TY - JOUR AU - Jávor, Péter János AU - Donka, Tibor AU - Solli, Hanne Sofie AU - Sándor, Lilla AU - Baráth, Bálint AU - Perényi, Domonkos AU - Mohácsi, Árpád AU - Török, László AU - Hartmann, Petra TI - Could exhaled methane be used as a possible indicator for hemodynamic changes in trauma induced hemorrhagic shock? Scientific basis supported by a case study JF - INJURY: INTERNATIONAL JOURNAL OF THE CARE OF THE INJURED J2 - INJURY VL - 55 PY - 2024 IS - Suppl. 3 PG - 6 SN - 0020-1383 DO - 10.1016/j.injury.2024.111456 UR - https://m2.mtmt.hu/api/publication/35422953 ID - 35422953 LA - English DB - MTMT ER - TY - JOUR AU - Kurokawa, Takayuki AU - Csete, Károly AU - Jávor, Péter János AU - Sándor, Lilla AU - Baráth, Bálint AU - Holovic, Helga AU - Török, László AU - Hartmann, Petra TI - Anterior cruciate ligament reconstruction in the elderly: 5-Year follow-up study JF - INJURY: INTERNATIONAL JOURNAL OF THE CARE OF THE INJURED J2 - INJURY VL - 55 PY - 2024 IS - Suppl. 3 PG - 7 SN - 0020-1383 DO - 10.1016/j.injury.2024.111529 UR - https://m2.mtmt.hu/api/publication/35419480 ID - 35419480 LA - English DB - MTMT ER - TY - JOUR AU - Nagy, Gergely Ármin AU - Tombácz, Dóra AU - Prazsák, István AU - Csabai, Zsolt AU - Dörmő, Ákos AU - Gulyás, Gábor AU - Kemenesi, Gábor AU - Tóth, Gábor Endre AU - Holoubek, Jiří AU - Růžek, Daniel AU - Kakuk, Balázs AU - Boldogkői, Zsolt TI - Exploring the transcriptomic profile of human monkeypox virus via CAGE and native RNA sequencing approaches JF - mSPHERE J2 - MSPHERE PY - 2024 PG - 22 SN - 2379-5042 DO - 10.1128/msphere.00356-24 UR - https://m2.mtmt.hu/api/publication/35201514 ID - 35201514 N1 - * Megosztott szerzőség WoS:hiba:001299806300004 2024-09-24 08:44 cikkazonosító nem egyezik LA - English DB - MTMT ER - TY - JOUR AU - Ábrahám, Ágnes AU - Dér, László AU - Csákvári, Eszter AU - Vizsnyiczai, Gaszton AU - Pap, Imre AU - Lukacs, Rebeka AU - Varga-Zsíros, Vanda AU - Nagy, Krisztina AU - Galajda, Péter TI - Single-cell level LasR-mediated quorum sensing response of Pseudomonas aeruginosa to pulses of signal molecules JF - SCIENTIFIC REPORTS J2 - SCI REP VL - 14 PY - 2024 IS - 1 PG - 20 SN - 2045-2322 DO - 10.1038/s41598-024-66706-6 UR - https://m2.mtmt.hu/api/publication/35159268 ID - 35159268 N1 - Funding Agency and Grant Number: HUN-REN Biological Research Centre, Szeged; National Research, Development, and Innovation Office, Hungary [OTKA PD 124889, K 116516, FK 138520]; Janos Bolyai Research Scholarship of the Hungarian Academy of Sciences [BO/00463/18/8, BO/00290/21/11]; Eoetvoes Lorand Research Network [SA-75/2021]; Dr. Rollin D. Hotchkiss Foundation; Hungarian Government; European 1106 Regional Development Fund [GINOP- 1107 2.3.2-15-2016-00001, GINOP-2.3.2-15-2016-00026, GINOP- 1108 2.3.2-15-2016-00037] Funding text: Open access funding provided by HUN-REN Biological Research Centre, Szeged. KN, PG, and GV acknowledge the support of the National Research, Development, and Innovation Office, Hungary, under grant numbers OTKA PD 124889, K 116516 and FK 138520. KN and VG were also supported by the Janos Bolyai Research Scholarship of the Hungarian Academy of Sciences (BO/00463/18/8 and BO/00290/21/11). VG was also sup-ported by the Eoetvoes Lorand Research Network under the grant number SA-75/2021. This work was also supported by the Dr. Rollin D. Hotchkiss Foundation. Furthermore, this work was 1105 supported by the Hungarian Government and the European 1106 Regional Development Fund under the Grant Numbers GINOP- 1107 2.3.2-15-2016-00001, GINOP-2.3.2-15-2016-00026, and GINOP- 1108 2.3.2-15-2016-00037. DAS:All data generated or analyzed during this study are included in this published article (and its Supplementary Information files). Raw data are available from the corresponding authors upon reasonable request. A subset of data is available in the BioImage Archive with the ID S-BIAD1158. AB - Quorum sensing (QS) is a communication form between bacteria via small signal molecules that enables global gene regulation as a function of cell density. We applied a microfluidic mother machine to study the kinetics of the QS response of Pseudomonas aeruginosa bacteria to additions and withdrawals of signal molecules. We traced the fast buildup and the subsequent considerably slower decay of a population-level and single-cell-level QS response. We applied a mathematical model to explain the results quantitatively. We found significant heterogeneity in QS on the single-cell level, which may result from variations in quorum-controlled gene expression and protein degradation. Heterogeneity correlates with cell lineage history, too. We used single-cell data to define and quantitatively characterize the population-level quorum state. We found that the population-level QS response is well-defined. The buildup of the quorum is fast upon signal molecule addition. At the same time, its decay is much slower following signal withdrawal, and the quorum may be maintained for several hours in the absence of the signal. Furthermore, the quorum sensing response of the population was largely repeatable in subsequent pulses of signal molecules. LA - English DB - MTMT ER - TY - JOUR AU - Csete, Károly AU - Baráth, Bálint AU - Sándor, Lilla AU - Holovic, Helga AU - Mátrai, Péter AU - Török, László AU - Hartmann, Petra TI - Does Combined Reconstruction of the Medial Collateral and Anterior Cruciate Ligaments Provide Better Knee Function? A Systematic Review and Meta-Analysis JF - JOURNAL OF CLINICAL MEDICINE J2 - J CLIN MED VL - 13 PY - 2024 IS - 13 PG - 12 SN - 2077-0383 DO - 10.3390/jcm13133882 UR - https://m2.mtmt.hu/api/publication/35135168 ID - 35135168 N1 - * Megosztott szerzőség AB - Objective: This study aimed to determine if medial collateral ligament reconstruction (MCLR) alongside anterior cruciate ligament reconstruction (ACLR) preserves knee functionality better than isolated ACLR in combined ACL and MCL tears. Methods: MEDLINE, EMBASE, Scopus, CENTRAL, and Web of Science were searched systematically on 31 March 2023. Studies reporting post-operative function after ACLR and ACLR + MCLR in combined injuries were included. Outcomes included International Knee Documentation Committee (IKDC) score, side-to-side difference (SSD), Lysholm, and Tegner scale values. Results: Out of 2362 papers, 8 studies met the criteria. The analysis found no significant difference in outcomes (MD = 3.63, 95% CI: [-5.05, 12.3] for IKDC; MD = -0.64, 95% CI: [-3.24, 1.96] for SSD at 0° extension; MD = -1.79, 95% CI: [-4.61, 1.04] for SSD at 30° extension; MD = -1.48, 95% CI: [-16.35, 13.39] for Lysholm scale; MD = -0.21, 95% CI: [-4.29, 3.87] for Tegner scale) between treatments. Conclusions: This meta-analysis found no significant difference in outcomes between ACLR and ACLR + MCLR, suggesting that adding MCLR does not provide additional benefits. Due to the heterogeneity and quality of the included studies, further high-quality randomized controlled trials are needed to determine the optimal treatment for combined severe MCL-ACL injuries. LA - English DB - MTMT ER - TY - JOUR AU - Karkas, Réka AU - Abdullah, Khaldoon Sadiq Ahmed AU - Kaizer, László AU - Ürmös, A AU - Raya, May AU - Tiszlavicz, Lilla Györgyi AU - Pankotai, Tibor AU - Nagy, István AU - Mátés, Lajos AU - Sükösd, Farkas TI - LINE-1 ORF1p is a Promising Biomarker in Cervical Intraepithelial Neoplasia Degree Assessment JF - INTERNATIONAL JOURNAL OF GYNECOLOGICAL PATHOLOGY J2 - INT J GYNECOL PATHOL PY - 2024 SN - 0277-1691 DO - 10.1097/PGP.0000000000001035 UR - https://m2.mtmt.hu/api/publication/34883229 ID - 34883229 LA - English DB - MTMT ER - TY - JOUR AU - Szabó, Enikő AU - Faragó, Anna AU - Bodor, Gergely AU - Gémes, Nikolett AU - Puskás, László AU - Kovács, László AU - Szebeni, Gábor TI - Identification of immune subsets with distinct lectin binding signatures using multi-parameter flow cytometry: correlations with disease activity in systemic lupus erythematosus JF - FRONTIERS IN IMMUNOLOGY J2 - FRONT IMMUNOL VL - 15 PY - 2024 PG - 22 SN - 1664-3224 DO - 10.3389/fimmu.2024.1380481 UR - https://m2.mtmt.hu/api/publication/34840255 ID - 34840255 N1 - Funding Agency and Grant Number: Nemzeti Kutatsi Fejlesztsi s Innovcis Hivatal10.13039/501100011019 Funding text: No Statement Available A közlemény a Bolyai János Kutatási Ösztöndíj (BO/00582/22/8) segítségével jött létre. LA - English DB - MTMT ER - TY - JOUR AU - Faragó, Anna AU - Zvara, Ágnes AU - Tiszlavicz, László AU - Hunyadi-Gulyás Éva, Csilla AU - Darula, Zsuzsanna AU - Hegedűs, Zoltán AU - Szabó, Enikő AU - Surguta, Sára Eszter AU - Tóvári, József AU - Puskás, László AU - Szebeni, Gábor TI - Lectin-Based Immunophenotyping and Whole Proteomic Profiling of CT-26 Colon Carcinoma Murine Model JF - INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES J2 - INT J MOL SCI VL - 25 PY - 2024 IS - 7 PG - 21 SN - 1661-6596 DO - 10.3390/ijms25074022 UR - https://m2.mtmt.hu/api/publication/34790193 ID - 34790193 N1 - * Megosztott szerzőség A közlemény a Bolyai János Kutatási Ösztöndíj (BO/00582/22/8) segítségével jött létre. AB - A murine colorectal carcinoma (CRC) model was established. CT26 colon carcinoma cells were injected into BALB/c mice's spleen to study the primary tumor and the mechanisms of cell spread of colon cancer to the liver. The CRC was verified by the immunohistochemistry of Pan Cytokeratin and Vimentin expression. Immunophenotyping of leukocytes isolated from CRC-bearing BALB/c mice or healthy controls, such as CD19+ B cells, CD11+ myeloid cells, and CD3+ T cells, was carried out using fluorochrome-labeled lectins. The binding of six lectins to white blood cells, such as galectin-1 (Gal1), siglec-1 (Sig1), Sambucus nigra lectin (SNA), Aleuria aurantia lectin (AAL), Phytolacca americana lectin (PWM), and galectin-3 (Gal3), was assayed. Flow cytometric analysis of the splenocytes revealed the increased binding of SNA, and AAL to CD3 + T cells and CD11b myeloid cells; and increased siglec-1 and AAL binding to CD19 B cells of the tumor-bearing mice. The whole proteomic analysis of the established CRC-bearing liver and spleen versus healthy tissues identified differentially expressed proteins, characteristic of the primary or secondary CRC tissues. KEGG Gene Ontology bioinformatic analysis delineated the established murine CRC characteristic protein interaction networks, biological pathways, and cellular processes involved in CRC. Galectin-1 and S100A4 were identified as upregulated proteins in the primary and secondary CT26 tumor tissues, and these were previously reported to contribute to the poor prognosis of CRC patients. Modelling the development of liver colonization of CRC by the injection of CT26 cells into the spleen may facilitate the understanding of carcinogenesis in human CRC and contribute to the development of novel therapeutic strategies. LA - English DB - MTMT ER - TY - JOUR AU - Kovács, Zoltán AU - Bajusz, Csaba AU - Szabó, Anikó AU - Borkúti, Péter AU - Vedelek, Balázs AU - Benke, Reka AU - Lipinszki, Zoltán AU - Kristó, Ildikó AU - Vilmos, Péter TI - A bipartite NLS motif mediates the nuclear import of Drosophila moesin JF - FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY J2 - FRONT CELL DEV BIOL VL - 12 PY - 2024 PG - 14 SN - 2296-634X DO - 10.3389/fcell.2024.1206067 UR - https://m2.mtmt.hu/api/publication/34743202 ID - 34743202 N1 - Funding Agency and Grant Number: NKFIH (Hungarian National Research, Development and Innovation Office) through the National Laboratory for Biotechnology program [PD127968, LP2017-7/2017]; Hungarian Academy of Sciences Lendulet Grant; [2022-2.1.1-NL-2022-00008] Funding text: This work was supported by NKFIH (Hungarian National Research, Development and Innovation Office) through the National Laboratory for Biotechnology program, grant 2022-2.1.1-NL-2022-00008 (PV), and PD127968 (IK), and the Hungarian Academy of Sciences Lendulet Grant LP2017-7/2017 (ZL). AB - The ERM protein family, which consists of three closely related proteins in vertebrates, ezrin, radixin, and moesin (ERM), is an ancient and important group of cytoplasmic actin-binding and organizing proteins. With their FERM domain, ERMs bind various transmembrane proteins and anchor them to the actin cortex through their C-terminal F-actin binding domain, thus they are major regulators of actin dynamics in the cell. ERMs participate in many fundamental cellular processes, such as phagocytosis, microvilli formation, T-cell activation and tumor metastasis. We have previously shown that, besides its cytoplasmic activities, the single ERM protein of Drosophila melanogaster, moesin, is also present in the cell nucleus, where it participates in gene expression and mRNA export. Here we study the mechanism by which moesin enters the nucleus. We show that the nuclear import of moesin is an NLS-mediated, active process. The nuclear localization sequence of the moesin protein is an evolutionarily highly conserved, conventional bipartite motif located on the surface of the FERM domain. Our experiments also reveal that the nuclear import of moesin does not require PIP2 binding or protein activation, and occurs in monomeric form. We propose, that the balance between the phosphorylated and non-phosphorylated protein pools determines the degree of nuclear import of moesin. LA - English DB - MTMT ER - TY - JOUR AU - Borkúti, Péter AU - Kristó, Ildikó AU - Szabó, Anikó AU - Kovács, Zoltán AU - Vilmos, Péter TI - FERM domain-containing proteins are active components of the cell nucleus JF - LIFE SCIENCE ALLIANCE J2 - LIFE SCI ALLIANCE VL - 7 PY - 2024 IS - 4 PG - 15 SN - 2575-1077 DO - 10.26508/lsa.202302489 UR - https://m2.mtmt.hu/api/publication/34575638 ID - 34575638 N1 - Funding Agency and Grant Number: NKFIH (Hungarian National Research, Development and Innovation Office) through the National Laboratory for Biotechnology program [2022-2.1.1-NL-2022-00008] Funding text: This work was supported by NKFIH (Hungarian National Research, Development and Innovation Office) through the National Laboratory for Biotechnology program, grant 2022-2.1.1-NL-2022-00008 (to P Vilmos) . AB - The FERM domain is a conserved and widespread protein module that appeared in the common ancestor of amoebae, fungi, and animals, and is therefore now found in a wide variety of species. The primary function of the FERM domain is localizing to the plasma membrane through binding lipids and proteins of the membrane; thus, for a long time, FERM domain-containing proteins (FDCPs) were considered exclusively cytoskeletal. Although their role in the cytoplasm has been extensively studied, the recent discovery of the presence and importance of cytoskeletal proteins in the nucleus suggests that FDCPs might also play an important role in nuclear function. In this review, we collected data on their nuclear localization, transport, and possible functions, which are still scattered throughout the literature, with special regard to the role of the FERM domain in these processes. With this, we would like to draw attention to the exciting, new dimension of the role of FDCPs, their nuclear activity, which could be an interesting novel direction for future research. LA - English DB - MTMT ER -