@article{MTMT:34232792,
	title = {Estimating the true stability of the prehydrolytic outward-facing state in an ABC protein.},
	url = {https://m2.mtmt.hu/api/publication/34232792},
	author = {Simon, Márton and Iordanov, Iordan and Szöllősi, András and Csanády, László},
	doi = {10.7554/eLife.90736},
	journal-iso = {ELIFE},
	journal = {ELIFE},
	volume = {12},
	unique-id = {34232792},
	issn = {2050-084X},
	abstract = {CFTR, the anion channel mutated in cystic fibrosis patients, is a model ABC protein whose ATP-driven conformational cycle is observable at single-molecule level in patch-clamp recordings. Bursts of CFTR pore openings are coupled to tight dimerization of its two nucleotide-binding domains (NBDs) and in wild-type (WT) channels are mostly terminated by ATP hydrolysis. The slow rate of non-hydrolytic closure - which determines how tightly bursts and ATP hydrolysis are coupled - is unknown, as burst durations of catalytic site mutants span a range of ~200-fold. Here, we show that Walker A mutation K1250A, Walker B mutation D1370N, and catalytic glutamate mutations E1371S and E1371Q all completely disrupt ATP hydrolysis. True non-hydrolytic closing rate of WT CFTR approximates that of K1250A and E1371S. That rate is slowed ~15-fold in E1371Q by a non-native inter-NBD H-bond, and accelerated ~15-fold in D1370N. These findings uncover unique features of the NBD interface in human CFTR.},
	keywords = {ZEBRAFISH; Xenopus; molecular biophysics; Structural biology; D-loop; composite ATP-binding site; flickery closure; mutant cycle},
	year = {2023},
	eissn = {2050-084X},
	orcid-numbers = {Iordanov, Iordan/0000-0001-8251-5857; Szöllősi, András/0000-0002-5570-4609; Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:31397038,
	title = {Simple binding of protein kinase A, prior to phosphorylation, allows CFTR anion channels to be opened by nucleotides},
	url = {https://m2.mtmt.hu/api/publication/31397038},
	author = {Mihályi, Csaba and Iordanov, Iordan and Törőcsik, Beáta and Csanády, László},
	doi = {10.1073/pnas.2007910117},
	journal-iso = {P NATL ACAD SCI USA},
	journal = {PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA},
	volume = {117},
	unique-id = {31397038},
	issn = {0027-8424},
	year = {2020},
	eissn = {1091-6490},
	pages = {21740-21746},
	orcid-numbers = {Mihályi, Csaba/0000-0001-7536-3066; Iordanov, Iordan/0000-0001-8251-5857; Törőcsik, Beáta/0000-0002-9838-3710; Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:31365406,
	title = {Selective profiling of N- And C-terminal nucleotide-binding sites in a TRPM2 channel},
	url = {https://m2.mtmt.hu/api/publication/31365406},
	author = {Tóth, Balázs and Iordanov, Iordan and Csanády, László},
	doi = {10.1085/jgp.201912533},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {152},
	unique-id = {31365406},
	issn = {0022-1295},
	abstract = {Transient receptor potential melastatin 2 (TRPM2) is a homotetrameric Ca2+-permeable cation channel important for the immune response, body temperature regulation, and insulin secretion, and is activated by cytosolic Ca2+ and ADP ribose (ADPR). ADPR binds to two distinct locations, formed by large N- and C-terminal cytosolic domains, respectively, of the channel protein. In invertebrate TRPM2 channels, the C-terminal site is not required for channel activity but acts as an active ADPR phosphohydrolase that cleaves the activating ligand. In vertebrate TRPM2 channels, the C-terminal site is catalytically inactive but cooperates with the N-terminal site in channel activation. The precise functional contributions to channel gating and the nucleotide selectivities of the two sites in various species have not yet been deciphered. For TRPM2 of the sea anemone Nematostella vectensis (nvTRPM2), catalytic activity is solely attributable to the C-terminal site. Here, we show that nvTRPM2 channel gating properties remain unaltered upon deletion of the C-terminal domain, indicating that the N-terminal site is single-handedly responsible for channel gating. Exploiting such functional independence of the N- and C-terminal sites, we selectively measure their affinity profiles for a series of ADPR analogues, as reflected by apparent affinities for channel activation and catalysis, respectively. Using site-directed mutagenesis, we confirm that the same N-terminal site observed in vertebrate TRPM2 channels was already present in ancient cnidarians. Finally, by characterizing the functional effects of six amino acid side chain truncations in the N-terminal site, we provide first insights into the mechanistic contributions of those side chains to TRPM2 channel gating. © 2020 Tóth et al. This article is distributed under the terms of an Attribution-Noncommercial-Share Alike-No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution-Noncommercial-Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/).},
	year = {2020},
	eissn = {1540-7748},
	orcid-numbers = {Tóth, Balázs/0000-0002-1257-2597; Iordanov, Iordan/0000-0001-8251-5857; Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:30637149,
	title = {Enzyme activity and selectivity filter stability of ancient TRPM2 channels were simultaneously lost in early vertebrates},
	url = {https://m2.mtmt.hu/api/publication/30637149},
	author = {Iordanov, Iordan and Tóth, Balázs and Szöllősi, András and Csanády, László},
	doi = {10.7554/eLife.44556},
	journal-iso = {ELIFE},
	journal = {ELIFE},
	volume = {8},
	unique-id = {30637149},
	issn = {2050-084X},
	abstract = {Transient Receptor Potential Melastatin 2 (TRPM2) is a cation channel important for the immune response, insulin secretion, and body temperature regulation. It is activated by cytosolic ADP ribose (ADPR) and contains a nudix-type motif 9 (NUDT9)-homology (NUDT9-H) domain homologous to ADPR phosphohydrolases (ADPRases). Human TRPM2 (hsTRPM2) is catalytically inactive due to mutations in the conserved Nudix box sequence. Here, we show that TRPM2 Nudix motifs are canonical in all invertebrates but vestigial in vertebrates. Correspondingly, TRPM2 of the cnidarian Nematostella vectensis (nvTRPM2) and the choanoflagellate Salpingoeca rosetta (srTRPM2) are active ADPRases. Disruption of ADPRase activity fails to affect nvTRPM2 channel currents, reporting a catalytic cycle uncoupled from gating. Furthermore, pore sequence substitutions responsible for inactivation of hsTRPM2 also appeared in vertebrates. Correspondingly, zebrafish (Danio rerio) TRPM2 (drTRPM2) and hsTRPM2 channels inactivate, but srTRPM2 and nvTRPM2 currents are stable. Thus, catalysis and pore stability were lost simultaneously in vertebrate TRPM2 channels.},
	keywords = {Xenopus; E. coli; molecular biophysics; Structural biology; Selectivity filter; ADP ribose; Nudix hydrolase; channel enzyme; rundown},
	year = {2019},
	eissn = {2050-084X},
	orcid-numbers = {Iordanov, Iordan/0000-0001-8251-5857; Tóth, Balázs/0000-0002-1257-2597; Szöllősi, András/0000-0002-5570-4609; Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:3341707,
	title = {Local and Global Dynamics in Klebsiella pneumoniae Outer Membrane Protein a in Lipid Bilayers Probed at Atomic Resolution},
	url = {https://m2.mtmt.hu/api/publication/3341707},
	author = {Saurel, O and Iordanov, Iordan and Nars, G and Demange, P and Le Marchand, T and Andreas, LB and Pintacuda, G and Milon, A},
	doi = {10.1021/jacs.6b11565},
	journal-iso = {J AM CHEM SOC},
	journal = {JOURNAL OF THE AMERICAN CHEMICAL SOCIETY},
	volume = {139},
	unique-id = {3341707},
	issn = {0002-7863},
	abstract = {The role of membrane proteins in cellular mechanism strongly depends on their dynamics, and solid-state magic-angle spinning (MAS) nuclear magnetic resonance (NMR) is a unique method to exhaustively characterize motions of proteins in a lipid environment. Herein, we make use of advances in H-1-detected MAS NMR to describe the dynamics of the membrane domain of the Outer membrane protein A of Klebsiella pneumoniae (KpOmpA). By measuring H-1-N-15 dipolar coupling as well as N-15 R-1 and R-1 rho relaxation rates at fast (60 kHz) MAS and high magnetic field (1 GHz), we were able to describe the motions of the residues of the beta-barrel as a collective rocking of low amplitude and of hundreds of nanoseconds time scale. Residual local motions at the edges of the strands, underscored by enhanced (NT)-N-15 R-1 rho relaxation rates, report on the mobility of the connected loops. In agreement with MAS NMR data, proteolysis experiments performed on the full length KpOmpA as well as on its membrane domain, reconstituted in liposomes or in detergent micelles, revealed in all cases the existence of a unique trypsin cleavage site within the membrane domain (out of 16 potential Lys and Arg sites). This site is located in the extracellular loop L3, showing that it is highly accessible to protein-protein interactions. KpOmpA is involved in cell-cell recognition, for adhesion and immune response mechanisms. The L3 region may therefore play a key role in pathogenicity.},
	keywords = {BACKBONE DYNAMICS; CONFORMATIONAL DYNAMICS; Solid-state NMR; MAS NMR; TRANSMEMBRANE DOMAIN; SPIN-LATTICE-RELAXATION; CRYSTALLINE PROTEIN; RESONANCE ASSIGNMENT; FULLY PROTONATED PROTEINS; HETERONUCLEAR DIPOLAR COUPLINGS},
	year = {2017},
	eissn = {1520-5126},
	pages = {1590-1597},
	orcid-numbers = {Iordanov, Iordan/0000-0001-8251-5857}
}

@article{MTMT:2940351,
	title = {Abolition of mitochondrial substrate-level phosphorylation by itaconic acid produced by LPS-induced Irg1 expression in cells of murine macrophage lineage},
	url = {https://m2.mtmt.hu/api/publication/2940351},
	author = {Németh, Beáta and Dóczi, Judit and Csete, Dániel and Kacsó, Gergely and Ravasz, Dóra and Daniel, Adams and Kiss, Gergely and Nagy, Ádám Miklós and Horváth, Gergő and Tretter, László and Mócsai, Attila and Csépányi-Kömi, Roland and Iordanov, Iordan and Ádám, Veronika and Chinopoulos, Christos},
	doi = {10.1096/fj.15-279398},
	journal-iso = {FASEB J},
	journal = {FASEB JOURNAL},
	volume = {30},
	unique-id = {2940351},
	issn = {0892-6638},
	year = {2016},
	eissn = {1530-6860},
	pages = {286-300},
	orcid-numbers = {Németh, Beáta/0000-0002-2334-9796; Dóczi, Judit/0000-0002-5797-5074; Csete, Dániel/0000-0001-8057-225X; Kacsó, Gergely/0000-0003-0428-3645; Ravasz, Dóra/0000-0002-0510-3282; Nagy, Ádám Miklós/0000-0002-9568-2555; Horváth, Gergő/0000-0001-5386-9509; Tretter, László/0000-0001-5638-2886; Mócsai, Attila/0000-0002-0512-1157; Csépányi-Kömi, Roland/0000-0001-6825-7142; Iordanov, Iordan/0000-0001-8251-5857; Ádám, Veronika/0000-0002-8350-8701; Chinopoulos, Christos/0000-0003-0183-4149}
}

@article{MTMT:3105008,
	title = {The proposed channel-enzyme transient receptor potential melastatin 2 does not possess ADP ribose hydrolase activity},
	url = {https://m2.mtmt.hu/api/publication/3105008},
	author = {Iordanov, Iordan and Mihályi, Csaba and Tóth, Balázs and Csanády, László},
	doi = {10.7554/eLife.17600},
	journal-iso = {ELIFE},
	journal = {ELIFE},
	volume = {5},
	unique-id = {3105008},
	issn = {2050-084X},
	year = {2016},
	eissn = {2050-084X},
	orcid-numbers = {Iordanov, Iordan/0000-0001-8251-5857; Mihályi, Csaba/0000-0001-7536-3066; Tóth, Balázs/0000-0002-1257-2597; Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:3099231,
	title = {Two transgenic mouse models for beta subunit components of succinate-CoA ligase yielding pleiotropic metabolic alterations},
	url = {https://m2.mtmt.hu/api/publication/3099231},
	author = {Kacsó, Gergely and Ravasz, Dóra and Dóczi, Judit and Németh, Beáta and Madgar, O and Saada, A and Ilin, P and Miller, C and Ostergaard, E and Iordanov, Iordan and Adams, D and Vargedo, Z and Araki, M and Araki, K and Nakahara, M and Ito, H and Gál, Anikó and Molnár, Mária Judit and Nagy, Zsolt and Patócs, Attila Balázs and Ádám, Veronika and Chinopoulos, Christos},
	doi = {10.1042/BCJ20160594},
	journal-iso = {BIOCHEM J},
	journal = {BIOCHEMICAL JOURNAL},
	volume = {473},
	unique-id = {3099231},
	issn = {0264-6021},
	abstract = {Succinate-CoA ligase is a heterodimer enzyme composed of Suclg1 -alpha- and a substrate-specific Sucla2 or Suclg2 -beta- subunit yielding ATP or GTP, respectively. In humans, the deficiency of this enzyme leads to encephalomyopathy with, or without methylmalonyl aciduria, in addition to resulting in mitochondrial DNA depletion. We generated mice lacking either one Sucla2 or Suclg2 allele. Sucla2 heterozygote mice exhibited tissue- and age-dependent decreases in Sucla2 expression associated with decreases in ATP-forming activity, but rebound increases in cardiac Suclg2 expression and GTP-forming activity. Bioenergetic parameters including substrate-level phosphorylation were not different between wild type and Sucla2 heterozygote mice unless a submaximal pharmacological inhibition of succinate-CoA ligase was concomitantly present. mtDNA contents were moderately decreased, but blood carnitine esters were significantly elevated. Suclg2 heterozygote mice exhibited decreases in Suclg2 expression but no rebound increases in Sucla2 expression or changes in bioenergetic parameters. Surprisingly, deletion of one Suclg2 allele in Sucla2 heterozygote mice still led to a rebound but protracted increase in Suclg2 expression, yielding double heterozygote mice with no alterations in GTP-forming activity or substrate-level phosphorylation, but more pronounced changes in mtDNA content and blood carnitine esters, and an increase in succinate dehydrogenase activity. We conclude that a partial reduction in Sucla2 elicits rebound increases in Suclg2 expression which is sufficiently dominant to overcome even a concomitant deletion of one Suclg2 allele, pleiotropically affecting metabolic pathways associated with succinate-CoA ligase. These results as well as the availability of the transgenic mouse colonies will be of value in understanding succinate-CoA ligase deficiency.},
	year = {2016},
	eissn = {1470-8728},
	pages = {3463-3485},
	orcid-numbers = {Kacsó, Gergely/0000-0003-0428-3645; Ravasz, Dóra/0000-0002-0510-3282; Dóczi, Judit/0000-0002-5797-5074; Németh, Beáta/0000-0002-2334-9796; Iordanov, Iordan/0000-0001-8251-5857; Gál, Anikó/0000-0002-2059-5748; Molnár, Mária Judit/0000-0001-9350-1864; Patócs, Attila Balázs/0000-0001-7506-674X; Ádám, Veronika/0000-0002-8350-8701; Chinopoulos, Christos/0000-0003-0183-4149}
}

@article{MTMT:2949645,
	title = {Ruling out pyridine dinucleotides as true TRPM2 channel activators reveals novel direct agonist ADP-ribose-2'-phosphate},
	url = {https://m2.mtmt.hu/api/publication/2949645},
	author = {Tóth, Balázs and Iordanov, Iordan and Csanády, László},
	doi = {10.1085/jgp.201511377},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {145},
	unique-id = {2949645},
	issn = {0022-1295},
	abstract = {Transient receptor potential melastatin 2 (TRPM2), a Ca(2+)-permeable cation channel implicated in postischemic neuronal cell death, leukocyte activation, and insulin secretion, is activated by intracellular ADP ribose (ADPR). In addition, the pyridine dinucleotides nicotinamide-adenine-dinucleotide (NAD), nicotinic acid-adenine-dinucleotide (NAAD), and NAAD-2'-phosphate (NAADP) have been shown to activate TRPM2, or to enhance its activation by ADPR, when dialyzed into cells. The precise subset of nucleotides that act directly on the TRPM2 protein, however, is unknown. Here, we use a heterologously expressed, affinity-purified-specific ADPR hydrolase to purify commercial preparations of pyridine dinucleotides from substantial contaminations by ADPR or ADPR-2'-phosphate (ADPRP). Direct application of purified NAD, NAAD, or NAADP to the cytosolic face of TRPM2 channels in inside-out patches demonstrated that none of them stimulates gating, or affects channel activation by ADPR, indicating that none of these dinucleotides directly binds to TRPM2. Instead, our experiments identify for the first time ADPRP as a true direct TRPM2 agonist of potential biological interest.},
	year = {2015},
	eissn = {1540-7748},
	pages = {419-430},
	orcid-numbers = {Tóth, Balázs/0000-0002-1257-2597; Iordanov, Iordan/0000-0001-8251-5857; Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:3110346,
	title = {Two classes of cholesterol binding sites for the β2AR revealed by thermostability and NMR},
	url = {https://m2.mtmt.hu/api/publication/3110346},
	author = {Gater, DL and Saurel, O and Iordanov, Iordan and Liu, W and Cherezov, V and Milon, A},
	doi = {10.1016/j.bpj.2014.10.011},
	journal-iso = {BIOPHYS J},
	journal = {BIOPHYSICAL JOURNAL},
	volume = {107},
	unique-id = {3110346},
	issn = {0006-3495},
	abstract = {Cholesterol binding to G protein-coupled receptors (GPCRs) and modulation of their activities in membranes is a fundamental issue for understanding their function. Despite the identification of cholesterol binding sites in high-resolution x-ray structures of the β2 adrenergic receptor (β2AR) and other GPCRs, the binding affinity of cholesterol for this receptor and exchange rates between the free and bound cholesterol remain unknown. In this study we report the existence of two classes of cholesterol binding sites in β2AR. By analyzing the β2AR unfolding temperature in lipidic cubic phase (LCP) as a function of cholesterol concentration we observed high-affinity cooperative binding of cholesterol with sub-nM affinity constant. In contrast, saturation transfer difference (STD) NMR experiments revealed the existence of a second class of cholesterol binding sites, in fast exchange on the STD NMR timescale. Titration of the STD signal as a function of cholesterol concentration provided a lower limit of 100 mM for their dissociation constant. However, these binding sites are specific for both cholesterol and β2AR, as shown with control experiments using ergosterol and a control membrane protein (KpOmpA). We postulate that this specificity is mediated by the high-affinity bound cholesterol molecules and propose the formation of transient cholesterol clusters around the high-affinity binding sites. © 2014 Biophysical Society.},
	keywords = {Humans; metabolism; TEMPERATURE; BINDING SITES; BINDING SITE; human; Chemistry; Protein Binding; Substrate Specificity; Protein Stability; cholesterol; Protein Denaturation; Magnetic Resonance Spectroscopy; Nuclear magnetic resonance spectroscopy; enzyme specificity; Receptors, Adrenergic, beta-2; beta 2 adrenergic receptor},
	year = {2014},
	eissn = {1542-0086},
	pages = {2305-2312},
	orcid-numbers = {Iordanov, Iordan/0000-0001-8251-5857}
}

@article{MTMT:2762109,
	title = {Putative chanzyme activity of TRPM2 cation channel is unrelated to pore gating},
	url = {https://m2.mtmt.hu/api/publication/2762109},
	author = {Tóth, Balázs and Iordanov, Iordan and Csanády, László},
	doi = {10.1073/pnas.1412449111},
	journal-iso = {P NATL ACAD SCI USA},
	journal = {PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA},
	volume = {111},
	unique-id = {2762109},
	issn = {0027-8424},
	year = {2014},
	eissn = {1091-6490},
	pages = {16949-16954},
	orcid-numbers = {Tóth, Balázs/0000-0002-1257-2597; Iordanov, Iordan/0000-0001-8251-5857; Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:3110796,
	title = {The transmembrane protein KpOmpA anchoring the outer membrane of Klebsiella pneumoniae unfolds and refolds in response to tensile load},
	url = {https://m2.mtmt.hu/api/publication/3110796},
	author = {Bosshart, PD and Iordanov, Iordan and Garzon-Coral, C and Demange, P and Engel, A and Milon, A and Müller, DJ},
	doi = {10.1016/j.str.2011.11.002},
	journal-iso = {STRUCTURE},
	journal = {STRUCTURE},
	volume = {20},
	unique-id = {3110796},
	issn = {0969-2126},
	abstract = {In Klebsiella pneumoniae the transmembrane β-barrel forming outer membrane protein KpOmpA mediates adhesion to a wide range of immune effector cells, thereby promoting respiratory tract and urinary infections. As major transmembrane protein OmpA stabilizes Gram-negative bacteria by anchoring their outer membrane to the peptidoglycan layer. Adhesion, osmotic pressure, hydrodynamic flow, and structural deformation apply mechanical stress to the bacterium. This stress can generate tensile load to the peptidoglycan-binding domain (PGBD) of KpOmpA. To investigate how KpOmpA reacts to mechanical stress, we applied a tensile load to the PGBD and observed a detailed unfolding pathway of the transmembrane β-barrel. Each step of the unfolding pathway extended the polypeptide connecting the bacterial outer membrane to the peptidoglycan layer and absorbed mechanical energy. After relieving the tensile load, KpOmpA reversibly refolded back into the membrane. These results suggest that bacteria may reversibly unfold transmembrane proteins in response to mechanical stress. © 2012 Elsevier Ltd.},
	keywords = {ARTICLE; Cell Adhesion; Bacteria (microorganisms); priority journal; nonhuman; Protein Binding; Protein Folding; Models, Molecular; Protein Conformation; hydrodynamics; unclassified drug; lipid membrane; tensile strength; Stress, Mechanical; Osmotic Pressure; protein structure; Negibacteria; bacterial protein; mechanical stress; PEPTIDOGLYCAN; Bacterial Outer Membrane Proteins; klebsiella pneumoniae; outer membrane; Protein Unfolding; outer membrane protein A; bacterial outer membrane; protein kpompa},
	year = {2012},
	eissn = {1878-4186},
	pages = {121-127},
	orcid-numbers = {Iordanov, Iordan/0000-0001-8251-5857}
}

@article{MTMT:3110595,
	title = {Dynamics of Klebsiella pneumoniae OmpA transmembrane domain: The four extracellular loops display restricted motion behavior in micelles and in lipid bilayers},
	url = {https://m2.mtmt.hu/api/publication/3110595},
	author = {Iordanov, Iordan and Renault, Marie and Réat, Valérie and Bosshart, Patrick D and Engel, Andreas and Saurel, Olivier and Milon, Alain},
	doi = {10.1016/j.bbamem.2012.05.004},
	journal-iso = {BBA-BIOMEMBRANES},
	journal = {BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES},
	volume = {1818},
	unique-id = {3110595},
	issn = {0005-2736},
	abstract = {The transmembrane domain of Klebsiella pneumoniae OmpA (KpOmpA) possesses four long extracellular loops that exhibit substantial sequence variability throughout OmpA homologs in Enterobacteria, in comparison with the highly conserved membrane-embedded β-barrel core. These loops are responsible for the immunological properties of the protein, including cellular and humoral recognition. In addition to key features revealed by structural elucidation of the KpOmpA transmembrane domain in detergent micelles, studies of protein dynamics provide insight into its function and/or mechanism of action. We have investigated the dynamics of KpOmpA in a lipid bilayer, using magic angle spinning solid-state NMR. The dynamics of the β-barrel and loop regions were probed by the spin–lattice relaxation times of the Cα and Cβ atoms of the serine and threonine residues, and by cross-polarization dynamics. The β-barrel core of the protein is rigid; the C-terminal halves of two of the four extracellular loops (L1 and L3), which are particularly long in KpOmpA, are highly mobile. The other two loops (L2 and L4), which are very similar to their homologs in Escherichia coli OmpA, and the N-terminal halves of L1 and L3 exhibit more restricted motions. We suggest a correlation between the sequence variability and the dynamics of certain loop regions, which accounts for their respective contributions to the structural and immunological properties of the protein.},
	keywords = {electron microscopy; Spin–lattice relaxation; Solid-state NMR; PROTEIN DYNAMICS; outer membrane protein A; Protein reconstitution},
	year = {2012},
	eissn = {1879-2642},
	pages = {2344-2353},
	orcid-numbers = {Iordanov, Iordan/0000-0001-8251-5857}
}

@article{MTMT:3110803,
	title = {Electrodelivery of drugs into cancer cells in the presence of poloxamer 188},
	url = {https://m2.mtmt.hu/api/publication/3110803},
	author = {Tsoneva, I and Iordanov, Iordan and Berger, AJ and Tomov, T and Nikolova, B and Mudrov, N and Berger, MR},
	doi = {10.1155/2010/314213},
	journal-iso = {J BIOMED BIOTECHNOL},
	journal = {JOURNAL OF BIOMEDICINE AND BIOTECHNOLOGY},
	volume = {2010},
	unique-id = {3110803},
	issn = {1110-7243},
	abstract = {In the present study it is shown that poloxamer 188, added before or immediately after an electrical pulse used for electroporation, decreases the number of dead cells and at the same time does not reduce the number of reversible electropores through which small molecules (cisplatin, bleomycin, or propidium iodide) can pass/diffuse. It was suggested that hydrophobic sections of poloxamer 188 molecules are incorporated into the edges of pores and that their hydrophilic parts act as brushy pore structures. The formation of brushy pores may reduce the expansion of pores and delay the irreversible electropermeability. Tumors were implanted subcutaneously in both flanks of nude mice using HeLa cells, transfected with genes for red fluorescent protein and luciferase. The volume of tumors stopped to grow after electrochemotherapy and the use of poloxamer 188 reduced the edema near the electrode and around the subcutaneously growing tumors. © 2010 Iana Tsoneva et al.},
	keywords = {Animals; Humans; MICE; ARTICLE; MOUSE; human; Cell Survival; controlled study; ELECTROCHEMOTHERAPY; nonhuman; animal model; animal experiment; cell proliferation; electrode; Cell Line, Tumor; Flow Cytometry; Hela Cells; Spectrometry, Fluorescence; Hemolysis; Porosity; human cell; drug delivery system; Drug Delivery Systems; hydrophilicity; edema; poloxamer; Xenograft Model Antitumor Assays; Antineoplastic Agents; cisplatin; bleomycin; Jurkat Cells; Cell viability; Hydrophobicity; Mice, Nude; Hydrophobic and Hydrophilic Interactions; Mus musculus; Propidium; cancer cell; Luciferases; genetic transfection; Electroporation; propidium iodide; Luminescent Proteins; Whole Body Imaging},
	year = {2010},
	eissn = {1110-7251},
	orcid-numbers = {Iordanov, Iordan/0000-0001-8251-5857}
}

@article{MTMT:3110804,
	title = {Cytotoxic activity of platinum(II) and palladium(II) complexes of N-3-pyridinylmethanesulfonamide: The influence of electroporation},
	url = {https://m2.mtmt.hu/api/publication/3110804},
	author = {Dodoff, NI and Iordanov, Iordan and Tsoneva, I and Grancharov, K and Detcheva, R and Pajpanova, T and Berger, MR},
	journal-iso = {Z NATURFORSCH C},
	journal = {ZEITSCHRIFT FÜR NATURFORSCHUNG C-A JOURNAL OF BIOSCIENCES},
	volume = {64},
	unique-id = {3110804},
	issn = {0939-5075},
	abstract = {The series of complexes: cis-[Pd(PMSA)2X2], cis-[Pt(PMSA)2X2], trans-[Pt(PMSA)2I 2] and [Pt(PMSA)4]Cl2 (PMSA = N-3-pyridinyhnethanesulfonamide; X = Cl, Br, I), previously synthesized and characterized by us, as well as the free ligand PMSA, were tested for their cytotoxic activity without electroporation - against murine leukemia F4N and human SKW-3 and MDA-MB-231 tumour cell lines - and with electroporation - against the latter two cell lines. The majority of the complexes exhibited cytotoxic effects (IC50 < 100 μmol/1) under the conditions of electroporation. Both cis- and trans-[Pt(PMSA)2I2] had pronounced cytotoxic effects (29-61 μmol/I against MDA-MB-231 cells). © 2009 Verlag der Zeitschrift für Naturforschung Tübingen.},
	keywords = {Animals; Humans; MICE; ARTICLE; MOUSE; methodology; human; animal; PALLADIUM; Cell Survival; drug effect; Cell Line, Tumor; Sulfonamides; Cell Cycle; Models, Molecular; antineoplastic agent; chemical structure; Antineoplastic Agents; platinum complexes; Leukemia, Erythroblastic, Acute; sulfonamide; Murinae; Electroporation; tumor cell line; Platinum compounds; erythroleukemia; Leukemia, T-Cell; t cell leukemia; Pyrrolidines; pyrrolidine derivative; platinum derivative; Cytostatic agents; pyrrolidin-3-yl-methanesulfonic acid; pyrrolidin 3 yl methanesulfonic acid; methanesulfonamide},
	year = {2009},
	eissn = {1865-7125},
	pages = {179-185},
	orcid-numbers = {Iordanov, Iordan/0000-0001-8251-5857}
}