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1.

001-es BibID:BIBFORM001016
Első szerző:Altafaj, Xavier
Cím:Maurocalcine interacts with the cardiac ryanodine receptor without inducing channel modification / Altafaj X., France J., Almássy J., Jóna I., Rossi D., Sorrentino V., Mabrouk K., De Waard M., Ronjat M.
Dátum:2007
Megjegyzések:We have previously shown that MCa (maurocalcine), a toxin from the venom of the scorpion Maurus palmatus, binds to RyR1 (type 1 ryanodine receptor) and induces strong modifications of its gating behaviour. In the present study, we investigated the ability of MCa to bind to and modify the gating process of cardiac RyR2. By performing pull-down experiments we show that MCa interacts directly with RyR2with an apparent affinity of 150 nM. By expressing different domains of RyR2 in vitro, we show that MCa binds to two domains of RyR2, which are homologous with those previously identified on RyR1. The effect of MCa binding to RyR2 was then evaluated by three different approaches: (i) [H-3]ryanodine binding experiments, showing a very weak effect of MCa (up to 1 mu M), (ii) Ca2+ release measurements from cardiac sarcoplasmic reticulum vesicles, showing that MCa up to 1 mu M is unable to induce Ca2+ release, and (iii) single-channel recordings, showing that MCa has no effect on the open probability or on the RyR2 channel conductance level. Long-lasting opening events of RyR2 were observed in the presence of MCa only when the ionic current direction was opposite to the physiological direction, i.e. from the cytoplasmic face of RyR2 to its luminal face. Therefore, despite the conserved MCa binding ability of RyR1 and RyR2, functional studies show that, in contrast with what is observed with RyR1, MCa does not affect the gating properties of RyR2. These results highlight a different role of the MCa-binding domains in the gating process of RyR1 and RyR2.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Biochemical Journal 406 (2007), p. 309-315. -
További szerzők:France, Julien Almássy János (1981-) (élettanász, biológus, angol-magyar szakfordító) Jóna István (1948-) (élettanász, fizikus) Rossi, Daniela Sorrentino, Vincenzo Mabrouk, Kamel De Waard, Michel Ronjat, Michel
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DOI
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2.

001-es BibID:BIBFORM059607
Első szerző:Bai Péter (biokémikus)
Cím:New route for the activation of poly(ADP-ribose) polymerase-1 : a passage that links poly(ADP-ribose) polymerase-1 to lipotoxicity? / Péter Bai, Balázs Csóka
Dátum:2015
ISSN:0264-6021
Megjegyzések:In this issue of Biochemical Journal, Chen and colleagues characterize an interaction between ACBD3 (acyl-CoA-binding domain-containing 3) protein and PARP [poly(ADP-ribose) polymerase]-1 through the activation of ERKs (extracellular-signal-regulated kinases). This study envisages a pathway through which ABCD3 translates enhanced fatty acid levels to ERK and consequently PARP-1 activation. The consequences of PARP-1 activation lead to cellular and tissue damage, implying that the ACBD3/PARP-1 pathway is an important pathway in lipotoxicity events.
Tárgyszavak:Orvostudományok Elméleti orvostudományok hozzászólás
ACBD3
cholesterol
ERK
fatty acid
lipotoxicity
PARP
Megjelenés:Biochemical Journal. - 469 : 2 (2015), p. 9-11. -
További szerzők:Csóka Balázs (1975-) (biokémikus)
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3.

001-es BibID:BIBFORM062128
Első szerző:Biri Beáta (Budapest)
Cím:Metastasis-associated S100A4 is a specific amine donor and an activity-independent binding partner of transglutaminase-2 / Beáta Biri, Bence Kiss, Róbert Király, Gitta Schlosser, Orsolya Láng, László Kőhidai, László Fésüs, László Nyitray
Dátum:2016
ISSN:0264-6021
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Biochemical Journal 473 : 1 (2016), p. 31-42. -
További szerzők:Kiss Bence Király Róbert (1975-) (biológus) Schlosser Gitta Láng Orsolya Kőhidai László Fésüs László (1947-) (orvos biokémikus) Nyitray László
Pályázati támogatás:TÁMOP 4.2.4. A/2-11-1-2012-0001
TÁMOP
OTKA K108437
OTKA
OTKA NK105046
OTKA
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4.

001-es BibID:BIBFORM063693
Első szerző:Blaszczyk, Katarzyna
Cím:STAT2/IRF9 directs a prolonged ISGF3-like transcriptional response and antiviral activity in the absence of STAT1 / Katarzyna Blaszczyk, Adam Olejnik, Hanna Nowicka, Lilla Ozgyin, Yi-Ling Chen, Stefan Chmielewski, Kaja Kostyrko, Joanna Wesoly, Balint Laszlo Balint, Chien-Kuo Lee, Hans A. R. Bluyssen
Dátum:2015
ISSN:0264-6021
Megjegyzések:Evidence is accumulating for the existence of a signal transducer and activator of transcription 2 (STAT2)/interferon regulatory factor 9 (IRF9)-dependent, STAT1-independent interferon alpha (IFN?) signalling pathway. However, no detailed insight exists into the genome-wide transcriptional regulation and the biological implications of STAT2/IRF9-dependent IFN? signalling as compared with interferon-stimulated gene factor 3 (ISGF3). In STAT1-defeicient U3C cells stably overexpressing human STAT2 (hST2-U3C) and STAT1-deficient murine embryonic fibroblast cells stably overexpressing mouse STAT2 (mST2-MS1KO) we observed that the IFN?-induced expression of 2'-5'-oligoadenylate synthase 2 (OAS2) and interferon-induced protein with tetratricopeptide repeats 1 (Ifit1) correlated with the kinetics of STAT2 phosphorylation, and the presence of a STAT2/IRF9 complex requiring STAT2 phosphorylation and the STAT2 transactivation domain. Subsequent microarray analysis of IFN?-treated wild-type (WT) and STAT1 KO cells overexpressing STAT2 extended our observations and identified ?120 known antiviral ISRE-containing interferon-stimulated genes (ISGs) commonly up-regulated by STAT2/IRF9 and ISGF3. The STAT2/IRF9-directed expression profile of these IFN-stimulated genes (ISGs) was prolonged as compared with the early and transient response mediated by ISGF3. In addition, we identified a group of 'STAT2/IRF9-specific' ISGs, whose response to IFN? was ISGF3-independent. Finally, STAT2/IRF9 was able to trigger an antiviral response upon encephalomyocarditis virus (EMCV) and vesicular stomatitis Indiana virus (VSV). Our results further prove that IFN?-activated STAT2/IRF9 induces a prolonged ISGF3-like transcriptome and generates an antiviral response in the absence of STAT1. Moreover, the existence of 'STAT2/IRF9-specific' target genes predicts a novel role of STAT2 in IFN? signalling.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Biochemical Journal. - 466 : 3 (2015), p. 511-524. -
További szerzők:Olejnik, Adam Nowicka, Hanna Ozgyin Lilla (1989-) (molekuláris biológus) Chen, Yi-Ling Chmielewski, Stefan Kostyrko, Kaja Wesoly, Joanna Bálint Bálint László (1971-) (kutató orvos) Lee, Chien-Kuo Bluyssen, Hans A. R.
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5.

001-es BibID:BIBFORM065146
Első szerző:Ergülen, Elvan
Cím:Identification of DNAJA1 as a novel interacting partner and substrate of human transglutaminase 2 / Elvan Ergülen, Bálint Bécsi, István Csomós, László Fésüs, Kajal Kanchan
Dátum:2016
ISSN:0264-6021
Megjegyzések:Transglutaminase 2 (TG2) is a ubiquitously expressed multi-functional member of the transglutaminase enzyme family. It has been implicated to have roles in many physiological and pathological processes such as differentiation, apoptosis, signal transduction, adhesion and migration, wound healing and inflammation. Previous studies revealed that TG2 has various intra- and extracellular interacting partners, which contribute to these processes. In this study, we identified a molecular co-chaperone, DNAJA1 as novel interacting partner of human TG2 using a GST pull down assay and subsequent mass spectrometry analysis and further confirmed this interaction via ELISA and SPR measurements. Interaction studies were also performed with domain variants of TG2 and results suggest that the catalytic core domain of TG2 is essential for the TG2-DNAJA1 interaction. Crosslinking activity was not essential for the interaction since DNAJA1 was also found to interact with the catalytically inactive form of TG2. Further, we have showed that DNAJA1 interacts with the open form of TG2 and regulates its transamidation activity both in vitro and in situ conditions. We also found that DNAJA1 is a glutamine donor substrate of TG2. Since DNAJA1 and TG2 are reported to regulate common pathological conditions such as neurodegenerative disorders and cancer, the findings in this paper open up possibilities to explore molecular mechanisms behind TG2 regulated functions.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Transglutaminase 2
transamidation
DNAJA1/HSP40
core domain
protein-protein interaction
in situ crosslinking activity
GST pull down assay
surface plasmon resonance
Megjelenés:Biochemical Journal. - 473 : 21 (2016), p. 3889-3901. -
További szerzők:Bécsi Bálint (1981-) (vegyészmérnök) Csomós István (1983-) (molekuláris biológus) Fésüs László (1947-) (orvos biokémikus) Kanchan, Kajal
Pályázati támogatás:NK 105046
OTKA
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6.

001-es BibID:BIBFORM020318
Első szerző:Jakab Balázs (Pécs)
Cím:Distribution of PACAP-38 in the central nervous system of various species determined by a novel radioimmunoassay / Balázs Jakab, Dóra Reglődi, Rita Józsa, Tibor Hollósy, Andrea Tamás, Andrea Lubics, István Lengvári, Gábor Oroszi, Zoltán Szilvássy, János Szolcsányi, József Németh
Dátum:2004
Megjegyzések:AbstractPituitary adenylate cyclase activating polypeptide (PACAP) occurs in two molecular forms: PACAP-38 and PACAP-27. Soon after the isolation and chemical characterization of PACAP, the first radioimmunoassay (RIA) methods have been developed, but it is a still rarely used laboratory technique in the field of PACAP research. The aim of the present study was to develop a novel, highly specific PACAP-38 assay to investigate the quantitative distribution of PACAP-38 in the central nervous system of various vertebrate species under the same technical and experimental conditions. Different areas of the brain and the spinal cord were removed from rats, chickens and fishes and the tissue samples were processed for PACAP-38 RIA. Our results indicate that the antiserum used in the RIA is C-terminal specific, without affinity for other members of the vasoactive intestinal polypeptide (VIP)/secretin/glucagon peptide family. The average ID50 value was 48.6+/-3.4 fmol/ml determined in 10 consecutive assays. Detection limit for PACAP-38 proved to be 2 fmol/ml. PACAP-38 immunoreactivity was present in the examined brain areas of each species studied, with highest concentration in the rat diencephalons. High levels of PACAP-38 were also detected in the rat telencephalon, followed by spinal cord and brainstem. The central nervous system of the fish also contained considerable concentrations of PACAP-38, whereas lowest concentrations were measured in the central nervous system of the chicken.
Tárgyszavak:Orvostudományok Gyógyszerészeti tudományok idegen nyelvű folyóiratközlemény külföldi lapban
PACAP-38
central nervous system
radioimmunoassay
Megjelenés:Journal of Biochemical and Biophysical Methods. - 61 : 1-2 (2004), p. 189-198. -
További szerzők:Reglődi Dóra (Idegtudományok) Józsa Rita (Pécs) Hollósy Tibor (Pécs) Tamás Andrea (Idegtudomány) (Pécs) Lubics Andrea (Pécs) Lengvári István Oroszi Gábor (Pécs) Szolcsányi János (Pécs) Németh József (Pécs) Szilvássy Zoltán (1957-) (belgyógyász, farmakológus, klinikai farmakológus)
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7.

001-es BibID:BIBFORM003920
Első szerző:Kádas János (molekuláris biológus, biokémikus, kertészmérnök)
Cím:C-terminal residues of mature human T-lymphotropic virus type 1 protease are critical for dimerization and catalytic activity / Kádas, J., Boross, P., Weber, I. T., Bagossi, P., Matúz, K., Tőzsér, J.
Dátum:2008
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:The Biochemical Journal 416 : 3 (2008), p. 357-364. -
További szerzők:Boross Péter (1972-) (biokémikus, vegyész) Weber, Irene T. Bagossi Péter (1966-2011) (biokémikus, vegyész) Matúz Krisztina (1980-) (vegyész, biokémikus) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész)
Internet cím:elektronikus változat
DOI
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8.

001-es BibID:BIBFORM049593
035-os BibID:PMID:23941696
Első szerző:Kanchan, Kajal
Cím:Identification of a specific one amino acid change in recombinant human transglutaminase 2 that regulates its activity and calcium sensitivity / Kajal Kanchan, Elvan Ergülen, Robert Király, Zsófia Simon-Vecsei, Mónika Fuxreiter, László Fésüs
Dátum:2013
ISSN:0264-6021
Megjegyzések:TG2 (transglutaminase 2) is a calcium-dependent protein cross-linking enzyme which is involved in a variety of cellular processes. The threshold level of calcium needed for endogenous and recombinant TG2 activity has been controversial, the former being more sensitive to calcium than the latter. In the present study we address this question by identifying a single amino acid change from conserved valine to glycine at position 224 in recombinant TG2 compared with the endogenous sequence present in the available genomic databases. Substituting a valine residue for Gly224 in the recombinant TG2 increased its calcium-binding affinity and transamidation activity 10-fold and isopeptidase activity severalfold, explaining the inactivity of widely used recombinant TG2 at physiological calcium concentrations. ITC (isothermal titration calorimetry) measurements showed 7-fold higher calcium-binding affinities for TG2 valine residues which could be activated inside cells. The two forms had comparable substrate- and GTP-binding affinities and also bound fibronectin similarly, but coeliac antibodies had a higher affinity for TG2 valine residues. Structural analysis indicated a higher stability for TG2 valine residues and a decrease in flexibility of the calcium-binding loop resulting in improved metal-binding affinity. The results of the present study suggest that Val224 increases TG2 activity by modulating its calcium-binding affinity enabling transamidation reactions inside cells.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Biochemical Journal. - 455 : 3 (2013), p. 261-272. -
További szerzők:Ergülen, Elvan Király Róbert (1975-) (biológus) Simon-Vecsei Zsófia (1980-) (biológus) Fuxreiter Mónika (1969-) (kutató vegyész) Fésüs László (1947-) (orvos biokémikus)
Pályázati támogatás:NK 105046
OTKA
TÁMOP-4.2.2.A-11/1/KONV-2012-0023-"VÉD-ELEM"
TÁMOP
TRANSCOM IAPP 251506
FP7
TRANSPATH ITN 289964
FP7
TÁMOP-4.2.4.A/2-11-1-2012-0001
TÁMOP
LP2012-41
Egyéb
Lendület program
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9.

001-es BibID:BIBFORM028726
Első szerző:Kiss Enikő
Cím:Integrin-linked kinase phosphorylates the myosin phosphatase target subunit at the inhibitory site in platelet cytoskeleton / Enikő Kiss, Andrea Murányi, Csilla Csortos, Pál Gergely, Masaaki Ito, David J. Hartshorne, Ferenc Erdődi
Dátum:2002
ISSN:0264-6021
Megjegyzések:The myosin phosphatase (MP) composed of the catalytic subunit of type 1 protein phosphatase and myosin phosphatase target subunit isoform 1 (MYPT1) was identified as the major serine/threonine phosphatase component in the platelet-cytoskeleton fraction. MYPT1 was phosphorylated by cytoskeletal kinase(s), but the identity of the kinase(s) and the effect of phosphorylation were not established. Incubation of platelet-cytoskeletal fraction with MgATP or MgATP[S] (magnesium adenosine 5'-[gamma-thio]triphosphate) caused a decrease in the 20 kDa light-chain of smooth-muscle myosin (MLC20) phosphatase and phosphorylase phosphatase activities. MYPT1 contains a phosphorylation site, Thr-695, involved in the inhibition of MP in a RhoA/Rho kinase-dependent manner. The cytoskeletal kinase(s) phosphorylated Thr-695 of glutathione S-transferase (GST)-MYPT1, as determined with an antibody specific for phosphorylated Thr-695. The level of Rho kinase was low in the cytoskeletal fraction and was detected primarily in the membrane and cytosolic fractions. The phosphorylation of Thr-695 by the cytoskeletal kinase(s) was not affected by Rho kinase inhibitor, Y-27632, suggesting that kinase(s) other than Rho kinase were involved. In-gel kinase assay identified a kinase at 54-59 kDa that phosphorylated the C-terminal fragment of MYPT1 (GST-MYPT1(667-1004)). Western blots detected both zipper-interacting protein kinase (ZIPK) and integrin-linked kinase (ILK) at 54-59 kDa in the cytoskeleton and membrane fractions. Cytoskeletal ZIPK and ILK were separated and partially purified by chromatography on SP-Sepharose and on MonoQ. ZIPK preferentially phosphorylated MLC20 and had low activity on MYPT1. ILK phosphorylated both MLC20 and MYPT1 and phosphorylation of MYPT1 occured on Thr-695. The above results raise the potential for regulation of MP activity in platelet cytoskeleton by ILK and suggest an alternative to the Rho-linked pathway.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
egyetemen (Magyarországon) készült közlemény
Megjelenés:Biochemical Journal. - 365 : 1 (2002), p. 79-87. -
További szerzők:Murányi Andrea (1966-) (biokémikus) Ito, Masaaki Hartshorne, David J. Erdődi Ferenc (1953-) (biokémikus) Csortos Csilla (1956-) (biokémikus) Gergely Pál (1947-) (biokémikus)
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10.

001-es BibID:BIBFORM051293
Első szerző:Kivinen, Niko
Cím:Hsp70 binds reversibly to proteasome inhibitor-induced protein aggregates and evades autophagic clearance in ARPE-19 cells / Niko Kivinen, Juha M. T. Hyttinen, Johanna Viiri, Jussi Paterno, Szabolcs Felszeghy, Anu Kauppinen, Antero Salminen, Kai Kaarniranta
Dátum:2014
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Journal of Biochemical and Pharmacological Research. - 2 : 1 (2014), p. 1-7. -
További szerzők:Hyttinen, Juha M. T. Viiri, Johanna Paterno, Jussi Felszeghy Szabolcs Béla (1972-) (fogorvos, anatómus, kötőszövetbiológus) Kauppinen, Anu (1977-) (sejtbiológus) Salminen, Antero Kaarniranta, Kai (1972-) (szemész szakorvos)
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11.

001-es BibID:BIBFORM028725
Első szerző:Murányi Andrea (biokémikus)
Cím:Phosphorylation of the myosin phosphatase target subunit by integrin-linked kinase / Andrea Murányi, Justin A. MacDonald, Jing Ti Deng, David P. Wilson, Timothy A. J. Haystead, Michael P. Walsh, Ferenc Erdődi, Enikő Kiss, Yue Wu, David J. Hartshorne
Dátum:2002
ISSN:0264-6021
Megjegyzések:A mechanism proposed for regulation of myosin phosphatase (MP) activity is phosphorylation of the myosin phosphatase target subunit (MYPT1). Integrin-linked kinase (ILK) is associated with the contractile machinery and can phosphorylate myosin at the myosin light-chain kinase sites. The possibility that ILK may also phosphorylate and regulate MP was investigated. ILK was associated with the MP holoenzyme, shown by Western blots and in-gel kinase assays. MYPT1 was phosphorylated by ILK and phosphorylation sites in the N- and C-terminal fragments of MYPT1 were detected. From sequence analyses, three sites were identified: a primary site at Thr(709), and two other sites at Thr(695) and Thr(495). One of the sites for cAMP-dependent protein kinase (PKA) was Ser(694). Assays with the catalytic subunit of type 1 phosphatase indicated that only the C-terminal fragment of MYPT1 phosphorylated by zipper-interacting protein kinase, and ILK inhibited activity. The phosphorylated N-terminal fragment activated phosphatase activity and phosphorylation by PKA was without effect. Using full-length MYPT1 constructs phosphorylated by various kinases it was shown that Rho kinase gave marked inhibition; ILK produced an intermediate level of inhibition, which was considerably reduced for the Thr(695)-->Ala mutant; and PKA had no effect. In summary, phosphorylation of the various sites indicated that Thr(695) was the major inhibitory site, Thr(709) had only a slight inhibitory effect and Ser(694) had no effect. The findings that ILK phosphorylated both MYPT1 and myosin and the association of ILK with MP suggest that ILK may influence cytoskeletal structure or function.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
külföldön készült közlemény
Megjelenés:Biochemical Journal. - 366 (2002), p. 211-216. -
További szerzők:MacDonald, Justin A. Deng, Jing Ti Wilson, David P. Haystead, Timothy A. J. Walsh, Michael P. Kiss Enikő Wu, Yue Hartshorne, David J. Erdődi Ferenc (1953-) (biokémikus)
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12.

001-es BibID:BIBFORM006788
Első szerző:Piccardoni, Paola
Cím:SRC-dependent outside-in signalling is a key step in the process of autoregulation of beta2 integrins in polymorphonuclear cells / Piccardoni, P., Manarini, S., Federico, L., Bagoly, Z., Pecce, R., Martelli, N., Piccoli, A., Totani, L., Cerletti, C., Evangelista, V.
Dátum:2004
ISSN:1470-8728
Megjegyzések:In human PMN (polymorphonuclear cells), challenged by P-selectin, the beta2-integrin Mac-1 (macrophage antigen-1) promoted the activation of the SRC (cellular homologue of Rous sarcoma virus oncogenic protein) family members HCK (haematopoietic cell kinase) and LYN (an SRC family protein tyrosine kinase) and phosphorylation of a P-110 (110 kDa protein). SRC kinase activity in turn was necessary for macrophage antigen-1-mediated adhesion [Piccardoni, Sideri, Manarini, Piccoli, Martelli, de Gaetano, Cerletti and Evangelista (2001) Blood 98, 108-116]. This suggested that an SRC-dependent outside-in signalling strengthens the beta2-integrin interaction with the ligand. To support this hypothesis further, in the present study, we used the monoclonal antibody KIM127 or manganese to lock beta2 integrins in a high-affinity state, and homotypic PMN adhesion was analysed to monitor beta2-integrin adhesive function. KIM127 or manganese induced PMN homotypic adhesion and P-110 phosphorylation. Both these processes were abolished by blocking antibodies against the common beta2 chain, by a combination of antibodies against alphaL and alphaM or by inhibitors of SRC activity. Confocal microscopy showed that activation epitopes were expressed by beta2 integrins co-localized with patches of F-actin at the adhesion sites. Blockade of SRC kinases or of actin polymerization prevented clustering of activated integrins as well as F-actin accumulation. FACS analysis showed that SRC inhibitors modified neither basal nor manganese-induced KIM127 binding. An SRC-dependent outside-in signalling initiated by beta2 integrins was also required for adhesion triggered by interleukin-8. These results confirm the hypothesis that an SRC-dependent outside-in signalling triggered by high affinity and ligand binding is necessary to stabilize beta2-integrin-mediated adhesion. Allowing clustering of activated integrins, SRC might link the high-affinity with the high-avidity state. Proline-rich tyrosine kinase-2 appears to be involved in this process.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Actins
Adult
Antibodies, Monoclonal
Cell Adhesion
Cells, Cultured
Enzyme Activation
Enzyme Inhibitors
Flow Cytometry
Focal Adhesion Kinase 2
Humans
Interleukin-8
Lymphocyte Function-Associated Antigen-1
Macrophage-1 Antigen
Neutrophils
P-Selectin
Phosphorylation
Protein Processing, Post-Translational
Protein-Tyrosine Kinases
Stress, Mechanical
Megjelenés:The Biochemical Journal. - 380 : Pt 1 (2004), p. 57-65. -
További szerzők:Manarini, Stefan Federico, Lorenzo Bagoly Zsuzsa (1978-) (orvos) Pecce, Romin Martelli, Nicol Piccoli, Antoni Totani, Licia Cerletti, Chiara Evangelista, Virgilio
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