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1.

001-es BibID:BIBFORM060830
Első szerző:Alvarado, Gerardo
Cím:Heme-induced contractile dysfunction in Human cardiomyocytes caused by oxidant damage to thick filament proteins / Gerardo Alvarado, Viktória Jeney, Attila Tóth, Éva Csősz, Gergő Kalló, An T. Huynh, Csaba Hajnal, Judit Kalász, Enikő T. Pásztor, István Édes, Magnus Gram, Bo Akerström, Ann Smith, John W. Eaton, György Balla, Zoltán Papp, József Balla
Dátum:2015
ISSN:0891-5849
Megjegyzések:Intracellular free heme predisposes to oxidant-mediated tissue damage. We hypothesized that free heme causes alterations in myocardial contractility via disturbed structure and/or regulation of the contractile proteins. Isometric force production and its Ca2þ-sensitivity (pCa50) were monitored in permeabilized human ventricular cardiomyocytes. Heme exposure altered cardiomyocyte morphology and evoked robust decreases in Ca2þ-activated maximal active force (Fo) while increasing Ca2þ-independent passive force (Fpassive). Heme treatments, either alone or in combination with H2O2, did not affect pCa50. The increase in Fpassive started at 3 mM heme exposure and could be partially reversed by the antioxidant dithiothreitol. Protein sulfhydryl (SH) groups of thick myofilament content decreased and sulfenic acid formation increased after treatment with heme. Partial restoration in the SH group content was observed in a protein running at 140 kDa after treatment with dithiothreitol, but not in other proteins, such as filamin C, myosin heavy chain, cardiac myosin binding protein C, and α-actinin. Importantly, binding of heme to hemopexin or alpha-1-microglobulin prevented its effects on cardiomyocyte contractility, suggesting an allosteric effect. In line with this, free heme directly bound to myosin light chain 1 in human cardiomyocytes. Our observations suggest that free heme modifies cardiac contractile proteins via posttranslational protein modifications and via binding to myosin light chain 1, leading to severe contractile dysfunction. This may contribute to systolic and diastolic cardiac dysfunctions in hemolytic diseases, heart failure, and myocardial ischemia-reperfusion injury.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Cardiomyocyte
Contractile function
Heme
Calcium sensitivity
Myosin light chain 1
Cardiac myosin binding protein C
Myosin heavy chain
Titin
H2O2
Sulfenic acid Oxidation
Megjelenés:Free Radical Biology And Medicine. - 89 (2015), p. 248-262. -
További szerzők:Jeney Viktória (1971-) (vegyész, kémia tanár) Tóth Attila (1971-) (biológus) Csősz Éva (1977-) (biokémikus, molekuláris biológus) Kalló Gergő (1989-) (molekuláris biológus) Huynh, An T. Hajnal Csaba Kalász Judit (1986-) (molekuláris biológus) Pásztorné Tóth Enikő (1966-) (laboratóriumi analitikus) Édes István (1952-) (kardiológus) Gram, Magnus Akerström, Bo Smith, Ann Eaton, John W. Balla György (1953-) (csecsemő és gyermekgyógyász, neonatológus) Papp Zoltán (1965-) (kardiológus, élettanász) Balla József (1959-) (belgyógyász, nephrológus)
Pályázati támogatás:TÁMOP-4.2.2.A-11/1/KONV-2012-0045
TÁMOP
Kardiológia Kutatócsoport
TÁMOP-4.2.2/B-10/1-2010-0024
TÁMOP
Laki Kálmán Doktori Iskola
84300
OTKA
109083
OTKA
112333
OTKA
MTA-DE
MTA
Vascularis Biológia, Thrombosis-Haemostasis Kutatócsoport
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2.

001-es BibID:BIBFORM028392
Első szerző:Balla György (csecsemő és gyermekgyógyász, neonatológus)
Cím:Ferritin : a cytoprotective antioxidant strategem of endothelium / Balla G., Jacob H. S., Balla J., Rosenberg M., Nath K., Apple F., Eaton J. W., Vercellotti G. M.
Dátum:1992
Megjegyzések:Phagocyte-mediated oxidant damage to vascular endothelium is likely involved in various vasculopathies including atherosclerosis and pulmonary leak syndromes such as adult respiratory distress syndrome. We have shown that heme, a hydrophobic iron chelate, is rapidly incorporated into endothelial cells where, after as little as 1 h, it markedly aggravates cytotoxicity engendered by polymorphonuclear leukocyte oxidants or hydrogen peroxide (H2O2). In contrast, however, if cultured endothelial cells are briefly pulsed with heme and then allowed to incubate for a prolonged period (16 h), the cells become highly resistant to oxidant-mediated injury and to the accumulation of endothelial lipid peroxidation products. This protection is associated with the induction within 4 h of mRNAs for both heme oxygenase and ferritin. After 16 h heme oxygenase and ferritin have increased approximately 50-fold and 10-fold, respectively. Differential induction of these proteins determined that ferritin is probably the ultimate cytoprotectant. Ferritin inhibits oxidant-mediated cytolysis in direct relation to its intracellular concentration. Apoferritin, when added to cultured endothelial cells, is taken up in a dose-responsive manner and appears as cytoplasmic granules by immunofluorescence; in a similar dose-responsive manner, added apoferritin protects endothelial cells from oxidant-mediated cytolysis. Conversely, a site-directed mutant of ferritin (heavy chain Glu62----Lys; His65----Gly) which lacks ferroxidase activity and is deficient in iron sequestering capacity, is completely ineffectual as a cytoprotectant. We conclude that endothelium and perhaps other cell types may be protected from oxidant damage through the iron sequestrant, ferritin.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:The Journal of Biological Chemistry. - 267 : 25 (1992), p. 18148-18153. -
További szerzők:Jacob, Harry S. Balla József (1959-) (belgyógyász, nephrológus) Rosenberg, M. Nath, Karl Apple, F. Eaton, John W. Vercellotti, Gregory M.
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3.

001-es BibID:BIBFORM078592
Első szerző:Balla József (belgyógyász, nephrológus)
Cím:Role of heme in soft tissue mineralization / Balla József, Zarjou Abolfazl, Agarwal Anupam, Becs Gergely, Kovács Katalin, Nyitrai Mónika, Potor László, Pethő Dávid, Oros Melinda, Zavaczki Erzsébet, Arosio Paolo, Eaton John, Balla György
Dátum:2016
ISSN:0891-5849
Megjegyzések:Infiltration of red blood cells into atherosclerotic lesions is a common event in the progression of atherosclerosis. Recently we have observed that after infiltration and exposure of erythrocytes to plaque material, are lysed, and the liberated hemoglobin is oxidized to ferryl hemoglobin (FeIII/FeIV?O) and ferri (FeIII) hemoglobin. After oxidation of ferro (FeII) hemoglobin heme dissociates from globin then is translocated into resident cells including smooth muscle cells within arteries. Mounting evidence suggests an essential role for the heme oxygenase 1 (HO-1)/ferritin system to maintain homeostasis of vascular function. We examined whether induction of HO-1 and ferritin by heme alters mineralization of human smooth muscle cells provoked by phosphorous and vitamin D3 analogs. Upregulation of the HO-1/ferritin system inhibited human smooth muscle cells calcification and osteoblastic differentiation. Of the products of the system, only ferritin and, to a lesser extent, biliverdin were responsible for the inhibition. Ferritin heavy chain and ceruloplasmin, which both possess ferroxidase activity, inhibited calcification; a site-directed mutant of ferritin heavy chain, which lacked ferroxidase activity, failed to inhibit calcification. In addition, osteoblastic transformation of human smooth muscle cells (assessed by upregulation of core binding factor alpha-1, osteocalcin, and alkaline phosphatase activity) was diminished by ferritin/ferroxidase activity. Furthermore, iron-provoked inhibition of osteoblast activity was also demonstrated to be mediated by ferritin and its ferroxidase activity. We conclude that induction of the HO-1/ferritin system prevents calcification and osteoblastic differentiation of human smooth muscle cells mainly via the ferroxidase activity of ferritin.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idézhető absztrakt
heme
mineralization
Megjelenés:Free Radical Biology And Medicine. - 96 (2016), p. S13. -
További szerzők:Zarjou, Abolfazl (1979-) (kutató orvos) Agarwal, Anupam Becs Gergely Sikura Katalin Éva (1985-) (biológus) Nyitrai Mónika Potor László Pethő Dávid Oros Melinda (1975-) (molekuláris biológus) Zavaczki Erzsébet (1983-) (biotechnológus) Arosio, Paolo Eaton, John W. Balla György (1953-) (csecsemő és gyermekgyógyász, neonatológus)
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4.

001-es BibID:BIBFORM041564
Első szerző:Balla József (belgyógyász, nephrológus)
Cím:Heme, heme oxygenase and ferritin in vascular endothelial cell injury / József Balla, Gregory M. Vercellotti, Viktória Jeney, Akihiro Yachie, Emőke Nagy, John W. Eaton, György Balla
Dátum:2005
Tárgyszavak:Orvostudományok Klinikai orvostudományok könyvfejezet
Megjelenés:Heme oxygenase : the elegant orchestration of its products in medicine / ed. L. E. Otterbein, [et al]. - p. 351-375. -
További szerzők:Vercellotti, Gregory M. Jeney Viktória (1971-) (vegyész, kémia tanár) Yachie, Akihiro Nagy Emőke (neonatológus, gyermekgyógyász) Eaton, John W. Balla György (1953-) (csecsemő és gyermekgyógyász, neonatológus)
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5.

001-es BibID:BIBFORM041562
Első szerző:Balla József (belgyógyász, nephrológus)
Cím:Role of heme, heme oxygenase and ferritin in free radical mediated vascular endothelial cell injury / József Balla, Gregory M. Vercellotti, Karl A. Nath, John W. Eaton, John D. Belcher, Harry S. Jacob, György Balla
Dátum:1994
Tárgyszavak:Orvostudományok Klinikai orvostudományok könyvfejezet
Megjelenés:Free Radicals in the Environment, Medicine and Toxicology : Critical Aspects and Current Highlights / ed. by H. Nohl, H. Esterbauer, C. Rice-Evans. - p. 429-466.
További szerzők:Vercellotti, Gregory M. Nath, Karl Eaton, John W. Belcher, John D. Jacob, Harry S. Balla György (1953-) (csecsemő és gyermekgyógyász, neonatológus)
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6.

001-es BibID:BIBFORM041560
Első szerző:Balla József (belgyógyász, nephrológus)
Cím:Heme oxygenase and ferritin induction as a protective vessel wall endothelial cell response against free radical stress / J. Balla, G. M. Vercellotti, J. W. Eaton, H. S. Jacob, Gy. Balla
Dátum:1993
Tárgyszavak:Orvostudományok Klinikai orvostudományok könyvfejezet
Megjelenés:Oxygen Free Radicals and Scavengers in the Natural Sciences / eds. Gy. Mózsik, I. Emerit, J. Fehér, B. Matkovics, Á. Vincze. - p. 123-126.
További szerzők:Vercellotti, Gregory M. Eaton, John W. Jacob, Harry S. Balla György (1953-) (csecsemő és gyermekgyógyász, neonatológus)
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7.

001-es BibID:BIBFORM040822
035-os BibID:PMID:12817058
Első szerző:Balla József (belgyógyász, nephrológus)
Cím:Haem, haem oxygenase and ferritin in vascular endothelial cell injury / József Balla, Gregory M. Vercellotti, Karl Nath, Akihiro Yachie, Emőke Nagy, John W. Eaton, György Balla
Dátum:2003
Megjegyzések:Iron-derived reactive oxygen species (ROS) are implicated in the pathogenesis of numerous vascular disorders including atherosclerosis, microangiopathic haemolytic anaemia, vasculitis and reperfusion injury. One abundant source of redox-active iron is haem, which is inherently dangerous when released from intracellular haem proteins. The present review concerns the likely involvement of haem in vascular endothelial cell damage and the strategies used by endothelium to minimize such damage. Exposure of endothelial cells to haem greatly potentiates cell killing mediated by polymorphonuclear leukocytes and other sources of ROS. Free haem also promotes the conversion of low-density lipoprotein to cytotoxic oxidized products. If only because of its abundance, haemoglobin probably represents the most important potential source of haem within the vascular endothelium; free haemoglobin in plasma, when oxidized, can transfer haem to endothelium, thereby enhancing cellular susceptibility to oxidant-mediated injury. As a defence against such toxicity, upon exposure to free haem, endothelial cells up-regulate haem oxygenase-1 and ferritin. Haem oxygenase is a haem-degrading enzyme that opens the porphyrin ring, producing biliverdin, carbon monoxide and a most dangerous product-free redox-active iron. The latter can be controlled effectively by sequestration within ferritin, a multimeric protein with a very high capacity for storing iron. These homeostatic adjustments have been shown to be effective in the protection of endothelium against the damaging effects of exogenous haem and oxidants. The central importance of this protective system was highlighted recently by the discovery of a child diagnosed with haem oxygenase-1 deficiency, who exhibited extensive endothelial damage.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
külföldön készült közlemény
Megjelenés:Nephrology, dialysis, transplantation. - 18 : Suppl. 5. (2003), p. v8-v12. -
További szerzők:Vercellotti, Gregory M. Nath, Karl Yachie, Akihiro Nagy Emőke (neonatológus, gyermekgyógyász) Eaton, John W. Balla György (1953-) (csecsemő és gyermekgyógyász, neonatológus)
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8.

001-es BibID:BIBFORM028399
Első szerző:Balla József (belgyógyász, nephrológus)
Cím:Endothelial-cell heme uptake from heme proteins : induction of sensitization and desensitization to oxidant damage / J. Balla, H. S. Jacob, G. Balla, K. Nath, J. W. Eaton, G. M. Vercellotti
Dátum:1993
Megjegyzések:Iron-derived reactive oxygen species are implicated in the pathogenesis of various vascular disorders including atherosclerosis, vasculitis, and reperfusion injury. The present studies examine whether heme, when liganded to physiologically relevant proteins as in hemoglobin, can provide potentially damaging iron to intact endothelium. We demonstrate that reduced ferrohemoglobin, while relatively innocuous to cultured endothelial cells, when oxidized to ferrihemoglobin (methemoglobin), greatly amplifies oxidant (H2O2)-mediated endothelial-cell injury. Drawing upon our previous observation that free heme similarly primes endothelium for oxidant damage, we posited that methemoglobin, but not ferrohemoglobin, releases its hemes that can then be incorporated into endothelial cells. In support, cultured endothelial cells exposed to methemoglobin--in contrast to exposure to ferrohemoglobin, cytochrome c, or metmyoglobin--rapidly increased their heme oxygenase mRNA and enzyme activity, thereby supporting heme uptake; ferritin production was also markedly increased after such exposure, thus attesting to eventual incorporation of Fe. These cellular methemoglobin effects were inhibited by the heme-scavenging protein hemopexin and by haptoglobin or cyanide, agents that strengthen the liganding between heme and globin. If the endothelium is exposed to methemoglobin for a more prolonged period (16 hr), it accumulates large amounts of ferritin; concomitantly, and presumably associated with iron sequestration by this protein, the endothelium converts from hypersusceptible to hyperresistant to oxidative damage. We conclude that when oxidation of hemoglobin facilitates release of its heme groups, catalytically active iron is provided to neighboring tissue environments. The effect of this relinquished heme on the vasculature is determined both by extracellular factors--i.e., plasma proteins, such as haptoglobin and hemopexin--as well as intracellular factors, including heme oxygenase and ferritin. Acutely, if both extra- and intracellular defenses are overwhelmed, cellular toxicity arises; chronically, when ferritin is induced, resistance to oxidative injury may supervene.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Proceedings of the National Academy of Sciences of the United States of America. - 90 : 20 (1993), p. 9285-9289. -
További szerzők:Jacob, Harry S. Balla György (1953-) (csecsemő és gyermekgyógyász, neonatológus) Nath, Karl Eaton, John W. Vercellotti, Gregory M.
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elektronikus változat
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9.

001-es BibID:BIBFORM023029
Első szerző:Balla József (belgyógyász, nephrológus)
Cím:Heme, heme oxygenase and ferritin in vascular endothelial cell injury / Balla József, Vercellotti Gregory M., Jeney Viktória, Yachie Akihiro, Varga Zsuzsa, Eaton John W., Balla György
Dátum:2005
ISSN:1613-4125
Megjegyzések:Iron-derived reactive oxygen species are implicated in the pathogenesis of numerous vascular disorders including atherosclerosis, microangiopathic hemolytic anemia, vasculitis, and reperfusion injury. One abundant source of redox active iron is heme, which is inherently dangerous when released from intracellular heme proteins. The present review concerns the involvement of heme in vascular endothelial cell damage and the strategies used by endothelium to minimize such damage. Exposure of endothelium to heme greatly potentiates cell killing mediated by polymorphonuclear leukocytes and other sources of reactive oxygen. Free heme also promotes the conversion of low-density lipoprotein (LDL) into cytotoxic oxidized products. Only because of its abundance, hemoglobin probably represents the most important potential source of heme within the vascular endothelium; hemoglobin in plasma, when oxidized, transfers heme to endothelium and LDL, thereby enhancing cellular susceptibility to oxidant-mediated injury. As a defense against such toxicity, upon exposure to heme or hemoglobin, endothelial cells up-regulate heme oxygenase-1 and ferritin. Heme oxygenase-1 is a heme-degrading enzyme that opens the porphyrin ring, producing biliverdin, carbon monoxide, and the most dangerous product - free redox active iron. The latter can be effectively controlled by ferritin via sequestration and ferroxidase activity. Ferritin serves as a protective gene by virtue of antioxidant, antiapoptotic, and antiproliferative actions. These homeostatic adjustments have been shown effective in the protection of endothelium against the damaging effects of exogenous heme and oxidants. The central importance of this protective system was recently highlighted by a child diagnosed with heme oxygenase-1 deficiency, who exhibited extensive endothelial damage.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Molecular Nutrition and Food Research. - 49 : 11 (2005), p. 1030-1043. -
További szerzők:Vercellotti, Gregory M. Jeney Viktória (1971-) (vegyész, kémia tanár) Yachie, Akihiro Varga Zsuzsa (1951-) (biokémikus, nephrológus) Eaton, John W. Balla György (1953-) (csecsemő és gyermekgyógyász, neonatológus)
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10.

001-es BibID:BIBFORM002292
Első szerző:Balla József (belgyógyász, nephrológus)
Cím:Heme, heme oxygenase and ferritin : how the vascular endothelium survives (and dies) in an iron-rich environment / J. Balla, G. M. Vercellotti, V. Jeney, A. Yachie, Zs. Varga, H. S. Jacob, J. W. Eaton, Gy. Balla
Dátum:2007
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Antioxidants and Redox Signaling 9 : 12 (2007), p. 2119-2137. -
További szerzők:Vercellotti, Gregory M. Jeney Viktória (1971-) (vegyész, kémia tanár) Yachie, Akihiro Varga Zsuzsa (1951-) (biokémikus, nephrológus) Jacob, Harry S. Eaton, John W. Balla György (1953-) (csecsemő és gyermekgyógyász, neonatológus)
Internet cím:elektronikus változat
DOI
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11.

001-es BibID:BIBFORM061878
Első szerző:Becs Gergely
Cím:Pharmacological induction of ferritin prevents osteoblastic transformation of smooth muscle cells / Gergely Becs, Abolfazl Zarjou, Anupam Agarwal, Katalin Éva Kovács, Ádám Becs, Mónika Nyitrai, Enikő Balogh, Emese Bányai, John W. Eaton, Paolo Arosio, Maura Poli, Viktória Jeney, József Balla, György Balla
Dátum:2016
ISSN:1582-1838
Megjegyzések:Vascular calcification is a frequent complication of atherosclerosis, diabetes and chronic kidney disease. In the latter group of patients, calcification is commonly seen in tunica media where smooth muscle cells (SMC) undergo osteoblastic transformation. Risk factors such as elevated phosphorus levels and vitamin D3 analogues have been identified. In the light of earlier observations by our group and others, we sought to inhibit SMC calcification via induction of ferritin. Human aortic SMC were cultured using b-glycerophosphate with activated vitamin D3, or inorganic phosphate with calcium, and induction of alkaline phosphatase (ALP) and osteocalcin as well as accumulation of calcium were used to monitor osteoblastic transformation. In addition, to examine the role of vitamin D3 analogues, plasma samples from patients on haemodialysis who had received calcitriol or paricalcitol were tested for their tendency to induce calcification of SMC. Addition of exogenous ferritin mitigates the transformation of SMC into osteoblast-like cells. Importantly, pharmacological induction of heavy chain ferritin by 3H-1,2-Dithiole-3-thione was able to inhibit the SMC transition into osteoblast-like cells and calcification of extracellular matrix. Plasma samples collected from patients after the administration of activated vitamin D3 caused significantly increased ALP activity in SMC compared to the samples drawn prior to activated vitamin D3 and here, again induction of ferritin diminished the osteoblastic transformation. Our data suggests that pharmacological induction of ferritin prevents osteoblastic transformation of SMC. Hence, utilization of such agents that will cause enhanced ferritin synthesis may have important clinical applications in prevention of vascular calcification.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
ferritin
ferroxidase activity
[béta]-glycerophosphate
vascular calcification
vitamin D3
Megjelenés:Journal Of Cellular And Molecular Medicine. - 20 : 2 (2016), p. 217-230. -
További szerzők:Zarjou, Abolfazl (1979-) (kutató orvos) Agarwal, Anupam Sikura Katalin Éva (1985-) (biológus) Becs Ádám Nyitrai Mónika Balogh Enikő (1987-) (molekuláris biológus) Bányai Emese (1984-) (orvos) Eaton, John W. Arosio, Paolo Poli, Maura Jeney Viktória (1971-) (vegyész, kémia tanár) Balla József (1959-) (belgyógyász, nephrológus) Balla György (1953-) (csecsemő és gyermekgyógyász, neonatológus)
Pályázati támogatás:TÁMOP-4.2.2.A-11/1/KONV-2012-0045
TÁMOP
Belgyógyászat Kutatócsoport
K-112333(B.J.)
OTKA
MTA-DE
MTA
Vascularis Biológia, Thrombosis-Haemostasis Kutatócsoport
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12.

001-es BibID:BIBFORM047602
035-os BibID:ID: 703571
Első szerző:Jeney Viktória (vegyész, kémia tanár)
Cím:Natural history of the bruise : formation, elimination, and biological effects of oxidized hemoglobin / Viktória Jeney, John W. Eaton, György Balla, József Balla
Dátum:2013
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Oxidative Medicine and Cellular Longevity. - 2013 (2013), p. [1-9]. -
További szerzők:Eaton, John W. Balla György (1953-) (csecsemő és gyermekgyógyász, neonatológus) Balla József (1959-) (belgyógyász, nephrológus)
Pályázati támogatás:TÁMOP-4.2.2/B-10/1-2010-0024
TÁMOP
TÁMOP-4.2.2.A-11/1/KONV-2012-0045
TÁMOP
Belgyógyászat Kutatócsoport
OTKA-K75883
OTKA
MTA-DE
MTA-DE Vascularis Biológia, Thrombosis- Haemostasis Kutatócsoport 11003
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