Varshney, Shashank S. Pataskar, R. Sarojini, S. Selvasekarapandian, P. Kolandaivel, S. Sukumar, P. Kolmdaivel, Motilal Maiti, Anjana Sen, Suman Das, Elisa Del Terra, Chiara Suraci, Silvia Diviacco, Franco Quadrifoglio, Luigi Xodo, Arghya Ray, G. Karthikeyan, Kandala V. R. Chary, Basuthkar J. Rao, Anwer Mujeeb, Thomas L. James, N. Kasyanenko, E. E. F. Haya, A. Bogdanov, A. Zanina, M. R. Bugs, M. L. Cornélio, M. Ye. Tolstorukov, Nitish K. Sanval, S. N. Tiwari, Nitish K. Sanyal, Mihir Roy Choudhury, P. K. Patel, Neel S. Bhavesh, Anna Gabrielian, Stefan Wennmalm, Lars Edman, Rudolf Rigler, B. Constantinescu, L. Radu, I. Radulcscu, D. Gazdaru, Sebastian Wärmländer, Mikael Leijon, Setsuyuki Aoki, Takao Kondo, Masahiro Ishiura, V. A. Pashinskaya, M. V. Kosevich, V. S. Shelkovsky, Yu. P. Blagoy, Ji-hua Wang, R. Malathi, K. Chandrasekhar, E. R. Kandimalla, S. Agrawal, V. K. Rastogi, M. Alcolea Palafox, Chatar Singh, A. D. Beniaminov, S. A. Bondarenko, E. M. Zdobnov, E. E. Minyat, N. B. Ulyanov, V. I. Ivanov, J. S. Singh, Kailas D. Sonawane, Henri Grosjean, Ravindra Tewari, Uddhavesh B. Sonavane, Annie Morin, Elizabeth A. Doherty, Jennifer A. Doudna, H. Tochio, S. Sato, H. Matsuo, M. Shirakawa, Y. Kyogoku, B. Javaram, Surjit B. Dixit, Piyush Shukla, Parul Kalra, Achintya Das, Kevin McConnell, David L. Beveridge, W. H. Sawyer, R. Y. S. Chan, J. F. Eccelston, Yuling Yan, B. E. Davidson, Eimer Tuite, Bengt Norden, Peter Nielsen, Masayuki Takahashi, Anirban Ghosh, Manju Bansal, Frauke Christ, Hubert Thole, Wolfgang Wende, Alfred Pingoud, Vera Pingoud, Pratibha Mehta Luthra, Ramesh Chandra, Ranjan Sen, Rodney King, Robert Weisberg, Olaf F. A. Larsen, Jos Berends, Hans A. Heus, Cornelis W. Hilbers, Ivo H. M. van Stokkum, Bas Gobets, Rienk van Grondelle, Herbert van Amerongen, HE. Sngrvan, Yu. S. Babayan, N. V. Khudaverdian, M. Gromiha, F. Pichierri, M. Aida, P. Prabakaran, K. Sayano, Saulius Serva, Eglė Merkienė, Giedrius Vilkaitis, Elmar Weinhold, Saulius Klimašauskas, Eleonora Marsich, Antonella Bandiera, Giorgio Manzini, G. Potikyan, V. Arakelyan, Yu. Babayan, Alex Ninaber, Julia M. Goodfellow, Yoichiro Ito, Shigeru Ohta, Yuzuru Husimi, J. Usukura, H. Tagami, H. Aiba, Mougli Suarez, Elia Nunes, Deborah Keszenman, E. Carmen Candreva, Per Thyberg, Zeno Földes-Papp, Amita Joshi, Dinesh Singh, M. R. Rajeswari, null Ira, M. Pregetter, H. Amenitsch, J. Chapman, B. N. Pandev, K. P. Mishra, E. E. Pohl, J. Sun, I. I. Agapov, A. G. Tonevitsky, P. Pohl, S. M. Dennison, G. P. Gorbeako, T. S. Dynbko, N. Pappavee, A. K. Mishra, Prieto Manuel, Almeida Rodrigo, Loura Luis, L. Ya. Gendel, S. Przestalski, J. Kuczera, H. Kleszczyńska, T. Kral, E. A. Chernitsky, O. A. Senkovich, V. V. Rosin, Y. M. Allakhverdieva, G. C. Papageorgiou, R. A. Gasanov, Calin Apetrei, Tudor Savopol, Marius Balea, D. Cucu, D. Mihailescu, K. V. Ramanathan, Goran Bačić, Nicolas Sajot, Norbert Garnier, Serge Crouzy, Monique Genest, Z. S. Várkonyi, O. Zsiros, T. Farkas, Z. Combos, Sophie Cribier, I. F. Fraceto, S. Schreier, A. Spisni, F. de Paula, F. Sevšek, G. Gomišček, V. Arrigler, S. Svetina, B. Žekš, Fumimasa Nomura, Miki Nagata, Kingo Takiguchi, Hirokazu Hotani, Lata Panicker, P. S. Parvathanathan, A. Ishino, A. Saitoh, H. Hotani, K. Takiguchi, S. Afonin, A. Takahashi, Y. Nakato, T. Takizawa, Dipti Marathe, Kent Jørgensen, Satinder S. Rawat, R. Rukmini, Amitabha Chattopadhyay, M. Šentiurc, J. Štrancar, Z. Stolič, K. Filipin, S. Pečar, S. C. Biswas, Satyen Sana, Anunay Samanta, Koji Kinoshita, Masahito Yamazaki, Tetsuhiko Ohba, Tai Kiuchi, null Yoshitoshi, null Kamakura, Akira Goto, Takaaki Kumeta, Kazuo Ohki, I. P. Sugar, T. E. Thompson, K. K. Thompson, R. L. Biltonen, Y. Suezaki, H. Ichinose, M. Akivama, S. Matuoka, K. Tsuchihashi, S. Gasa, P. Mattjus, J. G. Molotkovsky, H. M. Pike, R. E. Brown, Ashish Arora, Jörg H. Kleinschmidt, Lukas K. Tamm, O. G. Luneva, K. E. Kruglyakova, V. A. Fedin, O. S. Kuptsoya, J. W. Borst, N. V. Visser, A. J. W. G. Visser, T. S. Dyubko, Toshihiko Ogihara, Kiyoshi Mishima, A. L. Shvaleva, N. Č. Radenović, P. M. Minić, M. G. Jeremić, Č. N. Radenović, T. F. Aripov, E. T. Tadjibaeva, O. N. Vagina, M. V. Zamaraeva, B. A. Salakhutdinov, A. Cole, M. Poppofl, C. Naylor, R. Titball, A. K. Basak, J. T. Eaton, C. E. Naylor, N. Justin, D. S. Moss, R. W. Titball, F. Nomura, M. Nagata, S. Ishjkawa, S. Takahashi, Kaoru Obuchi, Erich Staudegger, Manfred Kriechbaum, Robert I. Lehrer, Alan J. Waring, Karl Lohner, Susanne Gangl, Bernd Mayer, Gottfried Köhler, J. Shobini, Z. Guttenberg, B. Lortz, B. Hu, E. Sackmann, N. M. Kozlova, L. M. Lukyanenko, A. N. Antonovich, E. I. Slobozhanina, Andrey V. Krylov, Yuri N. Antonenko, Elena A. Kotova, Alexander A. Yaroslavov, Subhendu Ghosh, Amal K. Bera, Sudipto Das, Eva Urbánková, Masood Jelokhani-Niaraki, Karl Freeman, Petr Jezek, P. B. Usmanov, A. Ongarbaev, A. K. Tonkikh, Peter Pohl, Sapar M. Saparov, P. Harikumar, J. P. Reeves, S. Rao, S. K. Sikdar, A. S. Ghatpande, C. Corsso, A. C. Campos de Carvalho, W. A. Varanda, C. ElHamel, E. Dé, N. Saint, G. Molle, Anurae Varshney, M. K. Mathew, E. Loots, E. Y. Isacoff, Michiki Kasai, Naohiro Yamaguchi, Paramita Ghosh, Joseph Tigyi, Gabor Tigyi, Karoly Liliom, Ricardo Miledi, Maja R. Djurisic, Pavle R. Andjus, Indira H. Shrivastava, M. S. P. Sansom, C. Barrias, P. F. Oliveira, A. C. Mauricio, A. M. Rebelo da Costa, I. A. Lopes, S. V. Fedorovich, V. S. Chubanov, M. V. Sholukh, S. V. Konev, N. Fedirko, V. Manko, M. Klevets, N. Shvinka, B. S. Prabhananda, Mamata H. Kombrabail, S. Aravamudhan, Berenice Venegas-Cotero, Ivan Ortega Blake, Zhi-hong Zhang, Xiao-jian Hu, Han-qing Zhou, Wei-ying Cheng, Hang-fang Feng, L. O. Dubitsky, L. S. Vovkanvch, I. A. Zalyvsky, E. Savio-Galimberti, P. Bonazzola, J. E. Ponce-Homos, Mario Parisi, Claudia Capurro, Roxana Toriano, Laxma G. Ready, Larry R. Jones, David D. Thomas, B. A. Tashmukhamedov, B. T. Sagdullaev, D. Heitzmann, R. Warth, M. Bleich, R. Greger, K. T. G. Ferreira, H. G. Ferreira, Orna Zagoory, Essa Alfahel, Abraham H. Parola, Zvi Priel, H. Hama-Inaba, R. Wang, K. Choi, T. Nakajima, K. Haginoya, M. Mori, H. Ohyama, O. Yukawa, I. Hayata, Nanda B. Joshi, Sridhar K. Kannurpatti, Preeti G. Joshi, Mau Sinha, Xun Shen, Tianhui Hu, Ling Bei, Menno L. W. Knetsch, Nicole Schäfers, John Sandblom, Juris Galvanovskis, Roxana Pologea-Moraru, Eugenia Kovacs, Alexandra Dinu, S. H. Sanghvi, V. Jazbinšek, G. Thiel, W. Müller, G. Wübeller, Z. Tronteli, Leš Fajmut, Marko Marhl, Milan Brumen, I. D. Volotovski, S. G. Sokolovski, M. R. Knight, Alexei N. Vasil’ev, Alexander V. Chalyi, P. Sharma, P. J. Steinbach, M. Sharma, N. D. Amin, J. Barchir, R. W. Albers, H. C. Pant, M. Balasubramanyam, M. Condrescu, J. P. Gardner, Shamci Monajembashi, Gotz Pilarczyk, K. O. Greulich, F. M. El-Refaei, M. M. Talaat, A. I. El-Awadi, F. M. Ali, Ivan Tahradník, Jana Pavelková, Alexandra Zahradniková, Boris S. Zhorov, Vettai S. Ananthanaravanan, M. Ch. Michailov, E. Neu, W. Seidenbusch, E. Gornik, D. Martin, U. Welscher, D. G. Weiss, B. R. Pattnaik, A. Jellali, V. Forster, D. Hicks, J. Sahel, H. Dreyfus, S. Picaud, Hong-Wei Wang, Sen-fang Sui, Pradeep K. Luther, John Barry, Ed Morris, John Squire, C. Sivakama Sundari, D. Balasubramanian, K. Veluraia, T. Hema Thanka Christlet, M. Xavier Suresh, V. Laretta-Garde, Dubravka Krilov, Nataša Stojanović, Janko N. Herak, Ravi Jasuja, Maria Ivanova, Rossen Mirchev, Frank A. Ferrone, David Stopar, Ruud B. Spruijt, Cor J. A. M. Wolfs, Marcus A. Hemminga, G. Arcovito, M. De Spirito, Rajendra K. Agrawal, Amy B. Heagle, Pawel Penczek, Robert Grassucci, Joachim Frank, Manjuli R. Sharma, Loice H. Jeyakumar, Sidney Fleischer, Terence Wagenknecht, Carlo Knupp, Peter M. G. Munro, Eric Ezra, John M. Squire, Koji Ichihara, Hidefumi Kitazawa, Yusuke Iguchi, Tomohiko J. Itoh, Greta Pifat, Marina Kveder, Slavko Pečar, Milan Schara, Deepak Nair, Kavita Singh, Kanury V. S. Rao, Kanwaljeet Kaur, Deepti Jain, B. Sundaravadivel, Manisha Goel, D. M. Salunke, E. I. Kovalenko, G. N. Semenkova, S. N. Cherenkevich, T. Lakshmanan, D. Sriram, S. Srinivasan, D. Loganathan, T. S. Ramalingam, J. A. Lebrón, P. J. Bjorkman, A. K. Singh, T. N. Gayatri, Ernesto R. Caffarena, J. Raul Grigera, Paulo M. Bisch, V. Kiessling, P. Fromherz, K. N. Rao, S. M. Gaikwad, M. I. Khan, C. G. Suresh, P. Kaliannan, M. Elanthiraiyan, K. Chadha, J. Payne, J. L. Ambrus, M. P. N. Nair, Madhavan P. N. Nair, S. Mahajan, K. C. Chadha, R. Hewitt, S. A. Schwartz, J. Bourguignon, M. Faure, C. Cohen-Addad, M. Neuburger, R. Ober, L. Sieker, D. Macherel, R. Douce, D. S. Gurumurthy, S. Velmurugan, Z. Lobo, Ratna S. Phadke, Prashant Desai, I. M. Guseinova, S. Yu. Suleimanov, I. S. Zulfugarov, S. N. Novruzova, J. A. Aliev, M. A. Ismayilov, T. V. Savchenko, D. R. Alieva, Petr Ilík, Roman Kouřil, Hana Bartošková, Jan Nauš, Jvoti U. Gaikwad, Sarah Thomas, P. B. Vidyasagar, G. Garab, I. Simidjiev, S. Rajagopal, Zs. Várkonyi, S. Stoylova, Z. Cseh, E. Papp, L. Mustárdy, A. Holzenburg, R. Bruder, U. K. Genick, T. T. Woo, D. P. Millar, K. Gerwert, E. D. Getzoff, Tamás Jávorfí, Győző Garab, K. Razi Naqvi, Md. Kalimullah, Jyoti Gaikwad, Manoj Semwal, Roman Kouril, Petr Ilik, Man Naus, István Pomozi, Gábor Horváth, Rüdiger Wehner, Gary D. Bernard, Ana Damjanović, Thorsten Ritz, Klaus Schulten, Wang Jushuo, Shan Jixiu, Gong Yandao, Kuang Tingyun, Zhao Nanming, Arvi Freiberg, Kõu Timpmann, Rein Ruus, Neal W. Woodbury, E. V. Nemtseva, N. S. Kudryasheva, A. G. Sizykh, V. N. Shikhov, T. V. Nesterenko, A. A. Tikhomirov, Giorgio Forti, Giovanni Finazzi, Alberto Furia, Romina Paola Barbagallo, S. Iskenderova, R. Agalarov, R. Gasanov, Miyashita Osamu, G. O. Nobuhiro, R. K. Soni, M. Ramrakhiani, Hiromasa Yagi, Kacko Tozawa, Nobuaki Sekino, Tomoyuki Iwabuchi, Masasuke Yoshida, Hideo Akutsu, A. V. Avetisyan, A. D. Kaulen, V. P. Skulachev, B. A. Feniouk, Cécile Breyton, Werner Kühlbrandt, Maria Assarsson, Astrid Gräslund, G. Horváth, B. Libisch, Z. Gombos, N. V. Budagovskaya, N. Kudryasheva, Erisa Harada, Yuki Fukuoka, Tomoaki Ohmura, Arima Fukunishi, Gota Kawai, Kimitsuna Watanabe, Jure Derganc, Bojan Božič, Saša Svetina, Boštjan Žekš, J. F. Y. Hoh, Z. B. Li, G. H. Rossmanith, E. L. de Beer, B. W. Treijtel, P. L. T. M. Frederix, T. Blangè, S. Hénon, F. Galtet, V. Laurent, E. Planus, D. Isabey, L. S. Rath, P. K. Dash, M. K. Raval, C. Ramakrishnan, R. Balaram, Milan Randic, Subhash C. Basak, Marjan Vracko, Ashesh Nandy, Dragan Amic, Drago Beslo, Sonja Nikolic, Nenad Trinajstic, J. Walahaw, Marc F. J. Lensink, Boojala V. B. Reddy, Ilya N. Shindylov, Philip E. Bourne, M. C. Donnamaria, J. de Xammar Oro, J. R. Grigera, Monica Neagu, Adrian Neagu, Matej Praprotnik, Dušanka Janežič, Pekka Mark, Lennart Nilsson, L. La Fata, Laurent E. Dardenne, Araken S. Werneck, Marçal de O. Neto, N. Kannan, S. Vishveshwara, K. Veluraja, Gregory D. Grunwald, Alexandra T. Balaban, Kanika Basak, Brian D. Gute, Denise Mills, David Opitz, Krishnan Balasubramanian, G. I. Mihalas, Diana Lungeanu, G. Macovievici, Raluca Gruia, C. Cortez-Maghelly, B. Dalcin, E. P. Passos, S. Blesic, M. Ljubisavljevic, S. Milosevic, D. J. Stratimirovic, Nandita Bachhawat, Shekhar C. Mande, A. Nandy, Ayumu Saito, Koichi Nishigaki, Mohammed Naimuddin, Takatsugu Hirokawa, Mitsuo Ono, Hirotomo Takaesu, M. I. El Gohary, Abdalla S. Ahmed, A. M. Eissa, Hiroshi Nakashima, G. P. S. Raghava, N. Kurgalvuk, O. Goryn, Bernard S. Gerstman, E. V. Gritsenko, N. N. Remmel, O. M. Maznyak, V. A. Kratasyuk, E. N. Esimbekova, D. Tchitchkan, S. Koulchitsky, A. Tikhonov, A. German, Y. Pesotskaya, S. Pashkevich, S. Pletnev, V. Kulchitsky, Umamaheswar Duvvuri, Sridhar Charagundla, Rahim Rizi, John S. Leigh, Ravinder Reddy, Mahesh Kumar, O. Coshic, P. K. Julka, O. K. Rath, NR. Jagannathan, Karina Roxana Iliescu, Maria Sajin, Nicolcta Moisoi, Ileana Petcu, A. I. Kuzmenko, R. P. Morozova, I. A. Nikolenko, G. V. Donchenko, M. K. Rahman, M. M. Ahmed, Takehiro Watanabe, Y. Rubin, H. Gilboa, R. Sharony, R. Ammar, G. Uretzky, M. Khubchandani, H. N. Mallick, V. Mohan Kumar, Arijitt Borthakur, Erik M. Shapiro, M. Gulnaz Begum, Mahaveer N. Degaonkar, S. Govindasamy, Ivan Dimitrov, T. A. Kumosani, W. Bild, I. Stefanescu, G. Titescu, R. Iliescu, C. Lupusoru, V. Nastasa, I. Haulica, Gopal Khetawat, N. Faraday, M. Nealen, S. Noga, P. F. Bray, T. V. Ananieva, E. A. Lycholat, MV. Kosevich, S. G. Stepanyan, S. V. Antonyuk, R. Khachatryan, H. Arakelian, A. Kumar, S. Ayrapetyan, V. Mkheyan, S. Agadjanyan, A. Khachatryan, S. S. Rajan, V. Kabaleeswaran, Geetha Gopalakrishnan, T. R. Govindachari, Meera Ramrakhiani, Phillip Lowe, Andrew Badley, David C. Cullen, H. Hermel, W. Schmahl, H. Möhwald, Nirmalya Majumdar, Joydip Das, András Dér, Loránd Kelemen, László Oroszi, András Hámori, Jeremy J. Ramsden, Pál Ormos, D. Savitri, Chanchal K. Mitra, Toshio Yanagida, Seiji Esaki, Yuji Kimura, Tomoyuki Nishida, Yosiyuki Sowa, M. Radu, V. K. Koltover, Ya. I. Estrin, L. A. Kasumova, V. P. Bubnov, E. E. Laukhina, Rajiv Dotta, M. Degaonkar, P. Raghunathan, Rama Jayasundar, Pavel Novák, Milan Marko, Ivan Zahradník, Hiroaki Hirata, Hidetake Miyata, J. Balaji, P. Sengupta, S. Maiti, M. Gonsalves, A. L. Barker, J. V. Macpherson, D. O’Hare, C. P. Winlove, P. R. Unwin, R. Phillip, S. Banerjee, G. Ravindra Kumar, K. Nagayaka, R. Danev, S. Sugitani, K. Murata, Michael Gősch, H. Blom, P. Thyberg, Z. Földes-Papp, G. Björk, J. Holm, T. Heino, Masashi Yokochi, Fuyuhiko Inagaki, Masami Kusunoki, E. K. Matthews, J. Pines, Yu. P. Chukova, Vitaly K. Koltover, Geetanjali Bansal, Uma Singh, M. P. Bansal, Kotoko Nakata, Tastuya Nakano, Tsuguchika Kaminuma, B. P. S. Kang, U. Singh, Bonn Kirn, Neja Potocnik, Vito Stare, Latal Shukla, V. Natarajan, T. P. A. Devasagayam, M. D. Sastry, P. C. Kesavan, R. Sayfutdinov, V. V. Adamovich, D. Yu. Rogozin, A. G. Degermendzhy, C. L. Khetrapal, G. A. Nagana Gowda, Kedar Nath Ghimire, Ishida Masaru, H. Fujita, S. Ishiwata, Y. Kishimoto, S. Kawahara, M. Suzuki, H. Mori, M. Mishina, Y. Kirino, H. Ohshima, A. S. Dukhin, V. N. Shilov, P. J. Goetz, and R. K. Mishra

Subjects
0303 health sciences, biology, General Medicine, 010402 general chemistry, 01 natural sciences, Horseradish peroxidase, General Biochemistry, Genetics and Molecular Biology, 0104 chemical sciences, 03 medical and health sciences, Biochemistry, Manganese porphyrin, biology.protein, Enzyme reconstitution, General Agricultural and Biological Sciences, 030304 developmental biology
Published
1999
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16. Modifying effect of nitric oxide on rat blood plasma proteins and hemoglobin

Author

M. Ia. Akhalaia, O. G. Luneva, A. A. Baizhumanov, N. Yu. Bryzgalova, Nadezda A. Brazhe, E. Yu. Parshina, Georgy V. Maksimov, Andrei B. Rubin, and I. V. Mikhailov

Subjects
Nitroprusside, Vasodilator Agents, Erythrocyte Membrane, Biophysics, Blood Proteins, General Chemistry, General Medicine, Blood Viscosity, Nitric Oxide, Biochemistry, Blood proteins, Rat blood, Rats, Nitric oxide, Oxygen, Hemoglobins, Plasma, chemistry.chemical_compound, chemistry, Animals, Hemoglobin, Protein Binding
Published
2007
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17. Role of viscosity and permeability of the erythrocyte plasma membrane in changes in oxygen-binding properties of hemoglobin during diabetes mellitus

Author

E. Matettuchi, O. G. Luneva, Georgy V. Maksimov, Rubin Ab, N. V. Maksimova, Pashchenko Vz, and E. A. Medvedev

Subjects
medicine.medical_specialty, Erythrocytes, Protoporphyrins, General Biochemistry, Genetics and Molecular Biology, Permeability, Viscosity, chemistry.chemical_compound, Hemoglobins, Diabetes mellitus, Internal medicine, medicine, Diabetes Mellitus, Homeostasis, Humans, Hematoporphyrin, Ions, Chemistry, Cell Membrane, Erythrocyte Membrane, General Medicine, Plasma, Hydrogen-Ion Concentration, medicine.disease, Oxygen, Hematoporphyrins, Membrane, Endocrinology, Cholesterol, Permeability (electromagnetism), Case-Control Studies, Calcium, sense organs, Hemoglobin, Oxygen binding, Protein Binding
Abstract

Changes in viscosity and permeability of the plasma membrane and conformation of erythrocyte hemoglobin hematoporphyrin were found in patients with diabetes mellitus. The decrease in oxygen binding and increase in deoxyhemoglobin concentration during diabetes mellitus were accompanied by changes in viscosity and permeability of the membrane for Na+, H+, Ca2+, and K+. Our results suggest that oxygen-binding properties of hemoglobin depend on viscosity and permeability of the erythrocyte plasma membrane.

Published
2006

18. Changes in plasma membrane viscosity and hemoporphyrin conformation in erythrocyte hemoglobin under the conditions of ischemia and reperfusion of rat brain

Author

E.Y. Parshina, Nadezda A. Brazhe, V B Koshelev, M Y Akhalaya, A E Demidova, O E Fadyukova, Georgy V. Maksimov, O. G. Luneva, and A. A. Baizhumanov

Subjects
medicine.medical_specialty, Erythrocytes, Biophysics, Ischemia, Biochemistry, Brain Ischemia, Brain ischemia, chemistry.chemical_compound, Hemoglobins, Internal medicine, Blood plasma, medicine, Animals, chemistry.chemical_classification, Reactive oxygen species, Chemistry, Superoxide, Viscosity, Erythrocyte Membrane, General Chemistry, General Medicine, Heparin, Hypoxia (medical), medicine.disease, Rats, Hematoporphyrins, Endocrinology, Reperfusion Injury, Hemoglobin, medicine.symptom, medicine.drug
Abstract

Hypoxia of various origin and localization is accompanied by changes in some physical and chemical properties of erythrocytes: deformability, plasma membrane viscosity, and the oxygen-binding capacity of hemoglobin [1, 4‐6]. Under the conditions of brain ischemia, these properties are studied insufficiently. After postischemic reperfusion (PIR) that restores blood circulation, the oxygen partial pressure in plasma increases, which may stimulate the generation of reactive oxygen species (ROS) and affect the erythrocyte functions. In blood plasma, Cu,Zn-superoxide dismutase (SOD) and ceruloplasmin (CP) are involved in utilization of superoxide anion radical ( ) that triggers ROS formation. In this study, changes in the viscosity of erythrocyte plasma membrane and the e 2 -binding ability of hemoporphyrin of deoxyhemoglobin were studied. SOD activity and CP level were also measured in blood plasma of rats with brain ischemia before and after brain PIR. White outbred male rats weighing 272 ± 11 g were used in experiments. The animals were divided into three groups: the sham-operated rats (the control) ( n = 10), the rats with brain ischemia ( n = 10), and the rats with postischemic brain reperfusion ( n = 7). One day before the experiment, both carotids of the anesthetized animals were underpinned with a fishing line (0.3 mm) that was later withdrawn under skin through the polyethylene tubes into the interscapular region. After one day, a one-stage complete occlusion of both carotids was induced by carotid retraction into the tubes by means of the fishing line; subsequent release of carotids led to PIR. Blood samples (3 ml of blood mixed with heparin, 10 U/ml) were taken from the jugular veins of

Published
2006

19. Investigation of erythrocyte shape, plasma membrane fluidity and conformation of haemoglobin haemoporphyrin under the influence of long-term space flight

Author

A I, Grigoriev, G V, Maksimov, B V, Morukov, S M, Ivanova, Yu V, Yarlikova, O G, Luneva, N A, Ulyanova, E Yu, Parshina, and A B, Rubin

Subjects
Hemoglobins, Cholesterol, Erythrocytes, Porphyrins, Membrane Fluidity, Weightlessness, Erythrocyte Deformability, Erythrocyte Membrane, Humans, Space Flight, Phospholipids
Abstract

The investigation of long-term space flight (SF) effect on the blood cells function is of great importance for modern space biology and medicine. We established that the number of discocytes decreased in the period of early rehabilitation after long-term SF. After SF plasma membrane fluidity and phospholipid content decreased and cholesterol content increased. After SF the amount of haemoglobin decreased and the parameters characterizing haemoglobin haemoporyphyrin (HH) conformation changed. We suppose that erythrocyte shape, membrane fluidity and HH conformation are among factors affecting oxygen transfer during and after space flight.

Published
2005

20. [Interaction of nonelectrolytes, the derivatives of 5-hydroxybenzimidazole, with erythrocyte membrane]

Author

O G, Luneva, L Ia, Gendel, Iu V, Kuznetsov, and L D, Smirnov

Subjects
Male, Erythrocytes, Erythrocyte Membrane, Electron Spin Resonance Spectroscopy, Microscopy, Electron, Scanning, Animals, Benzimidazoles, Spin Labels, In Vitro Techniques, Cell Shape, Antioxidants, Rats
Abstract

The method of spin probe and scanning electron microscopy were used to study the effects of some new synthetic antioxidants and bioregulators, the derivatives of 5-hydroxybenzimidazole, on the membrane structure and morphology of erythrocytes. Analysis of EPR spectra and electron micrographs revealed that the derivatives with various side substituents affect the membrane structure and shape of erythrocytes in a concentration-dependent manner, the effect correlating with the hydrophobic properties of the side derivatives. It was shown that all the compounds in the concentration range 1.10(-7) - 1.10(-3) M exhibit the echinocytogenic action, the most profound effect being found in the compound with benzyl- and ethoxygroup in sites 2 and 5, respectively. Our data suggest that nonelectrolytes, the derivatives of 5-hydroxybenzimidazole, are located in the outer monolayer of erythrocyte membrane.

Published
2005

21. Erythrocyte membrane fluidity and haemoglobin haemoporphyrin conformation: features revealed in patients with heart failure

Author

O. G. Luneva, E I Chazov, O. V. Rodnenkov, Georgy V. Maksimov, Andrei B. Rubin, N.A. Ulyanova, and Sergei N. Orlov

Subjects
medicine.medical_specialty, chemistry.chemical_element, Hypoxia (medical), medicine.disease, Oxygen, Pathology and Forensic Medicine, Nitric oxide, Pathogenesis, chemistry.chemical_compound, Endocrinology, Membrane, chemistry, Biochemistry, Physiology (medical), Heart failure, Internal medicine, medicine, Membrane fluidity, Globin, medicine.symptom
Abstract

This study examined the possible involvement of abnormal erythrocyte oxygen (O 2 ) transport in the pathogenesis of heart failure. Haemoglobin (Hb) haemoporphyrin conformation was assessed by Raman spectroscopy (RS) of blood samples, whereas membrane fluidity was estimated at depths of 0.6–0.8 and 2.2nm by electron-paramagnetic resonance spectroscopy of erythrocytes loaded with spin-labeled 5-doxylstearic acid and 16-doxylstearic acid, respectively. The fluidity of erythrocyte membranes from patients with heart failure was decreased in the area near the membrane surface and remained unchanged in the deeper hydrophobic membrane regions. The same differences were also detected in healthy controls subjected to chronic high-altitude hypoxia. RS demonstrated that in heart failure the total content of Hb–ligand complexes and the relative content of Hb–nitric oxide (NO) complexes with cleaved Fe 2+ -globin bond was decreased, whereas content of Hb–NO complexes with preserved Fe 2+ -globin bond was increased. We propose that this phenomenon contributes to the reduced O 2 tissue supply seen in patients with heart failure.

Published
2004

22. [Features of organic nonelectrolyte binding to the erythrocyte membrane]

Author

O G, Luneva, L Ia, Gendel', and K E, Krugliakova

Subjects
Electrolytes, Erythrocyte Membrane, Electron Spin Resonance Spectroscopy, Humans, Organic Chemicals
Abstract

The capacity of erythrocyte membranes for organic nonelectrolytes from different chemical groups of chemical compounds was studied by the spin probe method and scanning electron microscopy. Hydrophobic spin-labeled derivatives of gamma-carbolin and stearic acid and the screened phenol antioxidant fenozan-1 were used as nonelectrolytes. Based on the analysis of electron spin resonance spectra of the hydrophobic spin-labeled nonelectrolytes and electron micrographs of erythrocytes, differences in the capacity of distribution regions in the intramembrane space of the derivative of gamma-carbolin and fenozan-1, on the one hand, and the spin-labeled derivative of fatty acid, on the other hand, were found. The first group has at least two membrane distribution regions, whereas in the second case only one type of distribution was found. The influence of limited membrane capacity on the realization of biological activity of organic nonelectrolytes is discussed.

Published
2002

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