The FEBS journal最新文献

Activating AMPK improves pathological phenotypes due to mtDNA depletion.

The FEBS journal Pub Date : 2025-02-07 DOI: 10.1111/febs.70006

Gustavo Carvalho, Tran V H Nguyen, Bruno Repolês, Josefin M E Forslund, W M Ruchitha Rukmal Wijethunga, Farahnaz Ranjbarian, Isabela C Mendes, Choco Michael Gorospe, Namrata Chaudhari, Micol Falabella, Mara Doimo, Sjoerd Wanrooij, Robert D S Pitceathly, Anders Hofer, Paulina H Wanrooij

{"title":"Activating AMPK improves pathological phenotypes due to mtDNA depletion.","authors":"Gustavo Carvalho, Tran V H Nguyen, Bruno Repolês, Josefin M E Forslund, W M Ruchitha Rukmal Wijethunga, Farahnaz Ranjbarian, Isabela C Mendes, Choco Michael Gorospe, Namrata Chaudhari, Micol Falabella, Mara Doimo, Sjoerd Wanrooij, Robert D S Pitceathly, Anders Hofer, Paulina H Wanrooij","doi":"10.1111/febs.70006","DOIUrl":"https://doi.org/10.1111/febs.70006","url":null,"abstract":"AMP-activated protein kinase (AMPK) is a master regulator of cellular energy homeostasis that also plays a role in preserving mitochondrial function and integrity. Upon a disturbance in the cellular energy state that increases AMP levels, AMPK activity promotes a switch from anabolic to catabolic metabolism to restore energy homeostasis. However, the level of severity of mitochondrial dysfunction required to trigger AMPK activation is currently unclear, as is whether stimulation of AMPK using specific agonists can improve the cellular phenotype following mitochondrial dysfunction. Using a cellular model of mitochondrial disease characterized by progressive mitochondrial DNA (mtDNA) depletion and deteriorating mitochondrial metabolism, we show that mitochondria-associated AMPK becomes activated early in the course of the advancing mitochondrial dysfunction, before any quantifiable decrease in the ATP/(AMP + ADP) ratio or respiratory chain activity. Moreover, stimulation of AMPK activity using the specific small-molecule agonist A-769662 alleviated the mitochondrial phenotypes caused by the mtDNA depletion and restored normal mitochondrial membrane potential. Notably, the agonist treatment was able to partially restore mtDNA levels in cells with severe mtDNA depletion, while it had no impact on mtDNA levels of control cells. The beneficial impact of the agonist on mitochondrial membrane potential was also observed in cells from patients suffering from mtDNA depletion. These findings improve our understanding of the effects of specific small-molecule activators of AMPK on mitochondrial and cellular function and suggest a potential application for these compounds in disease states involving mtDNA depletion.","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-02-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143367215","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Structural analysis of the ribosome assembly factor Nep1, an N1-specific pseudouridine methyltransferase, reveals mechanistic insights.

The FEBS journal Pub Date : 2025-02-07 DOI: 10.1111/febs.70005

Sayan Saha, Shankar Prasad Kanaujia

{"title":"Structural analysis of the ribosome assembly factor Nep1, an N1-specific pseudouridine methyltransferase, reveals mechanistic insights.","authors":"Sayan Saha, Shankar Prasad Kanaujia","doi":"10.1111/febs.70005","DOIUrl":"https://doi.org/10.1111/febs.70005","url":null,"abstract":"Nucleolar essential protein 1 (Nep1; also known as ribosomal RNA small subunit methyltransferase Nep1) is a crucial factor in forming small ribosomal subunits in eukaryotes and archaea. Nep1 possesses an S-adenosyl-L-methionine (SAM)-dependent SpoU-TrmD (SPOUT) ribosomal RNA (rRNA) methyltransferase (MTase) fold and catalyzes pseudouridine (Ψ) methylation at specific sites of the small subunit (SSU) rRNA. Mutations in Nep1 proteins result in a severe developmental disorder in humans and reduced growth in yeast, suggesting its role in ribosome biogenesis. In this study, the crystal structures of Nep1 from the archaebacterium Pyrococcus horikoshii (PhNep1), both in its apo and holo (adenosine or 5-methylthioadenosine bound) forms have been reported. The structural analysis of PhNep1 revealed an α/β fold featuring a deep trefoil knot akin to the SPOUT domain, with two novel extensions-a globular loop and a β-α-β extension. Moreover, the cofactor-binding site of PhNep1 exhibits a preformed pocket, topologically similar to that of other SPOUT-class MTases. Further, structural analysis of PhNep1 revealed that it forms a homodimer coordinated by inter-subunit hydrogen bonds and hydrophobic interactions. Moreover, the results of this study indicate that PhNep1 can specifically methylate consensus RNAs, having a pseudouridine (ψ) located at position 926 of helix 35 (h35) of 16S rRNA in P. horikoshii. The stability of the Nep1-RNA complex seems to be primarily assisted by the conserved arginine residues located at the dimeric interface.","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-02-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143367217","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Shifting the substrate scope of dimeric pyranose oxidase from monosaccharide to glycoside preference through oligomeric state modification.

The FEBS journal Pub Date : 2025-02-06 DOI: 10.1111/febs.70004

Anja Kostelac, Enikő Hermann, Clemens Peterbauer, Chris Oostenbrink, Dietmar Haltrich

{"title":"Shifting the substrate scope of dimeric pyranose oxidase from monosaccharide to glycoside preference through oligomeric state modification.","authors":"Anja Kostelac, Enikő Hermann, Clemens Peterbauer, Chris Oostenbrink, Dietmar Haltrich","doi":"10.1111/febs.70004","DOIUrl":"https://doi.org/10.1111/febs.70004","url":null,"abstract":"Pyranose oxidase (POx) and C-glycoside oxidase (CGOx) are FAD-dependent oxidoreductases belonging to the glucose-methanol-choline oxidoreductase superfamily and share the same sequence space. Despite a shared structural fold, these two members possess homologous domains that enable (arm and head domain) or disable (insertion-1 domain and barrel-shaped bottom) oligomerization. POxs with a higher oligomerization state (dimeric or tetrameric) exclusively catalyze the oxidation of monosaccharides (d-glucose, d-xylose). In contrast, the monomeric state of POxs/CGOxs is observed to prefer glycosides (homoorientin, phlorizin) and has low activity with free monosaccharides. We aimed to engineer dimeric POx from Kitasatospora aureofaciens (KaPOx) to form a functional monomer, and monomeric POx/CGOx from Streptomyces canus (ScPOx) to a dimeric structure. Deletion of the head and arm domains of the KaPOx subunit resulted in enzyme variants with a less hydrophobic surface, thus affecting its oligomerization. These monomeric KaPOx variants KaPOx_xal and KaPOx_xalh resembled monomeric wild-type POxs/CGOxs and preferred glycosides as substrates over monosaccharides with catalytic efficiencies for phlorizin being 24 × 106 higher compared to those for d-xylose. The wild-type dimeric KaPOx showed no activity towards glycosides. We hypothesize that KaPOx_xalh is unable to react with monosaccharides because the introduced mutations alter the positions of monosaccharide-binding residues. The inability of KaPOx to react with glycosides is likely caused by steric hindrance and the inaccessibility of the active site to bulky glycosides due to dimerization. The attempt to engineer ScPOx into a dimeric structure failed at the stage of soluble expression, likely due to exposed hydrophobic patches and aggregation.","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-02-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143367216","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

RING dimerisation drives higher-order organisation of SINA/SIAH E3 ubiquitin ligases.

The FEBS journal Pub Date : 2025-02-05 DOI: 10.1111/febs.70000

Franck Coste, Aanchal Mishra, Catherine Chapuis, Lucija Mance, Zofia Pukało, Nicolas Bigot, Stéphane Goffinont, Virginie Gaudon, Norbert Garnier, Ibtissam Talhaoui, Bertrand Castaing, Sebastien Huet, Marcin J Suskiewicz

{"title":"RING dimerisation drives higher-order organisation of SINA/SIAH E3 ubiquitin ligases.","authors":"Franck Coste, Aanchal Mishra, Catherine Chapuis, Lucija Mance, Zofia Pukało, Nicolas Bigot, Stéphane Goffinont, Virginie Gaudon, Norbert Garnier, Ibtissam Talhaoui, Bertrand Castaing, Sebastien Huet, Marcin J Suskiewicz","doi":"10.1111/febs.70000","DOIUrl":"https://doi.org/10.1111/febs.70000","url":null,"abstract":"RING-type E3 ubiquitin ligases promote ubiquitylation by stabilising an active complex between a ubiquitin-loaded E2-conjugating enzyme and a protein substrate. To fulfil this function, the E3 ubiquitin-protein ligase SIAH1 and other SINA/SIAH subfamily RING-type E3 ligases employ an N-terminal catalytic RING domain and a C-terminal substrate-binding domain (SBD), separated by two zinc fingers. Here, we present the first crystal structure of the RING domain of human SIAH1, together with an adjacent zinc finger, revealing a potential RING dimer, which was validated in solution using static light scattering. RING dimerisation contributes to the E3 ligase activity of SIAH1 both in vitro and in cells. Moreover, as the RING domain is the second element, after the SBD, to independently favour homodimerisation within SINA/SIAH E3 ligases, we propose that alternating RING:RING and SBD:SBD interactions organise multiple copies of a SINA/SIAH protein into a higher-order homomultimer. In line with this hypothesis, fluorescently tagged full-length human SIAH1, human SIAH2 and fruit fly SINA show cytoplasmic clusters in human cells, whereas their distribution becomes more diffuse when RING dimerisation is disabled. The wild-type (WT) form of SIAH1, but not its RING dimerisation mutant, colocalises with aggregated synphilin-1A under proteasomal inhibition, suggesting that SIAH1 multimerisation might contribute to its reported preference for aggregated or multimeric substrates.","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-02-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143257669","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Contact and communication: ZO-2 and the Hippo pathway.

The FEBS journal Pub Date : 2025-02-05 DOI: 10.1111/febs.17417

Miranda Thomas

引用次数: 0

CryoEM and crystal structure analyses reveal the indirect role played by Trp89 in glutamate dehydrogenase enzymatic reactions.

The FEBS journal Pub Date : 2025-02-01 DOI: 10.1111/febs.17415

Taiki Wakabayashi, Yuka Matsui, Masayoshi Nakasako

{"title":"CryoEM and crystal structure analyses reveal the indirect role played by Trp89 in glutamate dehydrogenase enzymatic reactions.","authors":"Taiki Wakabayashi, Yuka Matsui, Masayoshi Nakasako","doi":"10.1111/febs.17415","DOIUrl":"https://doi.org/10.1111/febs.17415","url":null,"abstract":"Glutamate dehydrogenase from Thermococcus profundus is a homo-hexameric enzyme that catalyzes the reversible deamination of glutamate to 2-oxoglutarate in the presence of a cofactor. In each subunit, a large active-site cleft is formed between the two functional domains, one of which displays motion to open and close the cleft. Trp89 in the cleft displays two sidechain conformers in the open cleft and a single conformer in the closed cleft. To reveal the role of the Trp89 sidechain in the domain motion, we mutated Trp89 to phenylalanine. Despite the Trp89 sidechain being located away from the reaction center, the catalytic constant decreased to 1/38-fold of that of the wild-type without a fatal reduction of the affinities to the cofactor and ligand molecules. To understand the molecular mechanism underlying this reduction, we determined the crystal structure in the unliganded state and the metastable conformations appearing in the steady stage of the reaction using cryo-electron microscopy (cryoEM). The four identified metastable conformations were similar to the three conformations observed in the wild-type, but their populations were different from those of the wild-type. In addition, a conformation with a completely closed active-site cleft necessary for the reaction to proceed was quite rare. The crystal structure and the four metastable conformations suggested that the reduction in the catalytic constant could be attributed to changes in the interactions between Gln13 and the 89th side chains, preventing the closing domain motion.","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143076749","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Nature AND nurture: enabling formate-dependent growth in Methanosarcina acetivorans.

The FEBS journal Pub Date : 2025-01-31 DOI: 10.1111/febs.17409

Jichen Bao, Tejas Somvanshi, Yufang Tian, Maxime G Laird, Pierre Simon Garcia, Christian Schöne, Michael Rother, Guillaume Borrel, Silvan Scheller

{"title":"Nature AND nurture: enabling formate-dependent growth in Methanosarcina acetivorans.","authors":"Jichen Bao, Tejas Somvanshi, Yufang Tian, Maxime G Laird, Pierre Simon Garcia, Christian Schöne, Michael Rother, Guillaume Borrel, Silvan Scheller","doi":"10.1111/febs.17409","DOIUrl":"https://doi.org/10.1111/febs.17409","url":null,"abstract":"Methanosarcinales are versatile methanogens, capable of regulating most types of methanogenic pathways. Despite the versatile metabolic flexibility of Methanosarcinales, no member of this order has been shown to use formate for methanogenesis. In the present study, we identified a cytosolic formate dehydrogenase (FdhAB) present in several Methanosarcinales, likely acquired by independent horizontal gene transfers after an early evolutionary loss, encouraging re-evaluation of our understanding of formate utilization in Methanosarcinales. To explore whether formate-dependent (methyl-reducing or CO2-reducing) methanogenesis can occur in Methanosarcinales, we engineered two different strains of Methanosarcina acetivorans by functionally expressing FdhAB from Methanosarcina barkeri in M. acetivorans. In the first strain, fdhAB was integrated into the N5-methyl- tetrahydrosarcinapterin:coenzyme M methyltransferase (mtr) operon, making it capable of growing by reducing methanol with electrons from formate. In the second strain, fdhAB was integrated into the F420-reducing hydrogenase (frh) operon, instead of the mtr operon, enabling its growth with formate as the only source of carbon and energy after adaptive laboratory evolution. In this strain, one CO2 is reduced to one methane with electrons from oxidizing four formate to four CO2, a metabolism reported only in methanogens without cytochromes. Although methanogens without cytochromes typically utilize flavin-based electron bifurcation to generate the ferredoxins needed for CO2 activation, we hypothesize that, in our engineered strains, reduced ferredoxins are obtained via the Rhodobacter nitrogen fixation complex complex running in reverse. Our work demonstrates formate-dependent methyl-reducing and CO2-reducing methanogenesis in M. acetivorans that is enabled by the flexible nature of the microbe working in tandem with the nurturing provided.","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-01-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143070588","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Sex-related changes in lactate dehydrogenase A expression differently impact the immune response in melanoma.

The FEBS journal Pub Date : 2025-01-31 DOI: 10.1111/febs.17423

Marta Iozzo, Giuseppina Comito, Luigi Ippolito, Giada Sandrini, Elisa Pardella, Erica Pranzini, Mariaelena Capone, Gabriele Madonna, Paolo Antonio Ascierto, Paola Chiarugi, Elisa Giannoni

{"title":"Sex-related changes in lactate dehydrogenase A expression differently impact the immune response in melanoma.","authors":"Marta Iozzo, Giuseppina Comito, Luigi Ippolito, Giada Sandrini, Elisa Pardella, Erica Pranzini, Mariaelena Capone, Gabriele Madonna, Paolo Antonio Ascierto, Paola Chiarugi, Elisa Giannoni","doi":"10.1111/febs.17423","DOIUrl":"https://doi.org/10.1111/febs.17423","url":null,"abstract":"Melanoma is more aggressive in male patients than female ones and this is associated with sexual dimorphism in immune responses. Taking into consideration the impact tumour metabolic alterations in affecting the immune landscape, we aimed to investigate the effect of the sex-dependent metabolic profile of melanoma in re-shaping immune composition. Melanoma is characterised by Warburg metabolism, and secreted lactate has emerged as a key driver in the establishment of an immunosuppressive environment. Here, we identified lactate dehydrogenase A (LDH-A) as a crucial player in modulating sex-related differences in melanoma immune responses, both in vitro and in patient-derived specimens. LDH-A is associated with higher lactate secretion in male melanoma cells, which leads to a significant enrichment in pro-tumoural regulatory T cells (Treg) with a concurrent decrease in the number and activity of anti-tumour CD8+ T cells. Remarkably, pharmacological and genetic impairment of LDH-A in male melanoma cells normalises Treg and CD8+ infiltration. In keeping with this, in vivo pharmacological targeting of LDH-A in melanoma-bearing male mice impairs tumour growth and lung colonisation, with a concomitant modulation of Treg and CD8+ T cells infiltration. Taken together, our findings highlight the sex-related differences promoted by LDH-A in immune reshaping in melanoma, and suggest that therapeutic targeting of LDH-A could be leveraged as an effective strategy to abolish the sex-gap in melanoma progression.","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-01-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143070591","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

A cellular model of TDP-43 induces phosphorylated TDP-43 aggregation with distinct changes in solubility and autophagy dysregulation.

The FEBS journal Pub Date : 2025-01-31 DOI: 10.1111/febs.17413

Matthew B Dopler, Muhammad I Abeer, Sanaz Arezoumandan, Keyshawn Cox, Tyler L Petersen, Esther H Daniel, Carlton L Cannon, Angelica Bautista, Kennedy D Blancher, Alysia M Bland, Kylie J Bond, Dominque A Davis, Jessica M Francois, Eliana J McCray, Justin M Morgan, Jessica L Pulliam, Zymir A Robinson, Mykia J Taylor, James A Dowell, Nigel J Cairns, Michael A Gitcho

{"title":"A cellular model of TDP-43 induces phosphorylated TDP-43 aggregation with distinct changes in solubility and autophagy dysregulation.","authors":"Matthew B Dopler, Muhammad I Abeer, Sanaz Arezoumandan, Keyshawn Cox, Tyler L Petersen, Esther H Daniel, Carlton L Cannon, Angelica Bautista, Kennedy D Blancher, Alysia M Bland, Kylie J Bond, Dominque A Davis, Jessica M Francois, Eliana J McCray, Justin M Morgan, Jessica L Pulliam, Zymir A Robinson, Mykia J Taylor, James A Dowell, Nigel J Cairns, Michael A Gitcho","doi":"10.1111/febs.17413","DOIUrl":"https://doi.org/10.1111/febs.17413","url":null,"abstract":"Amyotrophic lateral sclerosis (ALS) is an incurable neurodegenerative disease that affects neurons in the brain and spinal cord, causing loss of muscle control, and eventually leads to death. Phosphorylated transactive response DNA binding protein-43 (TDP-43) is the major pathological protein in both sporadic and familial ALS, forming cytoplasmic aggregates in over 95% of cases. Of the 10-15% of ALS cases that are familial, mutations in TDP-43 represent about 5% of those with a family history. We have developed an in vitro overexpression model by introducing three familial ALS mutations (A315T, M337V, and S379P) in the TDP-43 (TARDBP) gene which we define as 3X-TDP-43. This overexpression model TDP-43 shows deficits in autophagy flux and colocalization of TDP-43 with stress granules. We also observe a progressive shift of TDP-43 to the cytoplasm in this model. This overexpression model shows a reduction in solubility of phosphorylated TDP-43 from RIPA to urea soluble. Four glycolytic enzymes, phosphoglycerate kinase one (PGK1), aldolase A (ALDOA), enolase 1 (ENO1), and pyruvate dehydrogenase kinase 1 (PDK1) show significant time-dependent decreases in 3X-TDP-43 expressing cells. Shotgun proteomic analysis shows global changes in the importin subunit alpha-1 (KPNA2), heat shock 70 kDa protein 1A (HSPA1A), and protein disulfide-isomerase A3 (PDIA3) expression levels and coimmunoprecipitation reveals that these proteins complex with TDP-43. Overall, these results suggest that the 3X-TDP-43 model may provide new insights into pathophysiology and an avenue for drug screening in vitro for those suffering from ALS and related TDP-43 proteinopathies.","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-01-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143070583","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Words of advice for young scientists in developing countries.

The FEBS journal Pub Date : 2025-01-31 DOI: 10.1111/febs.17425

Max Chavarría

{"title":"Words of advice for young scientists in developing countries.","authors":"Max Chavarría","doi":"10.1111/febs.17425","DOIUrl":"https://doi.org/10.1111/febs.17425","url":null,"abstract":"As scientists, change is the only constant in our journey. We often find ourselves in transition from one laboratory to another, and during our training we are fortunate to experience the excitement of pursuing postgraduate studies abroad in well-funded, high-level research centers. However, after completing doctoral or postdoctoral training, we are frequently drawn to return to our home countries, where funding and support for science are significantly more limited. In this brief commentary, first, I would like to highlight the challenges faced by scientists from developing countries who have had the opportunity to train internationally and then choose to return home, driven both by personal motivations (e.g., family) and by the desire to contribute to the scientific advancement of their regions. Second, I would like to share some advice that has been especially useful to me in establishing my laboratory, defining research topics, and maintaining academic productivity. I hope these insights can be useful to colleagues in similar situations across different regions. Although starting a research group in regions with less investment in Research and Development is challenging, it is achievable with perseverance and the implementation of concrete actions.","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-01-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143069576","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0