https://m2.mtmt.hu/ hun 2026-09-21 05:13 JournalArticle 35217359 VALIDATED true 0 false 2026-07-16T15:13:26.056+0000 2024-09-30T09:06:07.435+0000 2024-09-06T14:35:00.070+0000 true 10052421 Wisniewski Éva /api/author/10052421 Author Wisniewski Éva (Sejtélettan) true 10052421 2024-12-18T09:49:43.030+0000 2024-09-12T09:52:14.897+0000 true 10080205 Szalóky-Siki Ágnes /api/admin/10080205 Admin Szalóky-Siki Ágnes (SE_KK_Admin5_SZSA, admin) true Admin 10014568 /api/admin/10014568 Vándor Andrea (VA, admin) Vándor Andrea true 10014568 true 2025-04-30T11:24:07.640+0000 true false true 24 24 /api/publicationtype/24 PublicationType Folyóiratcikk 1 true 24 JournalArticle true 10000059 Article true 24 24 /api/publicationtype/24 PublicationType Folyóiratcikk 1 true 24 JournalArticle /api/subtype/10000059 Szakcikk SubType Szakcikk (Folyóiratcikk) 101 true 10000059 true 1 /api/category/1 Category Tudományos true 1 Sasvári, Péter true true /api/journal/10019966 REVIEWED SCIENTIFIC REPORTS 2045-2322 true false 10019966 false 10019966 true 2045-2322 Journal FOREIGN 14 1 20106 20106 13 2024 ARHGAP25, a crucial molecule in immunological processes, serves as a Rac-specific GTPase-activating protein. Its role in cell migration and phagocyte functions, affecting the outcome of complex immunological diseases such as rheumatoid arthritis, renders it a promising target for drug research. Despite its importance, our knowledge of its intracellular interactions is still limited. This study employed proteomic analysis of glutathione S-transferase (GST)-tag pulldowns and co-immunoprecipitation from neutrophilic granulocyte cell lysate, revealing 76 candidates for potential physical interactions that complement ARHGAP25’s known profile. Notably, four small GTPases (RAC2, RHOG, ARF4, and RAB27A) exhibited high affinity for ARHGAP25. The ARHGAP25–RAC2 and ARHGAP25–RHOG interactions appeared to be affected by the activation state of the small GTPases, suggesting a GTP–GDP cycle-dependent interaction. In silico dimer prediction pinpointed ARHGAP25’s GAP domain as a credible binding interface, suggesting its suitability for GTP hydrolysis. Additionally, a list of Fc receptor-related kinases, phosphatases, and three of the 14-3-3 members were identified as potential partners, with in silico predictions highlighting eight binding sites, presenting novel insight on a potential regulatory mechanism for ARHGAP25. Funding 2043979 /api/funding/2043979 (FK_18 128376) false true Funding 2043980 /api/funding/2043980 (TKP2021-EGA-24) false true Funding 2043981 /api/funding/2043981 HCEMM(2022-2.1.1-NL-2022-00005) Támogató: NKFIH false true Funding 2043982 /api/funding/2043982 (GINOP-2.3.2-15-2016-00001) false true Funding 2043983 /api/funding/2043983 European Regional Development Fund(GINOP-2.3.2-15-2016-00020) Támogató: GINOP false true Funding 2043984 /api/funding/2043984 (Open access funding provided by Semmelweis University) false true true true 2024 true true true false true false GOLD 2026-07-16 true https://real.mtak.hu/217838 3 0 3 2 1 3 3 3 3 3 3 2 2 2 1 0 3 2 3 2 0 10 10 Folyóiratcikk Journal Article 24 3 Könyvrészlet Chapter in Book 25 0 Könyv Book 23 0 Egyéb konferenciaközlemény Conference paper 31 0 Egyéb konferenciakötet Conference proceedings 32 0 Oltalmi formák Protection forms 26 0 Disszertáció Thesis 28 0 Egyéb Miscellaneous 29 0 Alkotás Achievement 22 0 Kutatási adat Research data 33 0 Folyóiratcikk Journal Article 24 0 0 0 Könyvrészlet Chapter in Book 25 0 0 0 Könyv Book 23 0 0 0 Egyéb konferenciaközlemény Conference paper 31 0 0 0 Egyéb konferenciakötet Conference proceedings 32 0 0 0 Oltalmi formák Protection forms 26 0 0 0 Disszertáció Thesis 28 0 0 0 Egyéb Miscellaneous 29 0 0 0 Alkotás Achievement 22 0 0 0 Kutatási adat Research data 33 0 0 0 2025 0 2 1 2 1 2026 0 1 1 1 1 Q1 A nemzetközi false 10023793 false false false 2024-09-11T09:52:14.702+0000 Biokémiai Intézet (HRN SZBK); Központi Laboratóriumok (HRN SZBK); Élettani Intézet (SE / AOK / I) 4 17 3 4 0 true 10014568 Language 10002 /api/language/10002 Angol Angol English true 2 true PersonAuthorship 119004560 /api/authorship/119004560 Sasvári, Péter [Sasvári, Péter (Élettan), szerző] Élettani Intézet (SE / AOK / I) 1 0.25 true false false Author 10085543 /api/author/10085543 Sasvári Péter (Élettan) Sasvári Péter true true Sasvári Péter true false false AuthorshipType 1 /api/authorshiptype/1 Szerző 0 true 0 true false true PersonAuthorship 119004561 /api/authorship/119004561 Pettkó-Szandtner, Aladár [Pettkó-Szandtner, Aladár (növénybiológia), szerző] Biokémiai Intézet (HRN SZBK); Központi Laboratóriumok (HRN SZBK) 2 0.25 false false false Author 10025208 /api/author/10025208 Pettkó-Szandtner Aladár (növénybiológia) Pettkó-Szandtner Aladár true 10025208 true Pettkó-Szandtner Aladár true false false AuthorshipType 1 /api/authorshiptype/1 Szerző 0 true 0 true false true PersonAuthorship 119004562 /api/authorship/119004562 Wisniewski, Éva [Wisniewski, Éva (Sejtélettan), szerző] Élettani Intézet (SE / AOK / I) 3 0.25 false false false Author 10052421 /api/author/10052421 Wisniewski Éva (Sejtélettan) Wisniewski Éva true 10052421 true Wisniewski Éva true false false AuthorshipType 1 /api/authorshiptype/1 Szerző 0 true 0 true false true PersonAuthorship 119004563 /api/authorship/119004563 Csépányi-Kömi, Roland ✉ [Csépányi-Kömi, Roland (élettan), szerző] Élettani Intézet (SE / AOK / I) 4 0.25 false true true Author 10023793 /api/author/10023793 Csépányi-Kömi Roland (élettan) Csépányi-Kömi Roland true 10023793 true Csépányi-Kömi Roland true false false AuthorshipType 1 /api/authorshiptype/1 Szerző 0 true 0 true false true PublicationIdentifier 27056273 /api/publicationidentifier/27056273 DOI: 10.1038/s41598-024-71002-4 PlainSource 6 /api/publicationsource/6 DOI PublicationSourceType 10001 /api/publicationsourcetype/10001 DOI true true true DOI DOI https://doi.org/@@@ true true 6 true IDENTICAL 10.1038/s41598-024-71002-4 https://doi.org/10.1038/s41598-024-71002-4 false true PublicationIdentifier 27163952 /api/publicationidentifier/27163952 WoS: 001304109300016 PlainSource 1 /api/publicationsource/1 WoS PublicationSourceType 10003 /api/publicationsourcetype/10003 Indexelő adatbázis false true true WoS WoS https://www.webofscience.com/wos/woscc/full-record/@@@ true true 1 true IDENTICAL 001304109300016 https://www.webofscience.com/wos/woscc/full-record/001304109300016 true true PublicationIdentifier 29243679 /api/publicationidentifier/29243679 REAL: 217838 SwordSource 36 /api/publicationsource/36 REAL PublicationSourceType 10007 /api/publicationsourcetype/10007 Repozitórium true true true REAL REAL https://real.mtak.hu/@@@ true true 36 true GOLD true 217838 https://real.mtak.hu/217838 false true PublicationIdentifier 27163947 /api/publicationidentifier/27163947 Scopus: 85202747558 PlainSource 3 /api/publicationsource/3 Scopus PublicationSourceType 10003 /api/publicationsourcetype/10003 Indexelő adatbázis false true true Scopus Scopus http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-@@@ true true 3 true IDENTICAL 85202747558 http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-85202747558 true true PublicationIdentifier 27163953 /api/publicationidentifier/27163953 PubMed: 39210013 PlainSource 17 /api/publicationsource/17 PubMed PublicationSourceType 10003 /api/publicationsourcetype/10003 Indexelő adatbázis false true true PubMed PubMed http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=@@@&dopt=Abstract true true 17 true IDENTICAL 39210013 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=39210013&dopt=Abstract true true MtaRating 519359 /api/mtarating/519359 IX. Szociológiai Tudományos Bizottság:A nemzetközi SCIENTIFIC REPORTS 2045-2322 RatingType 10007 /api/ratingtype/10007 IX. Szociológiai Tudományos Bizottság SZTB Institute 14102 /api/institute/14102 Szociológiai Tudományos Bizottság IXGJO SZTB [1901-] 0 false true false Szociológiai Tudományos Bizottság Committee on Sociology true 14102 true true true A nemzetközi true 19359 true MtaRating 11551161 /api/mtarating/11551161 IX. Regionális Tudományok Bizottsága:B nemzetközi SCIENTIFIC REPORTS 2045-2322 RatingType 10010 /api/ratingtype/10010 IX. Regionális Tudományok Bizottsága RegTB Institute 14100 /api/institute/14100 Regionális Tudományok Bizottsága IXGJO RTB [1901-] 0 false true false Regionális Tudományok Bizottsága Committee on Regional Studies true 14100 true true true B nemzetközi false true SjrRating 11736109 /api/sjrrating/11736109 sjr:Q1 (2024) Scopus - Multidisciplinary SCIENTIFIC REPORTS 2045-2322 23 0.24 journal RatingType 10002 /api/ratingtype/10002 sjr sjr true true ClassificationExternal 1000 /api/classificationexternal/1000 Scopus - Multidisciplinary true 1000 true Q1 DIRECT true true Reference 57114489 /api/reference/57114489 1. El Masri, R. & Delon, J. RHO GTPases: From new partners to complex immune syndromes. Nat. Rev. Immunol. 21, 499–513. https://doi.org/10.1038/s41577-021-00500-7 (2021)., DOI: 10.1038/s41577-021-00500-7 1 10.1038/s41577-021-00500-7 false true Reference 57114490 /api/reference/57114490 2. Csepanyi-Komi, R., Safar, D., Grosz, V., Tarjan, Z. L. & Ligeti, E. In silico tissue-distribution of human Rho family GTPase activating proteins. Small GTPases 4, 90–101. https://doi.org/10.4161/sgtp.23708 (2013)., DOI: 10.4161/sgtp.23708 2 10.4161/sgtp.23708 false true Reference 57114491 /api/reference/57114491 3. Ligeti, E., Welti, S. & Scheffzek, K. Inhibition and termination of physiological responses by GTPase activating proteins. Physiol. Rev. 92, 237–272. https://doi.org/10.1152/physrev.00045.2010 (2012)., DOI: 10.1152/physrev.00045.2010 3 10.1152/physrev.00045.2010 false true Reference 57114492 /api/reference/57114492 4. Csepanyi-Komi, R., Levay, M. & Ligeti, E. Rho/RacGAPs: Embarras de richesse?. Small GTPases 3, 178–182. https://doi.org/10.4161/sgtp.20040 (2012)., DOI: 10.4161/sgtp.20040 4 10.4161/sgtp.20040 false true Reference 57114493 /api/reference/57114493 5. Katoh, M. & Katoh, M. Identification and characterization of ARHGAP24 and ARHGAP25 genes in silico. Int. J. Mol. Med. 14, 333–338 (2004). 5 false true Reference 57114494 /api/reference/57114494 6. Wang, L. D. et al. Phosphoproteomic profiling of mouse primary HSPCs reveals new regulators of HSPC mobilization. Blood 128, 1465–1474. https://doi.org/10.1182/blood-2016-05-711424 (2016)., DOI: 10.1182/blood-2016-05-711424 6 10.1182/blood-2016-05-711424 false true Reference 57114495 /api/reference/57114495 7. Schlam, D. et al. Phosphoinositide 3-kinase enables phagocytosis of large particles by terminating actin assembly through Rac/Cdc42 GTPase-activating proteins. Nat. Commun. 6, 8623. https://doi.org/10.1038/ncomms9623 (2015)., DOI: 10.1038/ncomms9623 7 10.1038/ncomms9623 false true Reference 57114496 /api/reference/57114496 8. Csepanyi-Komi, R., Sirokmany, G., Geiszt, M. & Ligeti, E. ARHGAP25, a novel Rac GTPase-activating protein, regulates phagocytosis in human neutrophilic granulocytes. Blood 119, 573–582. https://doi.org/10.1182/blood-2010-12-324053 (2012)., DOI: 10.1182/blood-2010-12-324053 8 10.1182/blood-2010-12-324053 false true Reference 57114497 /api/reference/57114497 9. Lorincz, A. M., Szarvas, G., Smith, S. M. & Ligeti, E. Role of Rac GTPase activating proteins in regulation of NADPH oxidase in human neutrophils. Free Radic. Biol. Med. 68, 65–71. https://doi.org/10.1016/j.freeradbiomed.2013.12.001 (2014)., DOI: 10.1016/j.freeradbiomed.2013.12.001 9 10.1016/j.freeradbiomed.2013.12.001 false true Reference 57114498 /api/reference/57114498 10. Czaran, D. et al. Lacking ARHGAP25 mitigates the symptoms of autoantibody-induced arthritis in mice. Front. Immunol. 14, 1182278. https://doi.org/10.3389/fimmu.2023.1182278 (2023)., DOI: 10.3389/fimmu.2023.1182278 10 10.3389/fimmu.2023.1182278 false true Reference 57114499 /api/reference/57114499 11. Wisniewski, E. et al. A novel BRET-Based GAP assay reveals phosphorylation-dependent regulation of the RAC-specific GTPase activating protein ARHGAP25. FASEB J 36, e22584. https://doi.org/10.1096/fj.202200689R (2022)., DOI: 10.1096/fj.202200689R 11 10.1096/fj.202200689R false true Reference 57114500 /api/reference/57114500 12. Xu, K., Liu, B. & Ma, Y. The tumor suppressive roles of ARHGAP25 in lung cancer cells. Onco Targets Ther. 12, 6699–6710. https://doi.org/10.2147/OTT.S207540 (2019)., DOI: 10.2147/OTT.S207540 12 10.2147/OTT.S207540 false true Reference 57114501 /api/reference/57114501 13. Tao, L., Zhu, Y., Gu, Y., Zheng, J. & Yang, J. ARHGAP25: A negative regulator of colorectal cancer (CRC) metastasis via the Wnt/beta-catenin pathway. Eur. J. Pharmacol. 858, 172476. https://doi.org/10.1016/j.ejphar.2019.172476 (2019)., DOI: 10.1016/j.ejphar.2019.172476 13 10.1016/j.ejphar.2019.172476 false true Reference 57114502 /api/reference/57114502 14. Huang, W. K. et al. ARHGAP25 inhibits pancreatic adenocarcinoma growth by suppressing glycolysis via AKT/mTOR pathway. Int. J. Biol. Sci. 17, 1808–1820. https://doi.org/10.7150/ijbs.55919 (2021)., DOI: 10.7150/ijbs.55919 14 10.7150/ijbs.55919 false true Reference 57114503 /api/reference/57114503 15. Han, S., Jin, X., Hu, T. & Chi, F. ARHGAP25 suppresses the development of breast cancer by an ARHGAP25/Wnt/ASCL2 feedback loop. Carcinogenesis 44, 369–382. https://doi.org/10.1093/carcin/bgad042 (2023)., DOI: 10.1093/carcin/bgad042 15 10.1093/carcin/bgad042 false true Reference 57114504 /api/reference/57114504 16. Jumper, J. et al. Applying and improving AlphaFold at CASP14. Proteins 89, 1711–1721. https://doi.org/10.1002/prot.26257 (2021)., DOI: 10.1002/prot.26257 16 10.1002/prot.26257 false true Reference 57114505 /api/reference/57114505 17. Jumper, J. et al. Highly accurate protein structure prediction with AlphaFold. Nature 596, 583–589. https://doi.org/10.1038/s41586-021-03819-2 (2021)., DOI: 10.1038/s41586-021-03819-2 17 10.1038/s41586-021-03819-2 false true Reference 57114506 /api/reference/57114506 18. O’Reilly, F. J. et al. Protein complexes in cells by AI-assisted structural proteomics. Mol. Syst. Biol. 19, e11544. https://doi.org/10.15252/msb.202311544 (2023)., DOI: 10.15252/msb.202311544 18 10.15252/msb.202311544 false true Reference 57114507 /api/reference/57114507 19. Madeira, F. et al. 14-3-3-pred: Improved methods to predict 14–3-3-binding phosphopeptides. Bioinformatics 31, 2276–2283. https://doi.org/10.1093/bioinformatics/btv133 (2015)., DOI: 10.1093/bioinformatics/btv133 19 10.1093/bioinformatics/btv133 false true Reference 57114508 /api/reference/57114508 20. Huttlin, E. L. et al. The BioPlex network: A systematic exploration of the human interactome. Cell 162, 425–440. https://doi.org/10.1016/j.cell.2015.06.043 (2015)., DOI: 10.1016/j.cell.2015.06.043 20 10.1016/j.cell.2015.06.043 false true Reference 57114509 /api/reference/57114509 21. Huttlin, E. L. et al. Architecture of the human interactome defines protein communities and disease networks. Nature 545, 505–509. https://doi.org/10.1038/nature22366 (2017)., DOI: 10.1038/nature22366 21 10.1038/nature22366 false true Reference 57114510 /api/reference/57114510 22. Huttlin, E. L. et al. Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. Cell 184, 3022-3040.e3028. https://doi.org/10.1016/j.cell.2021.04.011 (2021)., DOI: 10.1016/j.cell.2021.04.011 22 10.1016/j.cell.2021.04.011 false true Reference 57114511 /api/reference/57114511 23. Stark, C. et al. BioGRID: A general repository for interaction datasets. Nucleic Acids Res. 34, D535-539. https://doi.org/10.1093/nar/gkj109 (2006)., DOI: 10.1093/nar/gkj109 23 10.1093/nar/gkj109 false true Reference 57114512 /api/reference/57114512 24. Hayes, S., Malacrida, B., Kiely, M. & Kiely, P. A. Studying protein–protein interactions: Progress, pitfalls and solutions. Biochem. Soc. Trans. 44, 994–1004. https://doi.org/10.1042/BST20160092 (2016)., DOI: 10.1042/BST20160092 24 10.1042/BST20160092 false true Reference 57114513 /api/reference/57114513 25. Bagci, H. et al. Mapping the proximity interaction network of the Rho-family GTPases reveals signalling pathways and regulatory mechanisms. Nat Cell Biol. 22, 120–134. https://doi.org/10.1038/s41556-019-0438-7 (2020)., DOI: 10.1038/s41556-019-0438-7 25 10.1038/s41556-019-0438-7 false true Reference 57114514 /api/reference/57114514 26. Csepanyi-Komi, R. et al. Rac GTPase activating protein ARHGAP25 regulates leukocyte transendothelial migration in mice. J. Immunol. 197, 2807–2815. https://doi.org/10.4049/jimmunol.1502342 (2016)., DOI: 10.4049/jimmunol.1502342 26 10.4049/jimmunol.1502342 false true Reference 57114515 /api/reference/57114515 27. Muller, P. M. et al. Systems analysis of RhoGEF and RhoGAP regulatory proteins reveals spatially organized RAC1 signalling from integrin adhesions. Nat. Cell Biol. 22, 498–511. https://doi.org/10.1038/s41556-020-0488-x (2020)., DOI: 10.1038/s41556-020-0488-x 27 10.1038/s41556-020-0488-x false true Reference 57114516 /api/reference/57114516 28. Kouchi, Z. & Kojima, M. A structural network analysis of neuronal ArhGAP21/23 interactors by computational modeling. ACS Omega 8, 19249–19264. https://doi.org/10.1021/acsomega.2c08054 (2023)., DOI: 10.1021/acsomega.2c08054 28 10.1021/acsomega.2c08054 false true Reference 57114517 /api/reference/57114517 29. Hu, S. H. et al. The weak complex between RhoGAP protein ARHGAP22 and signal regulatory protein 14-3-3 has 1:2 stoichiometry and a single peptide binding mode. PLoS One 7, e41731. https://doi.org/10.1371/journal.pone.0041731 (2012)., DOI: 10.1371/journal.pone.0041731 29 10.1371/journal.pone.0041731 false true Reference 57114518 /api/reference/57114518 30. He, L. et al. ARHGAP45 controls naive T- and B-cell entry into lymph nodes and T-cell progenitor thymus seeding. EMBO Rep. 22, e52196. https://doi.org/10.15252/embr.202052196 (2021)., DOI: 10.15252/embr.202052196 30 10.15252/embr.202052196 false true Reference 57114519 /api/reference/57114519 31. Quinn, M. T. Low-molecular-weight GTP-binding proteins and leukocyte signal transduction. J. Leukoc. Biol. 58, 263–276. https://doi.org/10.1002/jlb.58.3.263 (1995)., DOI: 10.1002/jlb.58.3.263 31 10.1002/jlb.58.3.263 false true Reference 57114520 /api/reference/57114520 32. Baker, M. J., Pan, D. & Welch, H. C. Small GTPases and their guanine-nucleotide exchange factors and GTPase-activating proteins in neutrophil recruitment. Curr. Opin. Hematol. 23, 44–54. https://doi.org/10.1097/MOH.0000000000000199 (2016)., DOI: 10.1097/MOH.0000000000000199 32 10.1097/MOH.0000000000000199 false true Reference 57114521 /api/reference/57114521 33. Cougoule, C., Hoshino, S., Dart, A., Lim, J. & Caron, E. Dissociation of recruitment and activation of the small G-protein Rac during Fcgamma receptor-mediated phagocytosis. J. Biol. Chem. 281, 8756–8764. https://doi.org/10.1074/jbc.M513731200 (2006)., DOI: 10.1074/jbc.M513731200 33 10.1074/jbc.M513731200 false true Reference 57114522 /api/reference/57114522 34. Sluchanko, N. N. Recent advances in structural studies of 14-3-3 protein complexes. Adv. Protein Chem. Struct. Biol. 130, 289–324. https://doi.org/10.1016/bs.apcsb.2021.12.004 (2022)., DOI: 10.1016/bs.apcsb.2021.12.004 34 10.1016/bs.apcsb.2021.12.004 false true Reference 57114523 /api/reference/57114523 35. Fu, H., Subramanian, R. R. & Masters, S. C. 14-3-3 proteins: Structure, function, and regulation. Annu. Rev. Pharmacol. Toxicol. 40, 617–647. https://doi.org/10.1146/annurev.pharmtox.40.1.617 (2000)., DOI: 10.1146/annurev.pharmtox.40.1.617 35 10.1146/annurev.pharmtox.40.1.617 false true Reference 57114524 /api/reference/57114524 36. Saha, M. et al. RSK phosphorylates SOS1 creating 14-3-3-docking sites and negatively regulating MAPK activation. Biochem. J. 447, 159–166. https://doi.org/10.1042/BJ20120938 (2012)., DOI: 10.1042/BJ20120938 36 10.1042/BJ20120938 false true Reference 57114525 /api/reference/57114525 37. Thuault, S. et al. The RhoE/ROCK/ARHGAP25 signaling pathway controls cell invasion by inhibition of Rac activity. Mol. Biol. Cell 27, 2653–2661. https://doi.org/10.1091/mbc.E16-01-0041 (2016)., DOI: 10.1091/mbc.E16-01-0041 37 10.1091/mbc.E16-01-0041 false true Reference 57114526 /api/reference/57114526 38. Fischer, R. & Kessler, B. M. Gel-aided sample preparation (GASP)–a simplified method for gel-assisted proteomic sample generation from protein extracts and intact cells. Proteomics 15, 1224–1229. https://doi.org/10.1002/pmic.201400436 (2015)., DOI: 10.1002/pmic.201400436 38 10.1002/pmic.201400436 false true Reference 57114527 /api/reference/57114527 39. Kobayashi, K. et al. Transcriptional repression by MYB3R proteins regulates plant organ growth. EMBO J. 34, 1992–2007. https://doi.org/10.15252/embj.201490899 (2015)., DOI: 10.15252/embj.201490899 39 10.15252/embj.201490899 false true Reference 57114528 /api/reference/57114528 40. Yu, F., Haynes, S. E. & Nesvizhskii, A. I. IonQuant enables accurate and sensitive label-free quantification with FDR-controlled match-between-runs. Mol. Cell Proteom. 20, 100077. https://doi.org/10.1016/j.mcpro.2021.100077 (2021)., DOI: 10.1016/j.mcpro.2021.100077 40 10.1016/j.mcpro.2021.100077 false true Reference 57114529 /api/reference/57114529 41. Ge, S. X., Jung, D. & Yao, R. ShinyGO: A graphical gene-set enrichment tool for animals and plants. Bioinformatics 36, 2628–2629. https://doi.org/10.1093/bioinformatics/btz931 (2020)., DOI: 10.1093/bioinformatics/btz931 41 10.1093/bioinformatics/btz931 false true Reference 57114530 /api/reference/57114530 42. Hoogendijk, A. J. et al. Dynamic transcriptome-proteome correlation networks reveal human myeloid differentiation and neutrophil-specific programming. Cell Rep. 29, 2505-2519.e2504. https://doi.org/10.1016/j.celrep.2019.10.082 (2019)., DOI: 10.1016/j.celrep.2019.10.082 42 10.1016/j.celrep.2019.10.082 false true Reference 57114531 /api/reference/57114531 43. Szklarczyk, D. et al. The STRING database in 2023: Protein–protein association networks and functional enrichment analyses for any sequenced genome of interest. Nucleic Acids Res. 51, D638–D646. https://doi.org/10.1093/nar/gkac1000 (2023)., DOI: 10.1093/nar/gkac1000 43 10.1093/nar/gkac1000 false true Reference 57114532 /api/reference/57114532 44. Shannon, P. et al. Cytoscape: A software environment for integrated models of biomolecular interaction networks. Genome Res. 13, 2498–2504. https://doi.org/10.1101/gr.1239303 (2003)., DOI: 10.1101/gr.1239303 44 10.1101/gr.1239303 false true Reference 57114533 /api/reference/57114533 45. Mirdita, M. et al. ColabFold: Making protein folding accessible to all. Nat. Methods 19, 679–682. https://doi.org/10.1038/s41592-022-01488-1 (2022)., DOI: 10.1038/s41592-022-01488-1 45 10.1038/s41592-022-01488-1 false true /api/publication/35217359 Sasvári Péter et al. Neutrophil-specific interactome of ARHGAP25 reveals novel partners and regulatory insights. (2024) SCIENTIFIC REPORTS 2045-2322 14 1<div class="JournalArticle Publication long-list"> <div class="authors"> <img title="Forrásközlemény" style="float: left" src="/frontend/resources/grid/publication-core-icon.png"> <img title="Idézőközlemény" style="float: left" src="/frontend/resources/grid/publication-citation-icon.png"> <div class="autype autype0"> <span class="author-name" mtid="10085543"><a href="/gui2/?type=authors&mode=browse&sel=10085543" target="_blank">Sasvári Péter (<span class="authorship-author-name">Sasvári Péter</span> <span class="authorAux-mtmt"> Élettan</span>) </a> </span> <span class="author-affil"><span title="Semmelweis Egyetem">SE</span>/<span title="Általános Orvostudományi Kar">AOK</span>/<span title="Intézet">I</span>/Élettani Intézet</span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" mtid="10025208"><a href="/gui2/?type=authors&mode=browse&sel=10025208" target="_blank">Pettkó-Szandtner Aladár (<span class="authorship-author-name">Pettkó-Szandtner Aladár</span> <span class="authorAux-mtmt"> növénybiológia</span>) </a> </span> <span class="author-affil"><span title="HUN-REN Szegedi Biológiai Kutatóközpont">HRN SZBK</span>/Biokémiai Intézet; <span title="HUN-REN Szegedi Biológiai Kutatóközpont">HRN SZBK</span>/Központi Laboratóriumok</span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" mtid="10052421"><a href="/gui2/?type=authors&mode=browse&sel=10052421" target="_blank">Wisniewski Éva (<span class="authorship-author-name">Wisniewski Éva</span> <span class="authorAux-mtmt"> Sejtélettan</span>) </a> </span> <span class="author-affil"><span title="Semmelweis Egyetem">SE</span>/<span title="Általános Orvostudományi Kar">AOK</span>/<span title="Intézet">I</span>/Élettani Intézet</span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" mtid="10023793"><a href="/gui2/?type=authors&mode=browse&sel=10023793" target="_blank">Csépányi-Kömi Roland ✉ (<span class="authorship-author-name">Csépányi-Kömi Roland</span> <span class="authorAux-mtmt"> élettan</span>) </a> </span> <span class="author-affil"><span title="Semmelweis Egyetem">SE</span>/<span title="Általános Orvostudományi Kar">AOK</span>/<span title="Intézet">I</span>/Élettani Intézet</span> </div> </div> <div class="title"><a href="/gui2/?mode=browse&params=publication;35217359" target="_blank">Neutrophil-specific interactome of ARHGAP25 reveals novel partners and regulatory insights</a></div> <div> <span class="journal-title">SCIENTIFIC REPORTS</span> <span class="journal-issn">( <a target="_blank" href="https://portal.issn.org/resource/ISSN/2045-2322">2045-2322</a>)</span>: <span class="journal-volume">14</span> <span class="journal-issue">1</span> <span class="page"> Paper 20106. 13 p. </span> <span class="year">(2024)</span> </div> <div class="pub-footer"> <span class="language" xmlns="http://www.w3.org/1999/html">Nyelv: Angol | </span> <span class="identifiers"> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="10.1038/s41598-024-71002-4" target="_blank" href="https://doi.org/10.1038/s41598-024-71002-4"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="001304109300016" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/001304109300016"> WoS </a> </span> <span class="id identifier oa_GOLD" title=" Gold "> <a style="color:black" title="217838" target="_blank" href="https://real.mtak.hu/217838"> REAL </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="85202747558" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-85202747558"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="39210013" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=39210013&dopt=Abstract"> PubMed </a> </span> </span> <OnlyViewableByAuthor><div class="ratings"> <div class="journal-subject">Folyóirat szakterülete: Scopus - Multidisciplinary&nbsp;&nbsp;&nbsp;SJR indikátor:&nbsp;Q1</div> <div class="journal-subject">Szociológiai Tudományos Bizottság IXGJO SZTB [1901-]&nbsp;&nbsp;&nbsp;A nemzetközi</div> <div class="journal-subject">Regionális Tudományok Bizottsága IXGJO RTB [1901-]&nbsp;&nbsp;&nbsp;B nemzetközi</div> </div></OnlyViewableByAuthor> <div class="publication-citation" style="margin-left: 0.5cm;"> <span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 3</span> | Független: 2 | Függő: 1 | Nem jelölt: 0 | WoS jelölt: 3 | Scopus jelölt:&nbsp;3 | WoS/Scopus jelölt:&nbsp;3 | DOI jelölt:&nbsp;3 </div> <div class="publication-citation"> <a target="_blank" href="/api/publication?cond=citations.related;eq;35217359&sort=publishedYear,desc&sort=title"> Idézett közlemények száma: 10 </a> </div> <div class="mtid"><span class="long-pub-mtid">Közlemény: 35217359</span> | <span class="status-data status-VALIDATED"> Egyeztetett </span> Forrás Idéző | <span class="type-subtype">Folyóiratcikk ( Szakcikk ) </span> | <span class="pub-category">Tudományos</span> | <span class="publication-sourceOfData">kézi felvitel</span> </div> <div class="funder"> (FK_18 128376), (TKP2021-EGA-24), HCEMM(2022-2.1.1-NL-2022-00005) Támogató: NKFIH, (GINOP-2.3.2-15-2016-00001), European Regional Development Fund(GINOP-2.3.2-15-2016-00020) Támogató: GINOP, (Open access funding provided by Semmelweis University) </div> <div class="lastModified">Utolsó módosítás: 2024.09.30. 11:06 Patkósné Hanesz Andrea (SZBK-4-es admin) </div> <div class="lockedBy">Központi kezelésű 2025.04.30. 13:24 Vándor Andrea (VA, admin) </div> </div></div>