Auswahl der wissenschaftlichen Literatur zum Thema „Mitofusins“
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Zeitschriftenartikel zum Thema "Mitofusins":
Cohen, Mickael M., und David Tareste. „Recent insights into the structure and function of Mitofusins in mitochondrial fusion“. F1000Research 7 (28.12.2018): 1983. http://dx.doi.org/10.12688/f1000research.16629.1.
Wolf, Christina, Víctor López del Amo, Sabine Arndt, Diones Bueno, Stefan Tenzer, Eva-Maria Hanschmann, Carsten Berndt und Axel Methner. „Redox Modifications of Proteins of the Mitochondrial Fusion and Fission Machinery“. Cells 9, Nr. 4 (27.03.2020): 815. http://dx.doi.org/10.3390/cells9040815.
LeBrasseur, Nicole. „Pro-diversity mitofusins“. Journal of Cell Biology 176, Nr. 4 (12.02.2007): 373a. http://dx.doi.org/10.1083/jcb.1764iti3.
Schiavon, Cara R., Rachel E. Turn, Laura E. Newman und Richard A. Kahn. „ELMOD2 regulates mitochondrial fusion in a mitofusin-dependent manner, downstream of ARL2“. Molecular Biology of the Cell 30, Nr. 10 (Mai 2019): 1198–213. http://dx.doi.org/10.1091/mbc.e18-12-0804.
Koch, Linda. „Mitofusins and energy balance“. Nature Reviews Endocrinology 9, Nr. 12 (15.10.2013): 691. http://dx.doi.org/10.1038/nrendo.2013.202.
Escobar-Henriques, Mafalda. „Mitofusins: ubiquitylation promotes fusion“. Cell Research 24, Nr. 4 (21.02.2014): 387–88. http://dx.doi.org/10.1038/cr.2014.23.
Miao, Junru, Wei Chen, Pengxiang Wang, Xin Zhang, Lei Wang, Shuai Wang und Yuan Wang. „MFN1 and MFN2 Are Dispensable for Sperm Development and Functions in Mice“. International Journal of Molecular Sciences 22, Nr. 24 (16.12.2021): 13507. http://dx.doi.org/10.3390/ijms222413507.
Sloat, S. R., B. N. Whitley, E. A. Engelhart und S. Hoppins. „Identification of a mitofusin specificity region that confers unique activities to Mfn1 and Mfn2“. Molecular Biology of the Cell 30, Nr. 17 (August 2019): 2309–19. http://dx.doi.org/10.1091/mbc.e19-05-0291.
Alsayyah, Cynthia, Manish K. Singh, Maria Angeles Morcillo-Parra, Laetitia Cavellini, Nadav Shai, Christine Schmitt, Maya Schuldiner et al. „Mitofusin-mediated contacts between mitochondria and peroxisomes regulate mitochondrial fusion“. PLOS Biology 22, Nr. 4 (26.04.2024): e3002602. http://dx.doi.org/10.1371/journal.pbio.3002602.
R. Khalil, Rana, Mufeda AL-Ammar und Hayder A. L. Mossa. „Mitofusin 1 as Marker of Oocyte Maturation in Relevance to ICSI Outcome in Infertile Females“. IraQi Journal of Embryos and Infertility Researches 13, Nr. 2 (08.11.2023): 39–50. http://dx.doi.org/10.28969/ijeir.v13.i2.r4.23.
Dissertationen zum Thema "Mitofusins":
Versini, Raphaëlle. „Structural basis of outer-mitochondrial membrane mitofusin-guided fusion“. Electronic Thesis or Diss., Sorbonne université, 2023. https://accesdistant.sorbonne-universite.fr/login?url=https://theses-intra.sorbonne-universite.fr/2023SORUS653.pdf.
The Phd project is the structural study of mitofusins (Mfn1/2 in humans and Fzo1 in yeasts) using mainly modeling-based methods such as molecular dynamics or structure prediction methods based on artificial intelligence (mainly AlphaFold). This project is a part of an ANR (MITOFUSION) shared between different partners (Laboratoire de Biochimie Théorique: Antoine Taly, Marc Baaden, Laboratoire des Biomolécules: Patrick Fuchs, Laboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes: Mickaël Cohen, Institut de Psychiatrie et Neurosciences de Paris: David Tareste) whose goal is to understand the structure-function relationships of the mitofusin. Mitochondria form a complex network inside the cells, undergoing continuous fusion and fission events. These processes shape mitochondrial dynamics and are essential for the maintenance, function, distribution and inheritance of mitochondria. The morphology of the latter therefore respond to the ever-changing physiological changes of the cell. The large GTPase involved in the tethering and fusion of the mitochondrial outer membranes (OM) are transmembrane proteins called mitofusins. The mitofusins Mfn1 and Mfn2 can be found in mammals. Fzo1 (Fuzzy Onion 1) is the unique mitofusin homologue in Saccharomyces cerevisiae. The mitochondrial inner membrane fusion and cristea organisation is mediated by human OPA1 (Optic Atrophy 1) and yeast Mgm1 (Mitochondrial Genome Maintenance 1). Mitochondrial fusion dysfonction is related to several neurodegenerative disorders, such as Parkinson, Alzheimer and Huntingtion diseases. As a matter of fact, research has shown that mutations in Mfn2 induce the development and progression of muscular dystrophies, such as Charcot-Marie-Tooth Type 2A, the most common form of axonal CMT disease. The exact mechanism by which the mitofusins contributes to mitochondria dysfunction as well as the exact molecular fusion mechanism is not fully understood yet. Overall, mitochondrial fusion plays an important role in CMT2A, it is thus of paramount importance to get a full understanding of the process at the molecular level. The structure of both Mfn1 and Mfn2 was partially solved, the transmembrane domain being excluded, and no solved structure are available for Fzo1. With our ANR partners, we decided to work on the yeast version of Mitofusin (named Fzo1) as it is a good model (of homology with human Mfn1 and Mfn2) as yeast are convenient hosts for testing how other protein partners are involved in the process (e.g. Ugo1). Fzo1 is embedded in the mitochondrial OM as it possesses two transmembrane domains, exposing N- and C- terminal portions towards the cytosol and a loop towards the intermembrane space. On the N-terminal side can be found two coiled-coil heptad repeats (HRs) domains, HRN (in yeast only) and HR1, flanking a GTPase domain. A third coiled-coil heptad repeats domain HR2 is on the C-terminal portion. Some models of Fzo1 were built based on the mitofusin related bacterial dynamin-like protein (BDLP). BDLP is involved in membrane remodelling and exists in two conformational states, a closed compact version which changes to an opened extended structure, upon GTP-binding, on which the built models were based. The goal of the PhD is to update the model of Fzo1 built in 2017, by working on the transmembrane domains using multiscale molecular dynamics, and then update the overall structure using artificial intelligence methods. An other project consisted in studying the amphipathic helix of HR1 domain of Mfn1 (MfnA-AH), test its membrane binding capabilities. Initially, we employed coarse-grained simulations, establishing a robust foundation for evaluating the predictive capacity of the MARTINI family of force fields. Using other simulations ran with the penetratin, we were able to provide a comparative analysis for the AH-membranes interactions in the MARTINI force-fields. The Mfn1-AH was then further characterized using all-atom simulations
Sauvanet, Cécile. „Caractérisation des acteurs et des mécanismes de la fusion mitochondriale“. Thesis, Bordeaux 2, 2011. http://www.theses.fr/2011BOR21883/document.
Mitochondria are dynamic organelles that continuously fuse and divide. This dynamic is required for mitochondrial biogenesis, function and degradation. The cross-talk between OXPHOS and dynamics and the mechanisms ensuring modulation of dynamics remain largely unraveled. We have investigated the relationship between fusion and OXPHOS in yeast cells carrying point mutations in the mitochondrial ATP6 gene that are associated to human diseases. We show that OXPHOS defects provoke severe defects of inner membrane, but not outer membrane fusion. Selective inhibition of inner membrane fusion can be recapitulated by ionophores that dissipate the inner membrane potential, but not by inhibitors of OXPHOS. We show a dominant inhibition of fusion that further provides a mechanism for the exclusion of defective mitochondria from the functional mitochondrial network, a pre-requisite for their selective targeting to mitophagy. These results suggest that defects of fusion could contribute to the pathology of diseases caused by mtDNA mutations. Moreover, these results imply that in cells, inhibition of dominant fusion could allow the exclusion of dysfunctional mitochondria mitochondrial network. Mitochondrial fusion involves many proteins of the superfamily of dynamin. If these proteins have been identified, the molecular mechanisms of fusion remain undetermined. In order to understand these mechanisms, we choose to characterize Mitofusin 1 and 2 proteins, essential for outer mitochondrial membrane fusion. These transmembrane proteins are consisting of two coiled-coil domains and one N-terminal GTPase domain. We have characterized GTPase activity of Mitofusin and reconstituted Mitofusins or fragments of Mitofusins into liposomes to study their capacity to fuse these liposomes. Full-length mitofusins can fuse liposomes containing cardiolipins. Surprisingly, these fusion events are independent of GTP but require Mg2+ in the buffer. Using electron microscopy, we show that mitofusin 1 and 2 induce local deformation of liposomes. This capacity of mitofusins to locally create highly curved (and thus fusogenic) membrane regions opens a new angle to understand the molecular mechanisms of mitochondrial fusion
Alsayyah, Cynthia. „Régulation de la fusion mitochondriale par le Système Ubiquitine Protéasome et les contacts physiques mitochondrie - peroxysomes chez la levure Saccharomyces cerevisiae“. Electronic Thesis or Diss., Université Paris sciences et lettres, 2021. https://theses.hal.science/tel-03810525.
Mitochondria are highly dynamic organelles that undergo constant fission and fusion of their outer and inner membranes. These processes are critical to maintain essential mitochondrial functions such as oxidative phosphorylation or calcium signaling. On a molecular basis, mitochondrial fusion and fission both depend on large GTPases of the Dynamin-Related Protein (DRP) family. The DRPs that mediate attachment and fusion of mitochondrial outer membranes are called the Mitofusins. The yeast mitofusin Fzo1 is located in the mitochondrial outer membrane. Its oligomerization promotes mitochondrial tethering followed by mitochondrial outer membrane fusion. Fzo1 has recently been proposed as a potential tether between peroxisomes and mitochondria when overexpressed. However, whether Fzo1 is present on peroxisomal membranes in WT cells or whether this extra-mitochondrial localization is a consequence of overexpression is unknown. In addition, we still don’t know how peroxisomal and mitochondrial Fzo1 mediate these contacts and their purpose in the cell. In my thesis, we were able to prove that Fzo1 naturally localizes to peroxisomes and oligomerizes with the mitochondrial Fzo1 thus creating Fzo1-Fzo1 contacts between peroxisomes and mitochondria which we will now call “Fzo1-mediated permit” contacts. We found that these contacts are modulated by Fzo1 levels which are tightly regulated by an SCF ubiquitin ligase called Mdm30 but also depending on fatty acid desaturation levels in the cell. From a functional standpoint, we found that the role of Fzo1-mediated permit contacts is to regulate mitochondrial fusion through the glyoxylate cycle, a process which allows cells to convert C2 unit compounds to C4 precursors for amino acid and carbohydrate biosynthesis. We discovered that Fzo1-mediated permit contacts allow the mitochondrial transfer of early byproducts of the glyoxylate cycle to stimulate mitochondrial fusion. In fine, the results obtained during my thesis enriched our knowledge on organelle contacts and allowed us to prove that Fzo1 is localized on both mitochondrial and peroxisomal membranes in wild type cells. Our studies also show that Fzo1-mediated permit contacts are modulated according to the cell’s needs as they play a crucial role in upkeeping mitochondrial fusion by providing a possible shortcut for byproducts of the glyoxylate cycle to reach mitochondria when direly needed
Hamze, Carmen. „Mitofusin 1 and Mitofusin 2 Function in the Context of Brain Development“. Thèse, Université d'Ottawa / University of Ottawa, 2011. http://hdl.handle.net/10393/20347.
Daste, Frédéric. „Function and regulation of coiled‐coil domains in intracellular membrane fusion“. Thesis, Sorbonne Paris Cité, 2015. http://www.theses.fr/2015PA05T001.
The molecular mechanisms involved in membrane fusion have been extensively studied for the past thirty years. Our current understanding of this phenomenon is mainly based on results obtained by (i) the development of physical models describing the fusion of membranes, (ii) structural and mechanistic investigations on fusion proteins of enveloped viruses and (iii) studies of SNARE protein-mediated intracellular fusion events of eukaryotic cells. Discovery of the SNARE complex was the outcome of interdisciplinary works which involved a wide range of techniques including yeast genetics, electrophysiology, molecular biology, cell-free biochemistry, adhesion/fusion biophysics and imaging. Taking advantage of the paradigms and biophysical techniques that emerged from these studies, we investigated the function and regulation of coiled-coil domains in intracellular fusion processes involving Longin-SNAREs or Mitofusins, two fusion protein machineries whose exact mode of action still remains unclear. A comprehensive understanding of the molecular mechanisms of membrane fusion requires the in vitro reconstitution of fusion proteins into a wide variety of membrane environments with defined and tunable biophysical properties. Ideally, these membrane systems should allow the experimentalists to control the lipid and protein composition as well as the membrane topology, to account for the variability observed across cellular fusing compartments. Reconstitution into liposomes offers amazing flexibility with the capacity to vary most of these relevant parameters, and to create a minimal environment in which membrane and/or soluble factors can be added, one at a time or in combination, to reveal their role with clarity. We have set up the in vitro reconstitution of proteins into various artificial membrane platforms for both systems (the Longin-SNAREs TI-VAMP and Sec22b and the coiled-coil domains of Mitofusins) and performed biochemical assays to gain insight into how these proteins execute their functions. The long-term goal of this project is to compare the molecular mechanisms of SNARE and Mitofusin fusion machineries and thus reveal structural and functional similitudes between (i) their core fusion proteins, and (ii) their regulatory factors
Cerqueira, Fernanda Menezes. „Efeitos da restrição calórica nas vias de sinalização por insulina e óxido nítrico: implicações para biogênese, morfologia e função mitocondriais“. Universidade de São Paulo, 2012. http://www.teses.usp.br/teses/disponiveis/46/46131/tde-24022013-151501/.
Calorie restriction (RC) is known to extend the lifespan in many organisms, and its mechanisms of action are still under investigation. Enhanced mitochondrial biogenesis driven by nitric oxide (•NO), synthesized by the endothelial nitric oxide synthase (eNOS), is proposed to be a CR central effect. Insulin is one of the most potent physiological activators of eNOS. However, plasmatic insulin levels are dramatically reduced in organisms under CR. The goal of this work was uncover the mechanisms associated with enhanced •NO signaling during CR, in vivo and in vitro, as well as the cellular consequences of increased mitochondrial mass, regarding lifespan and reserve respiratory capability. Female Swiss mice were submitted to 40% of CR. A tissue-specific (skeletal muscle, abdominal adipose tissue and brain) increment in basal Akt and eNOS phosphorylation, which was related to enhanced mitochondrial biogenesis, was observed. Indeed, this association was also verified in tissues from mice treated with low doses of a mitochondrial uncoupler, dinitrophenol (DNP). To unveil the mechanism behind the insulin signaling effects on •NO levels, serum from Sprague-Dawley rats submmited to 40% of CR was used to culture in VSMC cells, an in vitro CR protocol. CR sera enhanced insulin receptor (IR) and Akt phosphorylation, as well as nitrite (NO2-) accumulation in the culture media, the expression of eNOS and nNOS (neural NOS isoform) and eNOS phosphorylation. The effects of CR sera were reversed by Akt inhibition. The immunoprecipitation of serum adiponectin, a cytokine known to improve peripheral insulin sensitivity, also reversed the CR serum effects on insulin and •NO signaling. Cerebellar neurons, which do not express eNOS, just nNOS, were also cultured with CR or AL serum and also presented striking increments in •NO signaling, associated with mitochondrial biogenesis, increased reserve respiratory capability and lifespan extension. The mitochondrial effects promoted by CR were also observed in insulin secreting cells (INS1). However, under the CR condition, insulin secretion stimulated by glucose was impaired. The likely explanations are reduced mitochondrial reactive oxygen species (ROS) generation, or the alteration in mitochondrial morphology, associated, in our model, with enhanced mitofusin-2 expression (Mfn-2). In cells which the Mfn-2 was knocked down, insulin secretion in CR and AL groups was responsive to glucose at the same level, and the intracellular oxidants levels were much higher. Overall, CR improves •NO signaling due to enhanced insulin sensitivity, through Akt, and results in mitochondrial biogenesis. Adiponectin is a key molecule in this phenomenon. Increments in mitochondrial mass enhance the cellular reserve respiratory capability and lifespan. Mitochondrial morphology alterations are associated with possible decreases in ROS generation and impaired insulin release, maintained the low levels of plasmatic insulin.
Guillery, Olwenn. „Dynamique mitochondriale : caractérisation moléculaire et fonctionnelle de ses acteurs, de ses besoins énergétiques et de son évolution au cours de la mitose“. Paris 6, 2008. http://www.theses.fr/2008PA066313.
Trevisan, Tatiana. „Ruolo della morfologia e della funzionalità mitocondriale sulla distribuzione intracellulare dei mitocondri in neuroni di Drosophila“. Doctoral thesis, Università degli studi di Padova, 2016. http://hdl.handle.net/11577/3424418.
RIASSUNTO I mitocondri sono organelli essenziali per la cellula e la loro funzione primaria è di produrre energia sottoforma di ATP. I mitocondri sono organelli altamente dinamici:processi di fusione e fissione delle membrane mitocondriali ne controllano la forma, la lunghezza e il numero e un equilibrio tra i due meccanismi è fondamentale per una corretta morfologia mitocondriale. Numerose proteine sono coinvolte nei processi di fusione e fissione mitocondriale: Mitofusina 1 e Mitofusina 2 (Mfn1 e Mfn2) e Optic atrophy 1 (Opa1) regolano i processi di fusione mitocondriale, mentre Dynamin-related protein 1 (Drp1)mediala fissione. Drosophila possiede il gene mitochondrial assembly regulatory factor (MARF), espresso in modo ubiquitario ed omologo al gene MFN2. Nel tessuto muscolare la riduzione di espressione di Marf induce frammentazione e alterazione della morfologia del mitocondrio. Inoltre, mutanti di Marf mostrano una severa deplezione dei mitocondri nelle giunzioni neuromuscolari (NMJs) ed un’alterazione della morfologia della giunzione caratterizzata dall’aumento nel numero e da una riduzione nella dimensione dei bottoni sinaptici. Un altro aspetto della dinamica mitocondriale, oltre ai processi di fusione e fissione, è la motilità dei mitocondri, che deve essere altamente regolata soprattutto in cellule come i neuroni. Il trasporto mitocondriale e la continua ridistribuzione dei mitocondri lungo l’assone è essenziale per il mantenimento dell’integrità assonale e delle normali funzioni della cellula. Studi hanno messo in evidenza come la mancanza di mitocondri a livello delle giunzioni neuromuscolari in Drosophila comprometta la trasmissione sinaptica e come difetti nel trasporto mitocondriale assonale siano implicati nello sviluppo di disordini neurologici e malattie neurodegenerative (Chan, 2006). Lo scopo di questo lavoro è quello di capire il ruolo della morfologia e della funzione mitocondriale nella distribuzione intracellulare dei mitocondri nei neuroni. Per fare questo abbiamo utilizzato Drosophila melanogaster, organismo modello efficace per l’analisi della funzione genica, inclusa quella di geni responsabili di patologie umane. L’analisi della morfologia mitocondriale è stata effettuata utilizzando linee di Drosophilache esprimono in vivo un transgene per RNA interference e che permette di ridurre l’espressione di geni endogeni coinvolti nei processi di fusione e fissione mitocondriale, quali Marf, Opa1 e Drp1. Abbiamo inoltre creato linee che esprimono contemporaneamente i trangeni per RNAi di Marf e Drp1 o Opa1 e Drp1, con lo scopo di bilanciare i meccanismi di fusione e/o fissione. Ci siamo soffermati in particolare sullo studio di due aspetti principali, la morfologia e la funzionalità mitocondriale, per capire se difetti nella morfologia e nella funzionalità mitocondriale siano collegate e concorrano insieme allo sviluppo di patologie.Numerose patologie neurodegenerative sono infatti caratterizzate da alterazioni del trasporto mitocondriale e spesso questo è associato a difetti nella morfologia e nella funzionalità mitocondriale. Per studiare la morfologia mitocondriale, le linee UAS-RNAi sono state incrociate con una linea che contiene il promotore ELAV per l’espressione tessuto-specifica nei neuroni ed esprime una GFP mitocondriale. Abbiamo analizzato la morfologia dei mitocondri, sia nel corpo cellulare sia negli assoni e la distribuzione mitocondriale in assoni lunghi come i motoneuroni e assoni corti come quelli del nervo ottico e la distribuzione mitocondriale nella giunzione neuromuscolare.I risultati ottenuti mostrano che frammentazione dei mitocondri e alterazione della distribuzione mitocondriale assonale in individui in cui sia ridotta l’espressione di proteine di fusione. Inoltre si osserva una diminuzione della percentuale dei mitocondri mobili e del numero assoluto dei mitocondri anterogradi e retrogradi. Questi dati dimostrano che vi è una stretta correlazione tra morfologia mitocondriale e distribuzione dei mitocondri, in particolare in assoni lunghi. Inoltre analizzando le linee Marf RNAi Drp1 RNAi e Opa1 RNAi Drp1 RNAi, nelle quali gli eventi di fusione e fissione ridotti ma sono in equilibrio tra loro, si osserva un miglioramento la morfologia, la distribuzione e il trasporto mitocondriale assonale in modo particolare nel caso di Opa1 e non nel caso di Marf. Abbiamo cercato di capire quindi se in questi individui vi fossero alterazioni delle funzionalità mitocondriali attraverso l’analisi della capacità respiratoria mitocondriale, dell’attività dei complessi della catena respiratoria e della capacità di produzione di ATP. I risultati ottenuti dimostrano che morfologia e funzionalità mitocondriale non sempre sono collegate tra loro hanno effetti diversi nella modulazione della distribuzione mitocondriale assonale. In conclusione possiamo affermare che solamente la morfologia e la dimensione del mitocondrio sembrano essere essenziali per la corretta distribuzione mitocondriale assonale.
Sexton, Jaime. „Genetic Analysis of Miro and Mitofusin Protein Interactions“. Thesis, The University of Arizona, 2014. http://hdl.handle.net/10150/321953.
Gangaraju, Sandhya. „Role of mitofusin2 in the regulation of mitochondrial dynamics“. Thesis, University of Ottawa (Canada), 2003. http://hdl.handle.net/10393/26483.
Bücher zum Thema "Mitofusins":
Williams, Linda. Role of Mitofusin 2 in the biology of hematopoietic stem cells. [New York, N.Y.?]: [publisher not identified], 2020.
Buchteile zum Thema "Mitofusins":
Muñoz, Juan Pablo, und Antonio Zorzano. „Analysis of Mitochondrial Morphology and Function Under Conditions of Mitofusin 2 Deficiency“. In Methods in Molecular Biology, 307–20. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4939-2288-8_21.
Gegg, Matthew E. „Ubiquitination of Mitofusins in PINK1/Parkin-Mediated Mitophagy“. In Autophagy: Cancer, Other Pathologies, Inflammation, Immunity, Infection, and Aging, 189–99. Elsevier, 2014. http://dx.doi.org/10.1016/b978-0-12-405528-5.00012-2.
Allegra, Alessandro, Vanessa Innao, Andrea Gaetano Allegra und Caterina Musolino. „Relationship between mitofusin 2 and cancer“. In Advances in Protein Chemistry and Structural Biology, 209–36. Elsevier, 2019. http://dx.doi.org/10.1016/bs.apcsb.2018.11.009.
Konferenzberichte zum Thema "Mitofusins":
Bhatia, D., E. Kallinos, M. Plataki, A. M. Choi und M. E. Choi. „Myeloid and Type II Alveolar Cell-specific Mitofusins Regulate Kidney Fibrosis-associated Lung Injury“. In American Thoracic Society 2023 International Conference, May 19-24, 2023 - Washington, DC. American Thoracic Society, 2023. http://dx.doi.org/10.1164/ajrccm-conference.2023.207.1_meetingabstracts.a1078.
Guda, Maheedhara Reddy, Swapna Asuthkar, Collin M. Labak, Chase P. Smith, Andrew J. Tsung und Kiran Velpula. „Abstract 5494: Targeting deregulated expression and function of Mitofusin 1 in glioblastoma“. In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-5494.
Wu, Meng-Ju, Mi Ran Kim, Silpa Gampala, Yingsheng Zhang, Yueyang Wang, Jer-Yen Yang und Chun-Ju Chang. „Abstract 798: Epithelial-mesenchymal transition directs stem cell polarity via regulation of mitofusin“. In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-798.
Wu, Meng-Ju, Mi Ran Kim, Silpa Gampala, Yingsheng Zhang, Yueyang Wang, Jer-Yen Yang und Chun-Ju Chang. „Abstract 798: Epithelial-mesenchymal transition directs stem cell polarity via regulation of mitofusin“. In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-798.