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1.

001-es BibID:BIBFORM063538
Első szerző:Birukov, Konstantin G.
Cím:Molecular and biochemical characterization of alternatively spliced variants of human endothelial cell MLCK / K. G. Birukov, Cs. Csortos, S. Dudek, V. Lazar, A. D. Verin, J. G. N. Garcia
Dátum:1999
ISSN:1073-449X
Tárgyszavak:Orvostudományok Elméleti orvostudományok idézhető absztrakt
Megjelenés:American Journal of Respiratory and Critical Care Medicine 159 : 3 (1999), p. 1. -
További szerzők:Csortos Csilla (1956-) (biokémikus) Dudek, Steven Lázár Viktória (1981-) (molekuláris biológus) Verin, Alexander Garcia, Joe G. N.
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2.

001-es BibID:BIBFORM047043
035-os BibID:PMID:11113114
Első szerző:Birukov, Konstantin G.
Cím:Differential regulation of alternatively spliced endothelial cell myosin light chain kinase isoforms by p60(Src) / Konstantin G. Birukov, Csilla Csortos, Lisa Marzilli, Steven Dudek, Shwu-Fan Ma, Anne R. Bresnick, Alexander D. Verin, Robert J. Cotter, Joe G. N. Garcia
Dátum:2001
ISSN:0021-9258 1083-351X
Megjegyzések:The Ca(2+)/calmodulin-dependent endothelial cell myosin light chain kinase (MLCK) triggers actomyosin contraction essential for vascular barrier regulation and leukocyte diapedesis. Two high molecular weight MLCK splice variants, EC MLCK-1 and EC MLCK-2 (210-214 kDa), in human endothelium are identical except for a deleted single exon in MLCK-2 encoding a 69-amino acid stretch (amino acids 436-505) that contains potentially important consensus sites for phosphorylation by p60(Src) kinase (Lazar, V., and Garcia, J. G. (1999) Genomics 57, 256-267). We have now found that both recombinant EC MLCK splice variants exhibit comparable enzymatic activities but a 2-fold reduction of V(max), and a 2-fold increase in K(0.5 CaM) when compared with the SM MLCK isoform, whereas K(m) was similar in the three isoforms. However, only EC MLCK-1 is readily phosphorylated by purified p60(Src) in vitro, resulting in a 2- to 3-fold increase in EC MLCK-1 enzymatic activity (compared with EC MLCK-2 and SM MLCK). This increased activity of phospho-MLCK-1 was observed over a broad range of submaximal [Ca(2+)] levels with comparable EC(50) [Ca(2+)] for both phosphorylated and unphosphorylated EC MLCK-1. The sites of tyrosine phosphorylation catalyzed by p60(Src) are Tyr(464) and Tyr(471) within the 69-residue stretch deleted in the MLCK-2 splice variant. These results demonstrate for the first time that p60(Src)-mediated tyrosine phosphorylation represents an important mechanism for splice variant-specific regulation of nonmuscle MLCK and vascular cell function.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Journal of Biological Chemistry. - 276 : 11 (2001), p. 8567-8573. -
További szerzők:Csortos Csilla (1956-) (biokémikus) Marzilli, Lisa Dudek, Steven Ma, Shwu-Fan Bresnick, Anne R. Verin, Alexander Cotter, Robert J. Garcia, Joe G. N.
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3.

001-es BibID:BIBFORM074172
Első szerző:Csortos Csilla (biokémikus)
Cím:TIMAP is a positive regulator of pulmonary endothelial barrier function / Csilla Csortos, Istvan Czikora, Natalia V. Bogatcheva, Djanybek M. Adyshev, Christophe Poirier, Gabor Olah, Alexander D. Verin
Dátum:2008
ISSN:1040-0605 1522-1504
Megjegyzések:TGF-?-inhibited membrane-associated protein, TIMAP, is expressed at high levels in endothelial cells (EC). It is regarded as a member of the MYPT (myosin phosphatase target subunit) family of protein phosphatase 1 (PP1) regulatory subunits; however, its function in EC is not clear. In our pull-down experiments, recombinant TIMAP binds preferentially the ?-isoform of the catalytic subunit of PP1 (PP1c?) from pulmonary artery EC. As PP1c?, but not PP1c?, binds with MYPT1 into functional complex, these results suggest that TIMAP is a novel regulatory subunit of myosin phosphatase in EC. TIMAP depletion by small interfering RNA (siRNA) technique attenuates increases in transendothelial electrical resistance induced by EC barrier-protective agents (sphingosine-1-phosphate, ATP) and enhances the effect of barrier-compromising agents (thrombin, nocodazole) demonstrating a barrier-protective role of TIMAP in EC. Immunofluorescent staining revealed colocalization of TIMAP with membrane/cytoskeletal protein, moesin. Moreover, TIMAP coimmunoprecipitates with moesin suggesting the involvement of TIMAP/moesin interaction in TIMAP-mediated EC barrier enhancement. Activation of cAMP/PKA cascade by forskolin, which has a barrier-protective effect against thrombin-induced EC permeability, attenuates thrombin-induced phosphorylation of moesin at the cell periphery of control siRNA-treated EC. On the contrary, in TIMAP-depleted EC, forskolin failed to affect the level of moesin phosphorylation at the cell edges. These results suggest the involvement of TIMAP in PKA-mediated moesin dephosphorylation and the importance of this dephosphorylation in TIMAP-mediated EC barrier protection.protein phosphorylation and dephosphorylation are known to be the key signaling events affecting the status of vascular endothelial barrier (11). Cytoskeletal and intercellular junctional proteins are regulated via reversible phosphorylation of serine (Ser), threonine (Thr), or tyrosine (Tyr) side chains. Based on many recent data, it is apparent that several types of protein phosphatases are intimately involved in the regulation of endothelial barrier function (10, 17, 27?29). However, their regulation is not yet completely understood.Protein phosphatase 1 (PP1) is a multimeric phosphoserine/phosphothreonine-specific phosphatase. One of the four different isoforms, ?, ?, ?1, or ?2, of the catalytic subunit (PP1c) binds to one (or two) protein from a pool of regulatory subunits (R). The holoenzyme forms possess diverse cellular functions. A common structural element of R proteins is a short, conserved PP1c binding motif, (R/K)VXF (3, 9, 10). Different R subunits may direct PP1 holoenzymes to distinct subcellular locations and increase or suppress the activity toward specific substrates (3, 9). Myosin light chain phosphatase (or myosin phosphatase, MP), for example, is composed of PP1c? and two regulatory subunits, namely, a larger targeting/regulatory subunit (myosin phosphatase target subunit, MYPT) and a small regulatory subunit (M20) (2, 10, 14). The activity of MP holoenzyme is increased toward phosphorylated myosin compared with the activity of the PP1c monomer (15).It was recently shown that MP function is not limited to myosin dephosphorylation. The MP regulatory subunit MYPT1 can directly bind to F-actin binding proteins including ERM proteins (ezrin-radixin-moesin family). These proteins could be phosphorylated by either protein kinase C? or Rho kinase (12, 20); phosphorylation renders unfolded ERM protein, enabling its interaction with actin and membrane proteins (20, 21). ERM dephosphorylation by MP seems to affect ERM conformation and cytoskeletal/membrane binding capacities (12, 20). These data indicate that MP not only dephosphorylates myosin, but it is also involved in the regulation of F-actin cytoskeleton.Recently, other proteins of the MYPT family, namely MYPT3, TIMAP (TGF-?-inhibited membrane-associated protein), and myosin binding subunit 85 (MBS85), were identified and characterized from different sources (8, 25, 26). They share some structural features with MYPT1, e.g., all of these proteins contain the PP1c binding motif followed by ankyrin repeats. On the other hand, MYPT3, TIMAP, and MBS85 have their own special features as well. For example, both TIMAP and MYPT3 have COOH-terminal prenylation motif suggesting possible membrane association. The high level of homology with MYPT1 implies that TIMAP, MYPT3, and MBS85 may be regulatory subunits of PP1; however, their physiological significance is not known.TIMAP is a 64-kDa protein expressed at high levels in endothelial cells (EC). As TIMAP mRNA synthesis is strongly downregulated by TGF-?1 (8), it is likely to assume that TIMAP may be an important component of endothelial response to TGF-?1, including apoptosis, capillary morphogenesis, and barrier dysfunction. It is highly homologous to MYPT3 (?45% amino acid homology) and shares its structural features, i.e., PP1c binding motif, ankyrin repeats, prenylation motif, and possible nuclear localization signals (8). Yeast and bacterial two-hybrid screening revealed several potential protein partners for TIMAP (1, 16). For instance, TIMAP interacts with the 37/67-kDa laminin receptor (LAMR1). It was suggested that TIMAP targets PP1c to LAMR1, and LAMR1 is a TIMAP-dependent PP1c substrate (16). Although protein-protein interaction between TIMAP and PP1c was shown by immunoprecipitation, its role in regulating PP1c activity is not clarified yet. In the present work, we present evidence for specific interaction between TIMAP and PP1c?. Furthermore, we show that TIMAP has a barrier-protective role in human pulmonary artery endothelial cells (HPAEC), and we propose that ERM proteins are among its targets.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
transendothelial electrical resistance
small interfering RNA
moesin interaction with protein phosphatase 1
Megjelenés:American Journal Of Physiology-Lung Cellular And Molecular Physiology. - 295 : 3 (2008), p. L440-L450. -
További szerzők:Czikora István (1979-) (vegyész, biokémikus) Bogatcheva, Natalia V. Adyshev, Djanybek M. Poirier, Christophe Oláh Gábor Verin, Alexander
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4.

001-es BibID:BIBFORM063539
Első szerző:Csortos Csilla (biokémikus)
Cím:Molecular and biochemical characterization of protein phosphatase 1 (PP1) in endothelium / Cs. Csortos, A. D. Verin, S. D. Durbin, C. E. Patterson, J. G. N. Garcia
Dátum:1998
ISSN:1073-449X
Tárgyszavak:Orvostudományok Elméleti orvostudományok idézhető absztrakt
Megjelenés:American Journal of Respiratory and Critical Care Medicine 157 : 3 (1998), p. 1. -
További szerzők:Verin, Alexander Durbin, Steve D. Patterson, Carolyn E. Garcia, Joe G. N.
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5.

001-es BibID:BIBFORM001291
Első szerző:Csortos Csilla (biokémikus)
Cím:Regulation of vascular endothelial cell barrier function and cytoskeleton structure by protein phosphatases of the PPP family / Csortos Cs., Kolosova I., Verin A. D.
Dátum:2007
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
endothelial barrier function
Ser/Thr protein phosphatases
Megjelenés:American Journal of Physiology-Lung Cellular and Molecular Phsiology. - 293 (2007), p. L843-L854. -
További szerzők:Kolosova, Irina Verin, Alexander
Internet cím:elektronikus változat
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6.

001-es BibID:BIBFORM016824
Első szerző:Czikora István (vegyész, biokémikus)
Cím:Characterization of the effect of TIMAP phosphorylation on its interaction with protein phosphatase 1 / Czikora István, Kim Kyung-mi, Kása Anita, Bécsi Bálint, Verin Alexander D., Gergely Pál, Erdődi Ferenc, Csortos Csilla
Dátum:2011
ISSN:0300-9084
Megjegyzések:TIMAP, TGF-beta inhibited, membrane-associated protein, is highly abundant in endothelial cells (EC). We have shown earlier the involvement of TIMAP in PKA-mediated ERM (ezrin-radixin-moesin) dephosphorylation as part of EC barrier protection by TIMAP (Csortos et al., 2008). Emerging data demonstrate the regulatory role of TIMAP on protein phosphatase 1 (PP1) activity. We provide here evidence for specific interaction (Ka = 1.80 x 106 M-1) between non-phosphorylated TIMAP and the catalytic subunit of PP1 (PP1c) by surface plasmon resonance based binding studies. Thiophosphorylation of TIMAP by PKA, or sequential thiophosphorylation by PKA and GSK3β slightly modifies the association constant for the interaction of TIMAP with PP1c and decreases the rate of dissociation. However, dephosphorylation of phospho-moesin substrate by PP1cbeta is inhibited to different extent in the presence of non- (not, vert, similar60% inhibition), mono- (not, vert, similar50% inhibition) or double-thiophosphorylated (<10% inhibition) form of TIMAP. Our data suggest that double-thiophosphorylation of TIMAP has minor effect on its binding ability to PP1c, but considerably attenuates its inhibitory effect on the activity of PP1c. PKA activation by forskolin treatment of EC prevented thrombin evoked barrier dysfunction and ERM phosphorylation at the cell membrane (Csortos et al., 2008). With the employment of specific GSK3beta inhibitor it is shown here that PKA activation is followed by GSK3beta activation in bovine pulmonary EC and both of these activations are required for the rescuing effect of forskolin in thrombin treated EC. Our results suggest that the forskolin induced PKA/GSK3beta activation protects the EC barrier via TIMAP-mediated decreasing of the ERM phosphorylation level.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
TIMAP
Protein Phosphatase 1
Moesin
Surface Plasmon Resonance
Molekuláris Medicina
Megjelenés:Biochimie. - 93 : 7 (2011), p. 1139-1145. -
További szerzők:Kim, Kyung-mi Kovács-Kása Anita (1983-) Bécsi Bálint (1981-) (vegyészmérnök) Verin, Alexander Gergely Pál (1947-) (biokémikus) Erdődi Ferenc (1953-) (biokémikus) Csortos Csilla (1956-) (biokémikus)
Pályázati támogatás:TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
I. Protein foszfatázok szerepe az in vitro porcdifferenciációban és a mechano-transzdukcióban, II. Hypoglykaemiás szerek tervezése a glikogén foszforilázra (foszforilációval és defoszforilációval szabályozott kulcsenzim) ható molekulákkal
TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
Biomolekuláris interakciók jellemzőinek kvantitatív meghatározása
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7.

001-es BibID:BIBFORM047050
035-os BibID:PMID:7942275
Első szerző:DePaoli-Roach, Anna A.
Cím:Serine/threonine protein phosphatases in the control of cell function / Anna A. DePaoli-Roach, In-Kyung Park, Vaclav Cerovsky, Csilla Csortos, Stephen D. Durbin, Martha J. Kuntz, Albert Sitikov, Pauline M. Tang, Alexander Verin, Stanislaw Zolnierowicz
Dátum:1994
Megjegyzések:Reversible protein phosphorylation is a fundamental mechanism by which many biological functions are regulated. Achievement of such control requires the coordinated action of the interconverting enzymes, the protein kinases and protein phosphatases. By comparison with protein kinases, a limited number of protein phosphatase catalytic subunits are present in the cell, which raises the question of how such a small number of dephosphorylating enzymes can counterbalance the action of the more numerous protein kinases. In mammalian cells, four major classes of Ser/Thr-specific phosphatase catalytic subunits have been identified, comprising two distinct gene families. The high degree of homology among members of the same family, PP1, PP2A and PP2B, and the high degree of evolutionary conservation between organisms as divergent as mammals and yeast, implies that these enzymes are involved in fundamental cell functions. Type 1 enzymes appear to acquire specificity by association with targeting regulatory subunits which direct the enzymes to specific cellular compartments, confer substrate specificity and control enzyme activity. In spite of the progress made in determining the structure of the PP2A subunits, very little is known about the control of this activity and about substrate selection. Recent studies have unravelled a significant number of regulatory subunits. The potential existence of five distinct B or B-related polypeptides, some of which are present in multiple isoforms, two A and two C subunit isoforms, raises the possibility that a combinatorial association could generate a large number of specific PP2A forms with different substrate specificity and/or cellular localization. Moreover, biochemical, biological and genetic studies all concur in suggesting that the regulatory subunits may play an important role in determining the properties of the Ser/Thr protein phosphatases and hence their physiological functions.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Advances in Enzyme Regulation. - 34 (1994), p. 199-224. -
További szerzők:Park, In-Kyung Cerovsky, Vaclav Csortos Csilla (1956-) (biokémikus) Durbin, Steve D. Kuntz, Martha J. Sitikov, Albert Tang, Pauline M. Verin, Alexander Zolnierowicz, Stanislaw
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8.

001-es BibID:BIBFORM047045
035-os BibID:PMID:10362724
Első szerző:Garcia, Joe G. N.
Cím:Regulation of endothelial cell myosin light chain kinase by Rho, cortactin, and p60(src) / Joe G. N. Garcia, Alexander D. Verin, Kane Schaphorst, Rafat Siddiqui, Carolyn E. Patterson, Csilla Csortos, Viswanathan Natarajan
Dátum:1999
ISSN:1040-0605
Megjegyzések:Inflammatory diseases of the lung are characterized by increases in vascular permeability and enhanced leukocyte infiltration, reflecting compromise of the endothelial cell (EC) barrier. We examined potential molecular mechanisms that underlie these alterations and assessed the effects of diperoxovanadate (DPV), a potent tyrosine kinase activator and phosphatase inhibitor, on EC contractile events. Confocal immunofluorescent microscopy confirmed dramatic increases in stress-fiber formation and colocalization of EC myosin light chain (MLC) kinase (MLCK) with the actin cytoskeleton, findings consistent with activation of the endothelial contractile apparatus. DPV produced significant time-dependent increases in MLC phosphorylation that were significantly attenuated but not abolished by EC MLCK inhibition with KT-5926. Pretreatment with the Rho GTPase-inhibitory C3 exotoxin completely abolished DPV-induced MLC phosphorylation, consistent with Rho-mediated MLC phosphatase inhibition and novel regulation of EC MLCK activity. Immunoprecipitation of EC MLCK after DPV challenge revealed dramatic time-dependent tyrosine phosphorylation of the kinase in association with increased MLCK activity and a stable association of MLCK with the p85 actin-binding protein cortactin and p60(src). Translocation of immunoreactive cortactin from the cytosol to the cytoskeleton was noted after DPV in concert with cortactin tyrosine phosphorylation. These studies indicate that DPV activates the endothelial contractile apparatus in a Rho GTPase-dependent fashion and suggests that p60(src)-induced tyrosine phosphorylation of MLCK and cortactin may be important features of contractile complex assembly.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:American Journal of Physiology. Lung Cellular and Molecular Physiology. - 276 : 6 Pt 1 (1999), p. L989-L998. -
További szerzők:Verin, Alexander Schaphorst, Kane Siddiqui, Rafat Patterson, Carolyn E. Csortos Csilla (1956-) (biokémikus) Natarajan, Viswanathan
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9.

001-es BibID:BIBFORM046501
035-os BibID:PMID:23583905
Első szerző:Kim, Kyung-mi
Cím:Putative protein partners for the human CPI-17 protein revealed by bacterial two-hybrid screening / Kyung-mi Kim, Djanybek M. Adyshev, Anita Kása, Evgeny A. Zemskov, Irina A. Kolosova, Csilla Csortos, Alexander D. Verin
Dátum:2013
ISSN:0026-2862
Megjegyzések:We have previously demonstrated that PKC-potentiated inhibitory protein of protein phosphatase-1 (CPI-17) is expressed in lung endothelium. CPI-17, a specific inhibitor of myosin light chain phosphatase (MLCP), is involved in the endothelial cytoskeletal and barrier regulation. In this paper, we report the identification of fourteen putative CPI-17 interacting proteins in the lung using BacterioMatch Two-Hybrid System. Five of them: plectin 1 isoform 1, alpha II spectrin, OK/SW-CL.16, gelsolin isoform a, and junction plakoglobin are involved in actin cytoskeleton organization and cell adhesion, suggesting possible significance of these binding partners in CPI-17-mediated cytoskeletal reorganization of endothelial cells. Furthermore, we confirmed the specific interaction between plakoglobin and CPI-17, which is affected by the phosphorylation status of CPI-17 in human lung microvascular endothelial cells.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Microvascular Research. - 88 (2013), p. 19-24. -
További szerzők:Adyshev, Djanybek M. Kovács-Kása Anita (1983-) Zemskov, Evgeny A. Kolosova, Irina Csortos Csilla (1956-) (biokémikus) Verin, Alexander
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10.

001-es BibID:BIBFORM029024
Első szerző:Kim, Kyung-mi
Cím:Molecular characterization of myosin phosphatase in endothelium / Kyung-mi Kim, Csilla Csortos, Istvan Czikora, David Fulton, Nagavedi S. Umapathy, Gabor Olah, Alexander D. Verin
Dátum:2012
ISSN:0021-9541
Megjegyzések:The phosphorylation status of myosin light chain (MLC) is regulated by both MLC kinases and type 1 Ser/Thr phosphatase (PPase 1), MLC phosphatase (MLCP) activities. The activity of the catalytic subunit of MLCP (CS1β) towards myosin depends on its associated regulatory subunit, namely myosin PPase targeting subunit 1 (MYPT1). Our previously published data strongly suggested the involvement of MLCP in endothelial cell (EC) barrier regulation. In this study, our new data demonstrate that inhibition of MLCP by either CS1β or MYPT1 siRNA-based depletion results in significant attenuation of purine nucleotide (ATP and adenosine)-induced EC barrier enhancement. Consistent with the data, thrombin-induced EC F-actin stress fiber formation and permeability increase were attenuated by the ectopic expression of constitutively active (C/A) MYPT1. The data demonstrated for the first time direct involvement of MLCP in EC barrier enhancement/protection. Cloning of MYPT1 in human pulmonary artery EC (HPAEC) revealed the presence of two MYPT1 isoforms, long and variant 2 (V2) lacking 56 amino acids from 553 to 609 of human MYPT1 long, which were previously identified in HeLa and HEK 293 cells. Our data demonstrated that in Cos-7 cells ectopically expressed EC MYPT1 isoforms co-immunoprecipitated with intact CS1β suggesting the importance of PPase 1 activity for the formation of functional complex of MYPT1/CS1β. Interestingly, MYPT1 V2 shows decreased binding affinity compared to MYPT1 long for radixin (novel MLCP substrate and a member of ERM family proteins). These results suggest functional difference between EC MYPT1 isoforms in the regulation of MLCP activity and cytoskeleton. J. Cell. Physiol. 227: 1701-1708, 2012. © 2011 Wiley Periodicals, Inc.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
egyetemen (Magyarországon) készült közlemény
Megjelenés:Journal of Cellular Physiology. - 227 : 4 (2012), p. 1701-1708. -
További szerzők:Fulton, David Umapathy, Nagavedi S. Oláh Gábor Verin, Alexander Csortos Csilla (1956-) (biokémikus) Czikora István (1979-) (vegyész, biokémikus)
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11.

001-es BibID:BIBFORM063543
Első szerző:Kim K
Cím:Molecular characterization of myosin phosphatase in endothelium / Kim K., Csortos C., Verin A. D.
Dátum:2010
ISSN:1073-449X
Tárgyszavak:Orvostudományok Elméleti orvostudományok idézhető absztrakt
Megjelenés:American Journal Of Respiratory And Critical Care Medicine. - 181 (2010), p. A3437. -
További szerzők:Csortos Csilla (1956-) (biokémikus) Verin, Alexander
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12.

001-es BibID:BIBFORM057790
Első szerző:Kovács-Kása Anita
Cím:Cytoskeletal mechanisms regulating vascular endothelial barrier function in response to acute lung injury / Anita Kása, Csilla Csortos, Alexander D. Verin
Dátum:2015
ISSN:2168-8370
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
acute lung injury
barrier function
cytoskeleton
endothelial junctions
thrombin
pulmonary endothelium
Megjelenés:Tissue Barriers. - 3 : 1-2 (2015), p. e974448-1-e974448-11. -
További szerzők:Csortos Csilla (1956-) (biokémikus) Verin, Alexander
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