NIBAN1, Exploring its Roles in Cell Survival Under Stress Context
Open accessAbstract
Cell survival must quickly activate specific mechanisms that enable to detect changes in the cellular microenvironment. The impact of these cell alteration has direct consequences on cellular homeostasis. Cellular stress, as well as its regulation and implication, has been studied in different pathologies. In this sense, the alteration in NIBAN1 expression seems to act in response to different cellular disturbances. Over the years, the knowledge of NIBAN1 functions has improved, demonstrating its important cell roles, favoring the cell survival under stress context. In response to the disturbances, NIBAN1 seems to be involved in the decision-making process between cell survival and death. The increase in NIBAN1 expression has been related to cellular mechanisms that seek to minimize the damage caused to cellular homeostasis. In this review, the main biological insights attributed to the NIBAN1 gene in different cellular contexts and its role as a mediator of cellular stress are discussed.
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All three microglial sub-populations showed upregulation of APOE, ATG16L2, BCL2, CCNH and GAS7; negative regulators of senescence GRB2 and NIBAN1 were downregulated with increasing β-amyloid.
“All three microglial sub-populations showed upregulation of APOE, ATG16L2 (an autophagy antagonist gene), BCL2 (encoding a negative regulator of apoptosis), the CDK7 regulator gene CCNH and GAS7 (the growth arrest-specific protein 7 gene). Genes for negative regulators of senescence such as GRB2 and NIBAN1 were downregulated with increasing β-amyloid [17, 21, 34, 55].”
From Characterisation of premature cell senescence in Alzheimer's disease using single nuclear transcriptomics (2024) · cites this paper as [17]
The Cell Stress section (page unavailable) says NIBAN1 can suppress senescence in a prostate-cancer stress context, supporting its description as a negative regulator of senescence. It does not report NIBAN1 or GRB2 being downregulated as β-amyloid increases, or the stated expression changes across three microglial sub-populations. (LLM, conf=0.88)
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works
Tissue-based map of the human proteome
Uhlén, M., Fagerberg, L., Hallström, B. M., Lindskog, C., Oksvold, P., Mardinoglu, A., Sivertsson, Å., Kampf, C., Sjöstedt, E., Asplund, A., et al. (2015) · Science · doi:10.1126/science.1260419 · Cited by 15,286 · see citing works
Varadi, M., Anyango, S., Deshpande, M., Nair, S., Natassia, C., Yordanova, G., Yuan, D., Stroe, O., Wood, G., Laydon, A., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkab1061 · Cited by 7,850 · see citing works
The Unfolded Protein Response: From Stress Pathway to Homeostatic Regulation
Walter, P., & Ron, D. (2011) · Science · doi:10.1126/science.1209038 · Cited by 5,893 · see citing works
A pathology atlas of the human cancer transcriptome
Uhlen, M., Zhang, C., Lee, S., Sjöstedt, E., Fagerberg, L., Bidkhori, G., Benfeitas, R., Arif, M., Liu, Z., Edfors, F., et al. (2017) · Science · doi:10.1126/science.aan2507 · Cited by 3,371 · see citing works
PhosphoSitePlus, 2014: mutations, PTMs and recalibrations
Hornbeck, P. V., Zhang, B., Murray, B., Kornhauser, J. M., Latham, V. M., & Skrzypek, E. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku1267 · Cited by 3,243 · see citing works
The Heat Shock Response: Life on the Verge of Death
Richter, K., Haslbeck, M., & Büchner, J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.006 · Cited by 2,045 · see citing works
Non-homologous DNA end joining and alternative pathways to double-strand break repair
Chang, H. H. Y., Pannunzio, N. R., Adachi, N., & Lieber, M. R. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.48 · Cited by 1,757 · see citing works
Molecular definitions of autophagy and related processes
Galluzzi, L., Baehrecke, E. H., Ballabio, A., Boya, P., Bravo‐San Pedro, J. M., Cecconi, F., Choi, A. M., Chu, C. T., Codogno, P., Colombo, M. I., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201796697 · Cited by 1,646 · see citing works
The Unfolded Protein Response and Cell Fate Control
Hetz, C. A., & Papa, F. R. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.06.017 · Cited by 1,567 · see citing works
Regulatory T cells in cancer immunosuppression — implications for anticancer therapy
Togashi, Y., Shitara, K., & Nishikawa, H. (2019) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-019-0175-7 · Cited by 1,553 · see citing works
A Human Protein Atlas for Normal and Cancer Tissues Based on Antibody Proteomics
Uhlén, M., Björling, E., Agaton, C., Szigyarto, C. A., Amini, B., Andersen, E., Andersson, A., Angelidou, P., Asplund, A., Asplund, C., et al. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m500279-mcp200 · Cited by 1,543 · see citing works
Endoplasmic reticulum stress signals in the tumour and its microenvironment
Chen, X., & Cubillos-Ruiz, J. R. (2021) · Nature Reviews Cancer · doi:10.1038/s41568-020-00312-2 · Cited by 1,356 · see citing works
Cao, X. (2015) · Nature reviews. Immunology · doi:10.1038/nri.2015.8 · Cited by 661 · see citing works
Ralli, M., Angeletti, D., Fiore, M., D’Aguanno, V., Lambìase, A., Artico, M., VINCENTIIS, M. D., & Greco, A. (2020) · Autoimmunity Reviews · doi:10.1016/j.autrev.2020.102649 · Cited by 655 · see citing works
Conte, M. S., Bandyk, D. F., Clowes, A. W., Moneta, G. L., Seely, L., Lorenz, T. J., Namini, H., Hamdan, A. D., Roddy, S. P., Belkin, M., et al. (2006) · Journal of Vascular Surgery · doi:10.1016/j.jvs.2005.12.058 · Cited by 643 · see citing works
Live to die another way: modes of programmed cell death and the signals emanating from dying cells
Fuchs, Y., & Steller, H. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3999 · Cited by 632 · see citing works
Tang, T., Huang, X., Zhang, G., Hong, Z., Bai, X., & Liang, T. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00449-4 · Cited by 613 · see citing works
Linking cellular stress responses to systemic homeostasis
Galluzzi, L., Yamazaki, T., & Kroemer, G. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0068-0 · Cited by 529 · see citing works
Mitochondrial diseases: the contribution of organelle stress responses to pathology
Suomalainen, A., & Battersby, B. J. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.66 · Cited by 505 · see citing works
Genenames.org: the HGNC and VGNC resources in 2019
Braschi, B., Denny, P., Gray, K. A., Jones, T. E. M., Seal, R. L., Tweedie, S., Yates, B., & Bruford, E. A. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky930 · Cited by 310 · see citing works
Molecular mechanisms driving transcriptional stress responses
Vihervaara, A., Duarte, F. M., & Lis, J. T. (2018) · Nature Reviews Genetics · doi:10.1038/s41576-018-0001-6 · Cited by 273 · see citing works
Cerutti, J. M., Delcelo, R., Amadei, M. J., Nakabashi, C. C. D., Maciel, R. M. B., Peterson, B. L., Shoemaker, J. S., & Riggins, G. J. (2004) · Journal of Clinical Investigation · doi:10.1172/jci19617 · Cited by 183 · see citing works
Functional Proteomics Identifies Targets of Phosphorylation by B-Raf Signaling in Melanoma
Old, W. M., Shabb, J. B., Houel, S., Wang, H., Couts, K. L., Yen, C.-Y., Litman, E. S., Croy, C. H., Meyer-Arendt, K., Miranda, J. G., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.03.007 · Cited by 137 · see citing works
Liu, R., Hu, R., Zeng, Y., Zhang, W., & Zhou, H. (2020) · EBioMedicine · doi:10.1016/j.ebiom.2019.102602 · Cited by 105 · see citing works
Identification of crucial genes in abdominal aortic aneurysm by WGCNA
Chen, S., Yang, D., Lei, C., Li, Y., Sun, X., Chen, M., Wu, X., & Zheng, Y. (2019) · PeerJ · doi:10.7717/peerj.7873 · Cited by 103 · see citing works
Analyzing and validating the prognostic value and mechanism of colon cancer immune microenvironment
Wang, X., Duanmu, J., Fu, X., Li, T., & Jiang, Q. (2020) · Journal of Translational Medicine · doi:10.1186/s12967-020-02491-w · Cited by 89 · see citing works
Miller, S., Rogers, H. A., Lyon, P. C., Rand, V., Adamowicz‐Brice, M., Clifford, S. C., Hayden, J. T., Dyer, S., Pfister, S. M., Korshunov, A., et al. (2011) · Neuro-Oncology · doi:10.1093/neuonc/nor070 · Cited by 79 · see citing works
Boyd, R. S., Adam, P. J., Patel, S., Loader, J., Berry, J. M., Redpath, N., Poyser, H. R., Fletcher, G. C., Burgess, N. A., Stamps, A. C., et al. (2003) · Leukemia · doi:10.1038/sj.leu.2402993 · Cited by 70 · see citing works
Diagnosis of Suspicious Thyroid Nodules Using Four Protein Biomarkers
Cerutti, J. M., Latini, F. R. M., Nakabashi, C. C. D., Delcelo, R., de Andrade, V. P., Amadei, M. J., Maciel, R. M. B., Hojaij, F. C., Hollis, D. R., Shoemaker, J. S., et al. (2006) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-05-2226 · Cited by 68 · see citing works
The Early Effects of Rapid Androgen Deprivation on Human Prostate Cancer
Shaw, G. L., Whitaker, H. C., Corcoran, M., Dunning, M., Luxton, H. J., Kay, J. D., Massie, C. E., Miller, J. L., Lamb, A. D. G., Ross‐Adams, H., et al. (2015) · European Urology · doi:10.1016/j.eururo.2015.10.042 · Cited by 68 · see citing works
Regulation of the unfolded protein response through ATF4 and FAM129A in prostate cancer
Pällmann, N., Livgård, M., Tesikova, M., Nenseth, H. Z., Akkuş, E., Sikkeland, J., Jin, Y., Koç, D., Kuzu, O. F., Pradhan, M., et al. (2019) · Oncogene · doi:10.1038/s41388-019-0879-2 · Cited by 68 · see citing works
Glucocorticoid-induced Changes in Gene Expression of Airway Smooth Muscle in Patients with Asthma
Yick, C. Y., Zwinderman, A. H., Kunst, P. W. A., Grünberg, K., Mauad, T., Fluiter, K., Bel, E. H., Lutter, R., Baas, F., & Sterk, P. J. (2013) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201210-1886oc · Cited by 64 · see citing works
To construct a ceRNA regulatory network as prognostic biomarkers for bladder cancer
Jiang, J., Bi, Y., Liu, X., Yu, D., Yan, X., Yao, J., Liu, T., & Li, S. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.15193 · Cited by 64 · see citing works
Ji, H., Ding, Z., Hawke, D. H., Xing, D., Jiang, B., Mills, G. B., & Lu, Z. (2012) · EMBO Reports · doi:10.1038/embor.2012.53 · Cited by 61 · see citing works
Sun, G. D., Kobayashi, T., Abe, M., Tada, N., Adachi, H., Shiota, A., Totsuka, Y., & Hino, O. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.06.021 · Cited by 55 · see citing works
Membrane and Protein Interactions of the Pleckstrin Homology Domain Superfamily
Lenoir, M., Kufareva, I., Abagyan, R. A., & Overduin, M. (2015) · Membranes · doi:10.3390/membranes5040646 · Cited by 54 · see citing works
Zhu, N., Hou, J., Wu, Y., Liu, J., Li, G., Zhao, W., Ma, G., Chen, B., & Song, Y. (2018) · Medicine · doi:10.1097/md.0000000000011887 · Cited by 51 · see citing works
Gene expression profiling of laser microdissected airway smooth muscle tissue in asthma and atopy
Yick, C. Y., Zwinderman, A. H., Kunst, P. W. A., Grünberg, K., Mauad, T., Chowdhury, S., Bel, E. H., Baas, F., Lutter, R., & Sterk, P. J. (2014) · Allergy · doi:10.1111/all.12452 · Cited by 48 · see citing works
A novel tumor marker, Niban, is expressed in subsets of thyroid tumors and Hashimoto's thyroiditis
Matsumoto, F., Fujii, H., Abe, M., Kajino, K., Kobayashi, T., Matsumoto, T., Ikeda, K., & Hino, O. (2006) · Human Pathology · doi:10.1016/j.humpath.2006.06.022 · Cited by 47 · see citing works
Feng, X., Yan, N., Sun, W., Zheng, S., Jiang, S., Wang, J., Guo, C., Hao, L., Tian, Y., Liu, S., et al. (2019) · Cell Death Discovery · doi:10.1038/s41420-019-0167-5 · Cited by 47 · see citing works
Zhang, R., Xu, K., Shao, Y., Sun, Y., Saredy, J., Cutler, E., Tian, Y., Liu, M., Liu, L., Drummer, C., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2020.632239 · Cited by 44 · see citing works
Comparative proteome analysis of 3T3-L1 adipocyte differentiation using iTRAQ-coupled 2D LC-MS/MS
Feng, Y., Zhang, H., Yang, Y., Hu, H., Sze, S. K., Meng, W., Qian, J., Ren, H., Yang, B., Luo, M., et al. (2011) · Journal of Cellular Biochemistry · doi:10.1002/jcb.23223 · Cited by 43 · see citing works
FAM129B/MINERVA, a Novel Adherens Junction-associated Protein, Suppresses Apoptosis in HeLa Cells
Chen, S., Evans, H. G., & Evans, D. R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.175273 · Cited by 39 · see citing works
Adachi, H., Majima, S., Kon, S., Kobayashi, T., Kajino, K., Mitani, H., Hirayama, Y., Shiina, H., Igawa, M., & Hino, O. (2004) · Oncogene · doi:10.1038/sj.onc.1207468 · Cited by 38 · see citing works
Majima, S., Kajino, K., Fukuda, T., Otsuka, F., & Hino, O. (2000) · Japanese Journal of Cancer Research · doi:10.1111/j.1349-7006.2000.tb01027.x · Cited by 38 · see citing works
The activation of autophagy protects neurons and astrocytes against bilirubin-induced cytotoxicity
Qaisiya, M., Mardešić, P., Pastore, B., Tiribelli, C., & Bellarosa, C. (2017) · Neuroscience Letters · doi:10.1016/j.neulet.2017.09.056 · Cited by 35 · see citing works
Evstafieva, A. G., Kovaleva, I. E., Shoshinova, M. S., Budanov, A. V., & Chumakov, P. M. (2018) · PLoS ONE · doi:10.1371/journal.pone.0191107 · Cited by 35 · see citing works
Yuki, R., Aoyama, K., Kubota, S., Yamaguchi, N., Shoichi, K., Hasegawa, H., Morii, M., Huang, X., Liu, K., Williams, R. M., et al. (2015) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25046 · Cited by 34 · see citing works
FAM129A regulates autophagy in thyroid carcinomas in an oncogene-dependent manner
Nozima, B. H. N., Mendes, T. B., Pereira, G. J. S., Araldi, R. P., Iwamura, E. S. M., Smaili, S. S., Carvalheira, G. M. G., & Cerutti, J. M. (2018) · Endocrine Related Cancer · doi:10.1530/erc-17-0530 · Cited by 33 · see citing works
Self-citationTan, X., Mao, L., Huang, C., Yang, W., Guo, J., Chen, Z., & Chen, Z. (2021) · Bioengineered · doi:10.1080/21655979.2021.1940614 · Cited by 32 · see citing works
Wang, C., Shi, Z., Zhang, Y., Li, M., Zhu, J., Huang, Z. D., Zhang, J., & Chen, J. (2021) · Cell Death and Differentiation · doi:10.1038/s41418-021-00810-2 · Cited by 31 · see citing works
Carvalheira, G. M. G., Nozima, B. H. N., & Cerutti, J. M. (2015) · Oncotarget · doi:10.18632/oncotarget.4947 · Cited by 30 · see citing works
Self-citationHepatic angiomyolipoma and hepatic stellate cells share a similar gene expression profile
Kannangai, R., Diehl, A. M., Sicklick, J. K., Rojkind, M., Thomas, D. L., & Torbenson, M. S. (2005) · Human Pathology · doi:10.1016/j.humpath.2005.01.002 · Cited by 29 · see citing works
Multistep Renal Carcinogenesis in the Eker (Tsc 2 Gene Mutant) Rat Model
Hino, O. (2004) · Current Molecular Medicine · doi:10.2174/1566524043359692 · Cited by 25 · see citing works
Salgado-Albarrán, M., González‐Barrios, R., Guerra-Calderas, L., Alcaraz, N., Sánchez-Correa, T. E., Hernández, C. C., Sánchez-Pérez, Y., Aréchaga-Ocampo, E., García-Carrancá, A. M., de León, D. F. C., et al. (2019) · Oncogenesis · doi:10.1038/s41389-019-0150-2 · Cited by 23 · see citing works
Employing Genetic Markers to Improve Diagnosis of Thyroid Tumor Fine Needle Biopsy
Cerutti, J. M. (2011) · Current Genomics · doi:10.2174/138920211798120781 · Cited by 21 · see citing works
Frequent expression of Niban in head and neck squamous cell carcinoma and squamous dysplasia
Ito, S., Fujii, H., Matsumoto, T., Abe, M., Ikeda, K., & Hino, O. (2009) · Head & Neck · doi:10.1002/hed.21153 · Cited by 21 · see citing works
Luo, W., Feldman, D., McCallister, R., Brophy, C. M., & Cheung‐Flynn, J. (2017) · Purinergic Signalling · doi:10.1007/s11302-017-9585-0 · Cited by 18 · see citing works
Chen, Y., Zhu, S., Pei, Y., Hu, J., Hu, Z., Liu, X., Wang, X., Gu, M., Hu, S., & Liu, X. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.616809 · Cited by 15 · see citing works
Patel, M. R., Stadler, M., Deal, A. M., Kim, H. S., Shores, C. G., & Zanation, A. M. (2011) · The Laryngoscope · doi:10.1002/lary.21736 · Cited by 14 · see citing works
Whole blood mRNA in prostate cancer reveals a four-gene androgen regulated panel
Thomas, B., Kay, J. D., Menon, S., Vowler, S. L., Dawson, S. N., Bucklow, L. J., Luxton, H. J., Johnston, T. J., Massie, C. E., Pugh, M., et al. (2016) · Endocrine Related Cancer · doi:10.1530/erc-16-0287 · Cited by 14 · see citing works
Niban protein regulates apoptosis in HK-2 cells via caspase-dependent pathway
Tang, S., Wang, J., Liu, J., Huang, Y., Zhou, Y., Yang, S., Zhang, W., Yang, M., & Zhang, H. (2019) · Renal Failure · doi:10.1080/0886022x.2019.1619582 · Cited by 14 · see citing works
der Vorst, S. V., Dekairelle, A., Weynand, B., Hamoir, M., & Gala, J. (2011) · Head & Neck · doi:10.1002/hed.21960 · Cited by 13 · see citing works
Wen, C., Zhou, Y., Xu, Y., Tan, H., Pang, C., Liu, H., Liu, K., Wei, L., Luo, H., Qin, T., et al. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.706768 · Cited by 13 · see citing works
Expression of N iban in renal interstitial fibrosis
Liu, J., Qin, J., Mei, W., Zhang, H., Yuan, Q., Peng, Z., Luo, R., Yuan, X., Huang, L., & Tao, L. (2014) · Nephrology · doi:10.1111/nep.12266 · Cited by 12 · see citing works
Zhang, K.-K., Yu, S., Li, G., He, L., & Liang, X. (2019) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-019-02329-5 · Cited by 12 · see citing works
Pathogenesis of differentiated thyroid cancer (papillary and follicular)
Maciel, R. M. B., Kimura, E. T., & Cerutti, J. M. (2005) · Arquivos Brasileiros de Endocrinologia & Metabologia · doi:10.1590/s0004-27302005000500009 · Cited by 11 · see citing works
Zhang, N., Zhou, X., Yang, F., Zhang, Q., Miao, Y., & Hou, G. (2019) · Europe PMC (PubMed Central) · Cited by 10 · see citing works
Yim, T. W., Perling, D., Polcz, M. E., Komalavilas, P., Brophy, C. M., & Cheung‐Flynn, J. (2020) · The FASEB Journal · doi:10.1096/fj.201902745r · Cited by 9 · see citing works
Carvalheira, G. M. G., Nozima, B. H. N., Riggins, G. J., & Cerutti, J. M. (2013) · Modern Pathology · doi:10.1038/modpathol.2012.212 · Cited by 7 · see citing works
Self-citationAlterations in niban gene expression as a response to stress conditions in 3T3-L1 adipocytes
Çevik, M., Gündüz, M. K., Deliorman, G., & Duman, B. S. (2020) · Molecular Biology Reports · doi:10.1007/s11033-020-05992-5 · Cited by 5 · see citing works
Flagged first, then by citations
1 of the 73 references couldn’t be matched to a known paper.
Cited by
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Fancy, N. N., Smith, A. M., Caramello, A., Tsartsalis, S., Davey, K., Muirhead, R. C. J., McGarry, A., Jenkyns, M. H., Schneegans, E., Chau, V., et al. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02727-9 · Cited by 48 · see citing works
“Genes for negative regulators of senescence such as GRB2 and NIBAN1 were downregulated with increasing β-amyloid [17, 21, 34, 55].”
BackgroundSpace radiation damage rescued by inhibition of key spaceflight associated miRNAs
McDonald, J. T., Kim, J., Farmerie, L., Johnson, M. L., Trovão, N. S., Arif, S., Siew, K., Tsoy, S., Bram, Y., Park, J., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-48920-y · Cited by 30 · see citing works
Running, L. S., Cristobal, J. R., Karageorgiou, C., Camdzic, M., Aguilar, J. M. N., Gökçümen, Ö., Aga, D. S., & Atilla‐Gokcumen, G. E. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00652 · Cited by 25 · see citing works
Zhuang, D., Wang, S., Deng, H., Shi, Y., Liu, C. X., Leng, X., Zhang, Q., Bai, F., Zheng, B., Guo, J., et al. (2024) · International Journal of Oral Science · doi:10.1038/s41368-024-00297-w · Cited by 18 · see citing works
Alehashem, M. S., Alcaraz, A. J., Hogan, N., Weber, L. P., Siciliano, S. D., & Hecker, M. (2024) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2024.173041 · Cited by 10 · see citing works
Perfluorooctanoic acid inhibits cell proliferation through mitochondrial damage
Park, E., Li, K., Kang, M.-S., Choi, J.-W., Baek, B., Yang, Y.-K., Cho, A. E., & Lee, B. (2024) · Toxicology in Vitro · doi:10.1016/j.tiv.2024.105810 · Cited by 8 · see citing works
Age‐Associated Dysregulation of Postsynaptic Mitochondria Perturbs Reinnervation Kinetics
Guzman, S. D., Fraczek, P. M., Itsani, K., Furati, E., Juros, D., Kenney, G., Valdez, G., Chakkalakal, J. V., & Aguilar, C. A. (2026) · Aging Cell · doi:10.1111/acel.70355 · Cited by 10 · see citing works
Miao, X., Yue, W., Wang, J., Chen, J., Qiu, L., Paerhati, H., Zhou, Q., Li, P., Wu, A., & Zhang, M. (2025) · Current Neuropharmacology · doi:10.2174/011570159x417328250908080404 · Cited by 6 · see citing works
NR5A1/SF-1 Collaborates with Inhibin α and the Androgen Receptor
Elzenaty, R. N., Kouri, C., de la Piscina, I. M., Sauter, K., Moreno, F., Camats, N., & Flück, C. E. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms251810109 · Cited by 4 · see citing works
Papadatou, I., Geropeppa, M., Verrou, K., Tzanoudaki, M., Lagousi, T., Liatsis, E., & Spoulou, V. I. (2023) · Vaccines · doi:10.3390/vaccines11010103 · Cited by 4 · see citing works
Glass, J., Robinson, R. L., Edupuganti, N., Altman, J., Greenway, G., Lee, T. J., Zhi, W., Sharma, A. K., & Sharma, S. (2024) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.65.14.33 · Cited by 3 · see citing works
An exploration of molecular signaling in drug reprocessing for Oral Squamous Cell Carcinoma
Nakhaei, A., Marzoughi, S., Ghoflchi, S., Hosseini, H., Afshari, A. R., Jalili‐Nik, M., Kesharwani, P., & Sahebkar, A. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.117816 · Cited by 3 · see citing works
Giri, A. K., Lin, J., Kyriakidis, K., Tripathi, G., & Almusa, H. (2025) · BMC Medical Genomics · doi:10.1186/s12920-025-02130-7 · Cited by 3 · see citing works
Iuchi, S., & Paulo, J. A. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.13.638155 · Cited by 3 · see citing works
Diana, P., Carneiro, T. N. R., Cerutti, J. M., Kuroshu, R. M., & Carvalheira, G. M. G. (2023) · Genes & Diseases · doi:10.1016/j.gendis.2023.101094 · Cited by 2 · see citing works
Self-citationBui, L. T., Cao, X., Wang, J., Meng, F., Feng, M., Arvanitis, L. D., Mannan, R., Woo, Y., Idrees, K., Banovich, N. E., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.09.28.559817 · Cited by 2 · see citing works
Huang, W., Xu, Y., Liu, J., Cheng, T., & Tang, C. (2025) · Scientific Reports · doi:10.1038/s41598-025-10413-3 · Cited by 1 · see citing works
Lucibello, G., Ursino, G., Teixeira, P. D. S., Zahorán, S., Fanuele, F., Kallikourdis, M., Visentin, F., Veyrat‐Durebex, C., Widmer, A., Wu, Y., et al. (2025) · Endocrinology · doi:10.1210/endocr/bqaf131 · Cited by 1 · see citing works
Peng, W., Xie, Y., Xia, J., Qi, H., Liu, K., Li, B., Zhang, F., Wen, F., & Zhang, L. (2023) · Heliyon · doi:10.1016/j.heliyon.2023.e22466 · Cited by 1 · see citing works
Running, L. S., Cristobal, J. R., Karageorgiou, C., Camdzic, M., Aguilar, J. M. N., Gökçümen, Ö., Aga, D. S., & Atilla‐Gokcumen, G. E. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.01.26.577438 · Cited by 1 · see citing works
Mosavie, M., Rynne, J., Fish, M., Smith, P., Jennings, A., Singh, S., Millar, J. E., Harvala, H., Mora, A., Kaloyirou, F., et al. (2024) · Vaccines · doi:10.3390/vaccines12091040
Abotaleb, A., Le, N. P. K., Tucci, S., Hug, M. J., Lamy, E., & Günther, S. (2025) · Research Square · doi:10.21203/rs.3.rs-7327879/v1
Endothelial dysfunction in aging associated with reduced Niban phosphorylation
Baer, B., Morelli, M., Brophy, C. M., Bastarache, J. A., & Cheung‐Flynn, J. (2026) · Molecular Biology Reports · doi:10.1007/s11033-026-11504-8
Mitigating sepsis-induced vascular endothelial dysfunction through Niban phosphorylation
Baer, B., Morelli, M., Wadzinski, B. E., Katta, A. R., Sisung, A., Brophy, C. M., Bastarache, J. A., & Cheung‐Flynn, J. (2026) · Vascular Medicine · doi:10.1177/1358863x251412772
Chwiałkowska, K., Niemira, M., Zeller, A., Ostrowska, A., Michalska‐Falkowska, A., Reszeć-Giełażyn, J., Kozłowski, M., Mróz, R. M., Naumnik, W., Sierko, E., et al. (2026) · Journal of Translational Medicine · doi:10.1186/s12967-026-07957-x
BPTF is essential for vaccine-induced germinal center B cell responses
Sturtz, A. J., Evavold, B. K., Rarani, Z. H., Alsoussi, W. B., Zhou, J. Q., Matz, H. C., Muramatsu, H., Simkins, W., Malladi, S. K., McIntire, K. M., et al. (2026) · The Journal of Immunology · doi:10.1093/jimmun/vkag126
- Authors
- Diana, P., & Carvalheira, G. M. G.
- Affiliations
- Universidade Federal de São Paulo (BR)
- Corresponding author
- Carvalheira, Gianna Maria Griz
- Venue
- Frontiers in Cell and Developmental Biology
- Publisher
- Frontiers Media SA
- Published
- 2022-04-19
- Volume
- 10
- Pages
- 867003-867003
- ISSN
- 2296-634X (ISSN-L)
- PMC
- PMC9062034
- OpenAlex
- W4224298154
- Cited by
- 26
- References
- 73
- Citations by year
- 2026: 5 · 2025: 7 · 2024: 10 · 2023: 4
- FWCI
- 0.55
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Frontiers in Cell and Developmental Biology (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (88882.430337/2019-01)
- Fundação de Amparo à Pesquisa do Estado de São Paulo (2015/04164-3)
- Conselho Nacional de Desenvolvimento Científico e Tecnológico (470441/2013-5)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- cell survival, cellular stress, cellular homeostasis, cell death, stress response, gene expression regulation
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