Relevant bibliographies by topics / NF2/Merlin

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Academic literature on the topic 'NF2/Merlin'

Author: Grafiati
Published: 12 October 2024

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Journal articles on the topic "NF2/Merlin"

1

Bashour, Anne-Marie, J. J. Meng, Wallace Ip, Mia MacCollin, and Nancy Ratner. "The Neurofibromatosis Type 2 Gene Product, merlin, Reverses the F-Actin Cytoskeletal Defects in Primary Human Schwannoma Cells." Molecular and Cellular Biology 22, no. 4 (February 15, 2002): 1150–57. http://dx.doi.org/10.1128/mcb.22.4.1150-1157.2002.

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ABSTRACT Schwannoma tumors, which occur sporadically and in patients with neurofibromatosis, account for 8% of intracranial tumors and can only be treated by surgical removal. Most schwannomas have biallelic mutations in the NF2 tumor suppressor gene. We previously showed that schwannoma-derived Schwann cells exhibit membrane ruffling and aberrant cell spreading when plated onto laminin, indicative of fundamental F-actin cytoskeletal defects. Here we expand these observations to a large group of sporadic and NF2-related tumors and extend them to schwannomatosis-derived tumors. Mutation at NF2 correlated with F-actin abnormalities, but the extent of morphological change did not correlate with the type of NF2 mutation. We used a recently described molecular strategy, TAT-mediated protein transfer, to acutely introduce the NF2 protein, merlin, into primary human schwannoma cells in an attempt to reverse the cytoskeletal phenotype. Abnormal ruffling and cell spreading by cells with identified NF2 mutations were rapidly reversed by introduction of TAT-merlin. The effect is specific to TAT-merlin isoform 1, the growth-suppressive isoform of merlin. TAT-merlin isoform 2, a TAT-merlin mutant (L64P), and merlin lacking TAT were ineffective in reversing the cytoskeletal phenotype. Results show that merlin isoform 1 is sufficient to restore normal actin organization in NF2-deficient human tumor cells, demonstrating a key role for merlin in the NF2 phenotype. These results lay the foundation for epigenetic complementation studies in NF2 mouse models and possibly for experiments to evaluate the utility of merlin transduction into patients as protein therapy.
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Eaton, Charlotte, Abrar Choudhury, Timothy Casey-Clyde, Danielle Swaney, Nevan Krogan, and David Raleigh. "CSIG-26. NF2/MERLIN DRIVES MENINGIOMA APOPTOSIS AND SUCEPTIBILITY TO CYTOTOXIC THERAPY." Neuro-Oncology 23, Supplement_6 (November 2, 2021): vi39. http://dx.doi.org/10.1093/neuonc/noab196.152.

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Abstract BACKGROUND Alterations in NF2 underlie meningioma tumorigenesis, but tumor suppressor functions of the NF2 gene product, Merlin, are incompletely understood in meningiomas. Here we integrate proteomic proximity-labelling mass spectrometry with CRISPR interference (CRISPRi), RNA sequencing, and biochemical approaches to discover Merlin drives meningioma apoptosis and susceptibility to cytotoxic therapy. METHODS RNA sequencing was performed on triplicate M10G meningioma cells stably expressing CRISPRi machinery and either non-targeting control sgRNAs, sgRNAs suppressing NF2, or sgRNAs suppressing NF2 with Merlin rescue. QPCR in IOMM-Lee and MSC1 meningioma cells expressing non-targeting control shRNAs or shRNAs suppressing NF2 was used for orthogonal validation in vitro. RNA sequencing of euploid meningiomas (n=52) or meningiomas with loss of NF2 as the only copy number variant (n=28) was used for orthogonal validation in vivo. Merlin interactors in meningioma cells were identified using APEX proteomic proximity-labelling mass spectrometry. Mechanistic and functional studies were performed using biochemical, molecular, and cell biology approaches in meningioma cells and CH-157MN meningioma xenografts treated with cytotoxic chemotherapy or ionizing radiation. RESULTS Merlin suppression in meningioma cells and xenografts inhibited pro-apoptotic interferon regulatory factor (IRF) target genes and attenuated meningioma apoptosis. Merlin suppression did not alter IRF stability or subcellular localization in meningioma cells, and proteomic proximity-labelling mass spectrometry revealed a novel interaction between wildtype Merlin and ARHGAP35, a DNA binding factor that inhibits glucocorticoid receptor expression (NR3C1). NR3C1 inhibits IRF activity to prevent apoptosis, and Merlin suppression in meningioma cells induced NR3C1expression, which was inhibited by Merlin rescue. Further, NR3C1 suppression rescued meningioma cell apoptosis in the absence of Merlin, and NR3C1 expression was increased in human meningiomas with loss of NF2 compared to euploid meningiomas. CONCLUSIONS These data shed light on a novel pro-apoptotic tumor suppressor function of Merlin regulating glucocorticoid signalling and susceptibility to cytotoxic therapy in meningiomas.
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James, Marianne F., Sangyeul Han, Carolyn Polizzano, Scott R. Plotkin, Brendan D. Manning, Anat O. Stemmer-Rachamimov, James F. Gusella, and Vijaya Ramesh. "NF2/Merlin Is a Novel Negative Regulator of mTOR Complex 1, and Activation of mTORC1 Is Associated with Meningioma and Schwannoma Growth." Molecular and Cellular Biology 29, no. 15 (May 18, 2009): 4250–61. http://dx.doi.org/10.1128/mcb.01581-08.

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ABSTRACT Inactivating mutations of the neurofibromatosis 2 (NF2) gene, NF2, result predominantly in benign neurological tumors, schwannomas and meningiomas, in humans; however, mutations in murine Nf2 lead to a broad spectrum of cancerous tumors. The tumor-suppressive function of the NF2 protein, merlin, a membrane-cytoskeleton linker, remains unclear. Here, we identify the mammalian target of rapamycin complex 1 (mTORC1) as a novel mediator of merlin's tumor suppressor activity. Merlin-deficient human meningioma cells and merlin knockdown arachnoidal cells, the nonneoplastic cell counterparts of meningiomas, exhibit rapamycin-sensitive constitutive mTORC1 activation and increased growth. NF2 patient tumors and Nf2-deficient mouse embryonic fibroblasts demonstrate elevated mTORC1 signaling. Conversely, the exogenous expression of wild-type merlin isoforms, but not a patient-derived L64P mutant, suppresses mTORC1 signaling. Merlin does not regulate mTORC1 via the established mechanism of phosphoinositide 3-kinase-Akt or mitogen-activated protein kinase/extracellular signal-regulated kinase-mediated TSC2 inactivation and may instead regulate TSC/mTOR signaling in a novel fashion. In conclusion, the deregulation of mTORC1 activation underlies the aberrant growth and proliferation of NF2-associated tumors and may restrain the growth of these lesions through negative feedback mechanisms, suggesting that rapamycin in combination with phosphoinositide 3-kinase inhibitors may be therapeutic for NF2.
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Lee, Hansoo, Donghwa Kim, Han C. Dan, Eric L. Wu, Tatiana M. Gritsko, Chuanhai Cao, Santo V. Nicosia, et al. "Identification and Characterization of Putative Tumor Suppressor NGB, a GTP-Binding Protein That Interacts with the Neurofibromatosis 2 Protein." Molecular and Cellular Biology 27, no. 6 (January 8, 2007): 2103–19. http://dx.doi.org/10.1128/mcb.00572-06.

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ABSTRACT Mutations of the neurofibromatosis 2 (NF2) tumor suppressor gene have frequently been detected not only in schwannomas and other central nervous system tumors of NF2 patients but also in their sporadic counterparts and malignant tumors unrelated to the NF2 syndrome such as malignant mesothelioma, indicating a broader role for the NF2 gene in human tumorigenesis. However, the mechanisms by which the NF2 product, merlin or schwannomin, is regulated and controls cell proliferation remain elusive. Here, we identify a novel GTP-binding protein, dubbed NGB (referring to NF2-associated GTP binding protein), which binds to merlin. NGB is highly conserved between Saccharomyces cerevisiae, Caenorhabditis elegans, and human cells, and its GTP-binding region is very similar to those found in R-ras and Rap2. However, ectopic expression of NGB inhibits cell growth, cell aggregation, and tumorigenicity in tumorigenic schwanomma cells. Down-regulation and infrequent mutation of NGB were detected in human glioma cell lines and primary tumors. The interaction of NGB with merlin impairs the turnover of merlin, yet merlin does not affect the GTPase nor GTP-binding activity of NGB. Finally, the tumor suppressor functions of NGB require merlin and are linked to its ability to suppress cyclin D1 expression. Collectively, these findings indicate that NGB is a tumor suppressor that regulates and requires merlin to suppress cell proliferation.
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Kim, Bae-Hoon, Yeon-Ho Chung, Tae-Gyun Woo, So-mi Kang, Soyoung Park, Minju Kim, and Bum-Joon Park. "NF2-Related Schwannomatosis (NF2): Molecular Insights and Therapeutic Avenues." International Journal of Molecular Sciences 25, no. 12 (June 14, 2024): 6558. http://dx.doi.org/10.3390/ijms25126558.

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NF2-related schwannomatosis (NF2) is a genetic syndrome characterized by the growth of benign tumors in the nervous system, particularly bilateral vestibular schwannomas, meningiomas, and ependymomas. This review consolidates the current knowledge on NF2 syndrome, emphasizing the molecular pathology associated with the mutations in the gene of the same name, the NF2 gene, and the subsequent dysfunction of its product, the Merlin protein. Merlin, a tumor suppressor, integrates multiple signaling pathways that regulate cell contact, proliferation, and motility, thereby influencing tumor growth. The loss of Merlin disrupts these pathways, leading to tumorigenesis. We discuss the roles of another two proteins potentially associated with NF2 deficiency as well as Merlin: Yes-associated protein 1 (YAP), which may promote tumor growth, and Raf kinase inhibitory protein (RKIP), which appears to suppress tumor development. Additionally, this review discusses the efficacy of various treatments, such as molecular therapies that target specific pathways or inhibit neomorphic protein–protein interaction caused by NF2 deficiency. This overview not only expands on the fundamental understanding of NF2 pathophysiology but also explores the potential of novel therapeutic targets that affect the clinical approach to NF2 syndrome.
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Houshmandi, S. Sean, Ryan J. Emnett, Marco Giovannini, and David H. Gutmann. "The Neurofibromatosis 2 Protein, Merlin, Regulates Glial Cell Growth in an ErbB2- and Src-Dependent Manner." Molecular and Cellular Biology 29, no. 6 (December 22, 2008): 1472–86. http://dx.doi.org/10.1128/mcb.01392-08.

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ABSTRACT Individuals with the inherited cancer predisposition syndrome neurofibromatosis 2 (NF2) develop several central nervous system (CNS) malignancies, including glial cell neoplasms (ependymomas). Recent studies have suggested that the NF2 protein, merlin (or schwannomin), may regulate receptor tyrosine kinase signaling, intracellular mitogenic growth control pathways, or adherens junction organization in non-nervous-system cell types. For this report, we used glial fibrillary acidic protein conditional knockout mice and derivative glia to determine how merlin regulates CNS glial cell proliferation. We show that the loss of merlin in glial cells results in increased proliferation in vitro and in vivo. Merlin regulation of glial cell growth reflects deregulated Src activity, such that pharmacologic or genetic inhibition of Src activation reduces Nf2 −/− glial cell growth to wild-type levels. We further show that Src regulates Nf2 −/− glial cell growth by sequentially regulating FAK and paxillin phosphorylation/activity. Next, we demonstrate that Src activation results from merlin regulation of ErbB2 activation and that genetic or pharmacologic ErbB2 inhibition reduces Nf2 −/− glial cell Src/Src effector activation and proliferation to wild-type levels. Lastly, we show that merlin competes with Src for direct binding to ErbB2 and present a novel molecular mechanism for merlin regulation of ErbB2-dependent Src signaling and growth control.
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Xiao, Guang-Hui, Ryan Gallagher, Justin Shetler, Kristine Skele, Deborah A. Altomare, Richard G. Pestell, Suresh Jhanwar, and Joseph R. Testa. "The NF2 Tumor Suppressor Gene Product, Merlin, Inhibits Cell Proliferation and Cell Cycle Progression by Repressing Cyclin D1 Expression." Molecular and Cellular Biology 25, no. 6 (March 15, 2005): 2384–94. http://dx.doi.org/10.1128/mcb.25.6.2384-2394.2005.

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ABSTRACT Inactivation of the NF2 tumor suppressor gene has been observed in certain benign and malignant tumors. Recent studies have demonstrated that merlin, the product of the NF2 gene, is regulated by Rac/PAK signaling. However, the mechanism by which merlin acts as a tumor suppressor has remained obscure. In this report, we show that adenovirus-mediated expression of merlin in NF2-deficient tumor cells inhibits cell proliferation and arrests cells at G1 phase, concomitant with decreased expression of cyclin D1, inhibition of CDK4 activity, and dephosphorylation of pRB. The effect of merlin on cell cycle progression was partially overridden by ectopic expression of cyclin D1. RNA interference experiments showed that silencing of the endogenous NF2 gene results in upregulation of cyclin D1 and S-phase entry. Furthermore, PAK1-stimulated cyclin D1 promoter activity was repressed by cotransfection of NF2, and PAK activity was inhibited by expression of merlin. Interestingly, the S518A mutant form of merlin, which is refractory to phosphorylation by PAK, was more efficient than the wild-type protein in inhibiting cell cycle progression and in repressing cyclin D1 promoter activity. Collectively, our data indicate that merlin exerts its antiproliferative effect, at least in part, via repression of PAK-induced cyclin D1 expression, suggesting a unifying mechanism by which merlin inactivation might contribute to the overgrowth seen in both noninvasive and malignant tumors.
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Eaton, Charlotte, Paola Bisignano, and David Raleigh. "CSIG-22. CANCER-ASSOCIATED MISSENSE SINGLE NUCLEOTIDE VARIANTS REGULATE THE STABILITY AND SUBCELLULAR LOCALIZATION OF NF2/MERLIN." Neuro-Oncology 22, Supplement_2 (November 2020): ii32. http://dx.doi.org/10.1093/neuonc/noaa215.134.

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Abstract BACKGROUND Alterations in the NF2 tumor suppressor gene lead to meningiomas and schwannomas, but the tumor suppressor functions of the NF2 gene product, Merlin, are incompletely understood. To address this problem, we performed a structure-function analysis of Merlin by expressing cancer-associated missense single-nucleotide variants (mSNVs) in primary cancer cells for biochemical and cell biology experiments. METHODS All NF2 mSNVs were assembled from cBioPortal and COSMIC, and modelled on the FERM, a-helical, and C-terminal domains of Merlin (PDB 4ZRJ) using comparative structure prediction on the Robetta server and visually inspected using Pymol. mSNV hotspots were defined from sliding windows with at least 10 mutations within 5 residues in either direction. mSNVs from hotspots in meningiomas, schwannomas, or both, were selected for in vitro mechanistic analyses using immunofluorescence and immunoblotting of whole cell, plasma membrane, cytoskeletal, cytoplasmic, nuclear, and chromatin subcellular fractions from M10G meningioma cells and HEI-193 schwannoma cells. RESULTS We identified the following cancer-associated hotspot mSNVs in NF2, which were over-expressed for mechanistic studies: L46R, S156N, W191R, A211D, V219M, R418C and R462K. Endogenous Merlin was detected in all subcellular compartments, but was enriched in the nucleus. L46R and A211D mapped to hydrophobic pockets in the FERM domain, destabilized Merlin, and excluded Merlin from all subcellular compartments except the cytoskeleton. S156N, W191R and V219M also mapped to the FERM domain, but did not affect Merlin stability, and V219M attenuated chromatin localization, suggesting this motif may be involved in binding events that regulate subcellular localization. R418C and R463K mapped to the a-helical domain, but only R418C destabilized Merlin. CONCLUSION Our results suggest that cancer-associated mSNVs inactive the tumor suppressor functions of NF2 by altering the stability, subcellular localization, or binding partners of Merlin. Further work is required to identify and understand the impact of binding partners and subcellular localization on Merlin function.
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Bachir, Suha, Sanjit Shah, Scott Shapiro, Abigail Koehler, Abdelkader Mahammedi, Ravi N. Samy, Mario Zuccarello, Elizabeth Schorry, and Soma Sengupta. "Neurofibromatosis Type 2 (NF2) and the Implications for Vestibular Schwannoma and Meningioma Pathogenesis." International Journal of Molecular Sciences 22, no. 2 (January 12, 2021): 690. http://dx.doi.org/10.3390/ijms22020690.

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Patients diagnosed with neurofibromatosis type 2 (NF2) are extremely likely to develop meningiomas, in addition to vestibular schwannomas. Meningiomas are a common primary brain tumor; many NF2 patients suffer from multiple meningiomas. In NF2, patients have mutations in the NF2 gene, specifically with loss of function in a tumor-suppressor protein that has a number of synonymous names, including: Merlin, Neurofibromin 2, and schwannomin. Merlin is a 70 kDa protein that has 10 different isoforms. The Hippo Tumor Suppressor pathway is regulated upstream by Merlin. This pathway is critical in regulating cell proliferation and apoptosis, characteristics that are important for tumor progression. Mutations of the NF2 gene are strongly associated with NF2 diagnosis, leading to benign proliferative conditions such as vestibular schwannomas and meningiomas. Unfortunately, even though these tumors are benign, they are associated with significant morbidity and the potential for early mortality. In this review, we aim to encompass meningiomas and vestibular schwannomas as they pertain to NF2 by assessing molecular genetics, common tumor types, and tumor pathogenesis.
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LaJeunesse, Dennis R., Brooke M. McCartney, and Richard G. Fehon. "Structural Analysis of Drosophila Merlin Reveals Functional Domains Important for Growth Control and Subcellular Localization." Journal of Cell Biology 141, no. 7 (June 29, 1998): 1589–99. http://dx.doi.org/10.1083/jcb.141.7.1589.

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Merlin, the product of the Neurofibromatosis type 2 (NF2) tumor-suppressor gene, is a member of the protein 4.1 superfamily that is most closely related to ezrin, radixin, and moesin (ERM). NF2 is a dominantly inherited disease characterized by the formation of bilateral acoustic schwannomas and other benign tumors associated with the central nervous system. To understand its cellular functions, we are studying a Merlin homologue in Drosophila. As is the case for NF2 tumors, Drosophila cells lacking Merlin function overproliferate relative to their neighbors. Using in vitro mutagenesis, we define functional domains within Merlin required for proper subcellular localization and for genetic rescue of lethal Merlin alleles. Remarkably, the results of these experiments demonstrate that all essential genetic functions reside in the plasma membrane– associated NH2-terminal 350 amino acids of Merlin. Removal of a seven–amino acid conserved sequence within this domain results in a dominant-negative form of Merlin that is stably associated with the plasma membrane and causes overproliferation when expressed ectopically in the wing. In addition, we provide evidence that the COOH-terminal region of Merlin has a negative regulatory role, as has been shown for ERM proteins. These results provide insights into the functions and functional organization of a novel tumor suppressor gene.
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Dissertations / Theses on the topic "NF2/Merlin"

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Johnson, Kristen C. (Kristen Carrie) 1976. "Analysis of the function of the Nf2 tumor suppressor protein, Merlin." Thesis, Massachusetts Institute of Technology, 2003. http://hdl.handle.net/1721.1/29763.

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Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biology, 2003.
Vita.
Includes bibliographical references.
The Neurofibromatosis type 2 tumor suppressor gene (NF2) is mutated in inherited and sporadically occurring central nervous system tumors. The NF2 encoded protein, merlin, shares close sequence similarity in its amino-terminal domain to members of the band 4.1 family of membrane-cytoskeletal linkers. Similarities between merlin and this family suggest a role for merlin in regulating cytoskeletal function. Thus, NF2 may be a novel type of tumor suppressor gene that mediates its tumor suppressor function through interactions with the actin cytoskeleton. However, the molecular and cellular functions of this tumor suppressor gene were largely unknown when the work described here began. Mutational analysis of Nf2 in flies has lead to the identification of a dominant-negative allele, which harbors mutations in the amino-terminal domain of the protein. The work presented here demonstrates that expression of a murine analog of this amino-terminal mutant of Nf2 (termed, Nf2BBA) leads to complete transformation of NIH3T3 fibroblasts in culture. Cells that express Nf2BBA display disruptions of the actin cytoskeleton, lack of contact inhibition of growth, and anchorage-independent growth. In addition, Nf2-deficient mouse embryo fibroblasts (MEFs) exhibited similar contact inhibition and cell-matrix adhesion defects to Nf2BBA expressing cells. Nf2BBA cells continue to cycle under normal growth inhibitory conditions, such as serum withdrawal, and exhibit high levels of the cell cycle regulator, cyclin D1. Elevated levels of cyclin D1 are necessary for cellular transformation following Nf2BBA expression. Nevertheless, the exact mechanism by which Nf2BBA results in cellular transformation remains elusive. Recently published studies have revealed that merlin may regulate members of the RhoGTPase
(cont.) family, as absence of Nf2 expression in fibroblasts leads to many phenotypes reminiscent of overactive Rac, such as increased membrane ruffling and increased activity of the c-jun N- terminal kinase (JNK). Our work has extended to the analysis of the role of merlin in the regulation of the Rac pathway. Using rat schwannoma cells and N2-deficient MEFs, we have demonstrated that merlin exerts its inhibitory effects downstream of Rac, through a direct interaction with the p21 activated kinase, Pak. We demonstrate that in the absence of merlin, Pak is active and hyperphosphorylated, and, conversely, when merlin is overexpressed, Pak activity is diminished. The N-terminal half of merlin binds to the functionally conserved Rac/Cdc42 interaction binding (CRIB) domain of Pak. Several models for merlin regulation of Pak activity will be discussed. Finally, the identification of Pak as a kinase that is misregulated in the absence of NF2 may lead to possible avenues for therapeutic intervention.
by Kristen C. Johnson.
Ph.D.
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Schulze, Karin Marlies Marion. "Herstellung rekombinanter Retroviren, In-vitro-Gentransfer und Expressionsanalyse des NF2-Gens Merlin." [S.l. : s.n.], 2001. http://deposit.ddb.de/cgi-bin/dokserv?idn=962345210.

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Chen, Yaxiong. "Characterization of chicken NF2/merlin and its functions in early limb muscle development /." free to MU campus, to others for purchase, 2003. http://wwwlib.umi.com/cr/mo/fullcit?p3115532.

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Mani, Timmy. "The Role of Phosphoinositide Binding in Merlin Function." University of Cincinnati / OhioLINK, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1299181100.

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Zhan, Yu. "Mixed Lineage Kinase 3 Signaling in Ovarian Cancer and Neurofibromatosis-2." University of Toledo / OhioLINK, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=toledo1310127039.

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Adès, Noémie. "PAK1 and NF2 antagonist functions in regulating central nervous system myelination : from modulation of oligodendrocyte cytoskeleton to myelin sheath formation." Electronic Thesis or Diss., Sorbonne université, 2024. https://accesdistant.sorbonne-universite.fr/login?url=https://theses-intra.sorbonne-universite.fr/2024SORUS197.pdf.

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Dans le système nerveux central, la formation des gaines de myéline par les oligodendrocytes permet une propagation efficace et adaptée des potentiels d'action le long des axones, ainsi qu'un apport métabolique aux neurones. Le processus de myélinisation requière une fine régulation du cytosquelette d'actine des oligodendrocytes. En effet, la première étape de la myélinisation, qu'est l'extension d'un prolongement par les oligodendrocytes pour atteindre un axone, est soutenue par une polymérisation de l'actine. En revanche, l'enroulement de ce prolongement et son étalement autour de l'axone pour former cette structure multi-lamellaire qu'est la gaine de myéline nécessite une déconstruction drastique du cytosquelette d'actine. Les mécanismes moléculaires déclenchant ce passage vers la dépolymérisation de l'actine restent peu clairs. Néanmoins, leur identification est essentielle, car en plus de mieux comprendre les mécanismes sous-tendant la myélinisation, elle permettrait de trouver de nouvelles cibles thérapeutiques pour stimuler la formation et la réparation de la myéline dans les maladies qui l'affectent, qu'il s'agisse une perte de myéline comme dans la sclérose en plaques, ou une formation inadaptée de myéline par rapport aux besoins des circuits neuronaux comme dans les troubles du spectre autistique.Pendant la première partie de ma thèse, nous avons testé l'implication de la protéine PAK1 (P21 Activated Kinase 1) dans le contrôle de la myélinisation, agissant potentiellement comme levier permettant le passage à la dépolymérisation de l'actine. En effet, PAK1 est connue pour moduler les dynamiques de l'actine via son activité kinase : l'activer favorise le maintien du cytosquelette d'actine polymérisé, alors que l'inhiber permet son désassemblage. Au cours de la maturation des oligodendrocytes, nous avons montré que l'expression de PAK1 augmente, alors que son activité kinase est de plus en plus inhibée, ce qui est cohérent avec un potentiel rôle de PAK1 dans la myélinisation. De façon intéressante, nous avons montré qu'empêcher l'inhibition de PAK1 dans les oligodendrocytes in vitro restreint la dépolymérisation de l'actine et par conséquent l'expansion des membranes de myéline. À l'inverse, augmenter l'inhibition de PAK1 stimule la dépolymérisation de l'actine et l'expansion des membranes de myéline. Ainsi, l'inhibition endogène de PAK1 est nécessaire à la déconstruction du cytosquelette d'actine menant à la formation de la myéline. In vivo, la délétion de Pak1 dans les oligodendrocytes augmente spécifiquement l'épaisseur des gaines de myéline. Ensemble, ces résultats suggèrent que l'activité kinase de PAK1 doit nécessairement être inhibée pour stimuler la myélinisation. Ces observations impliquent également la présence d'un inhibiteur endogène de PAK1 dans les oligodendrocytes. Nos analyses ont mené à l’identification et la validation de NF2/Merlin. Nous avons montré que NF2/Merlin, en inhibant PAK1, régule la dynamique du cytosquelette d'actine dans l'oligodendrocyte et l'expansion des membranes de myéline in vitro. Ces résultats ont ainsi permis l'émergence d'un modèle mécanistique dans lequel l'action antagoniste de NF2/Merlin et PAK1 stimule la dépolymérisation de l'actine dans les oligodendrocytes, et donc l'expansion des membranes de myéline.Dans la seconde partie de ma thèse, qui est en cours, nous avons montré que NF2/Merlin contrôle la myélinisation développementale in vivo via des mécanismes dépendants et indépendants de l'axe PAK1/actine, impliquant notamment une modulation des microtubules.Dans l'ensemble, les résultats de ma thèse permettent de mieux comprendre les mécanismes sous-jacents de la myélinisation, qui pourraient également être étudiés dans le contexte de la remyélinisation
In the central nervous system, myelin sheath formation by oligodendrocytes ensures efficient and adapted propagation of action potentials, as well as metabolic support to neurons. Myelination is an intrinsic program of mature oligodendrocytes that requires precise modulation of their actin cytoskeleton. Indeed, the extension of the oligodendrocyte process to reach an axon is supported by actin polymerisation; whereas the extension and wrapping of oligodendrocyte membrane to form the concentric multi-layered membrane, that is myelin sheath, is supported by a drastic deconstruction of the actin cytoskeleton. The molecular mechanisms triggering this shift to actin depolymerisation remain unclear. Determining the mechanisms involved in this crucial process provides a better understanding of myelination and could pave the way for new therapeutic targets to stimulate myelin formation. This is of great importance for demyelinating diseases such as multiple sclerosis, and for neurodevelopmental diseases characterised by a mismatch of the amount of myelin formed to the needs of circuits, such as in autism spectrum disorders.During the first part of my thesis, we tested the involvement of P-21 activated kinase 1 (PAK1) in the regulation of myelination, hypothesising its potential control of actin dynamics. Indeed, PAK1 is known to regulate the actin cytoskeleton via its kinase activity: active PAK1 maintains actin cytoskeleton polymerised, while inhibited PAK1 stimulates its deconstruction. We showed that during oligodendrocyte maturation, PAK1 is increasingly expressed, yet its kinase activity is stronly inhibited, which is consistent with the potential role of PAK1 in regulating myelination. Moreover, we showed that maintaining PAK1 in an abnormal constitutively active form restrains actin deconstruction and myelin membrane expansion, whereas enhancing PAK1 inhibition increases myelin expansion via enhanced actin depolymerisation. Together, these results suggest that PAK1 endogenous inhibition is necessary for actin depolymerisation and subsequent myelin formation. In vivo, depleting Pak1 in oligodendrocytes specifically increases myelin thickness. Taken together, our findings suggest that to form the correct amount of myelin, PAK1 kinase activity must be inactivated, whether the protein is absent or inhibited. Moreover, this implies the presence of an endogenous PAK1 inhibitor in oligodendrocytes. We identified and validated NF2/Merlin as an endogenous inhibitor of PAK1 in oligodendrocytes, enabling actin depolymerisation and myelin membrane expansion. Overall, this initial study has led to the emergence of a mechanistic model in which the antagonistic actions of NF2/Merlin and PAK1 stimulates actin depolymerisation in oligodendrocytes and hence the formation of myelin membranes.In the second part of my thesis, currently in progress, we have shown that NF2/Merlin controls developmental myelination in vivo via PAK1/actin axis-dependent and -independent mechanisms, in particular involving microtubule modulation.Overall, the findings of my thesis provide a more comprehensive understanding of the underlying mechanisms of myelination, which could also be studied in the context of remyelination
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Lyons, Rimmer Jade. "The potential of CRL4-DCAF1 and KSR1 as therapeutic targets in low-grade Merlin-deficient tumours." Thesis, University of Plymouth, 2018. http://hdl.handle.net/10026.1/12833.

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Merlin is a tumour suppressor protein that is frequently mutated or downregulated in cancer. Biallelic Merlin inactivation is causative of tumour formation, including schwannoma, meningioma and ependymoma. These tumours can occur sporadically or as part of the genetic condition Neurofibromatosis type 2 (NF2) and cause significant morbidity. The current treatment options are restricted to surgery and radiotherapy, which are invasive and may cause further tumour development. The activity of both the E3 ubiquitin ligase complex Cullin 4 really interesting new gene (RING) E3 ubiquitin ligase- DNA damage binding protein (DDB1) and Cullin 4 associated factor 1 (CRL4-DCAF1) and Kinase suppressor of RAS 1 (KSR1) have been shown to be upregulated in schwannoma to drive tumour growth. KSR1 has also been shown to interact with components of the CRL4-DCAF1 complex. We investigated the expression, interaction and therapeutic potential of targeting these proteins in Merlin deficient schwannoma and meningioma using a primary human cell model and relevant cell lines. We found that DCAF1 and KSR1 protein were overexpressed in schwannoma and meningioma and confirmed that targeting both DCAF1 and KSR1 in meningioma had additive effects on proliferation. We also identified that CRL4-DCAF1 facilitates KSR1 dependent RAF/Mitogen-activated protein kinase (MAPK)/ Extracellular signal regulated kinase (ERK) kinase (MEK)/ERK pathway activity. We showed MLN3651, a neddylation inhibitor that targets ubiquitin ligase activity, reduced proliferation and activated apoptosis in Merlin-deficient tumours. We also showed that Merlin-positive tumours were less sensitive to MLN3651 than Merlin-deficient tumours; therefore, MLN3651 sensitivity may be CRL4-DCAF1-dependent. Finally, combination of MLN3651 and the MEK1/2 inhibitor AZD6244 had additive effects, particularly in meningioma. Combinatorial therapy activated the Hippo pathway, inhibited RAF/MEK/ERK pathway activity and proliferation demonstrating that targeting the activity and downstream pathways of both DCAF1 and KSR1 represents an attractive novel therapeutic strategy in Merlin-deficient tumours.
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Worseck, Josephine Maria. "Characterization of phosphorylation-dependent interactions involving neurofibromin 2 (NF2, merlin) isoforms and the Parkinson protein 7 (PARK7, DJ1)." Doctoral thesis, Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2012. http://dx.doi.org/10.18452/16533.

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Veränderungen in phosphorylierungsabhängigen Signalwegen, Akkumulation von Proteinaggregaten im Gehirn und neuronaler Zelltod sind Neurodegenerationskennzeichen und Indikatoren für überlappende molekulare Mechanismen. Um Einblicke in die involvierten Signalwege zu erhalten, wurde mit Hilfe eines modifizierten Hefe-Zwei-Hybrid (Y2H)-Systems für 71 Proteine, die mit neurologischen Erkrankungen assoziiert sind, proteomweit nach Protein-Protein Interaktionen (PPIs) gesucht. Für 21 dieser Proteine wurden PPIs identifiziert. Das Gesamtnetzwerk besteht aus 79 Proteinen und 90 PPIs von denen 5 phosphorylierungsabhängig sind. Ein Teil dieser PPIs wurde in unabhängigen Interaktionsassays mit einer Validierungsrate von 66 % getestet. Der netzwerkbasierte Versuch verbindet erfolgreich neurologische Erkrankungen untereinander aber auch mit zellulären Prozessen. Ser/Thr-Kinase abhängige PPIs verknüpfen zum Beispiel das Parkinson Protein 7 (PARK7, DJ1) mit den E3 Ligase Komponenten ASB3 und RNF31 (HOIP). Die Funktion dieser Proteine bekräftigt den Zusammenhang zwischen dem Ubiquitin-Proteasom-System und der Parkinson Krankheit (PD). Neurofibromin 2 (NF2, merlin) Isoformen und PARK7 interagieren mit der regulatorischen PI3K Untereinheit p55-gamma (PIK3R3). Diese PPIs basieren auf Tyr-Kinase Aktivität im modifizierten Y2H System und funktionellen PIK3R3 pTyr-Erkennungsmodulen (SH2 Domänen) in co-IP und Venus PCA Versuchen. Dies verknüpft den PI3K/AKT Überlebenssignalweg mit zwei unterschiedlichen neurologischen Erkrankungsphenotypen: dem PD assoziierten neuronalen Zelltod und der Neurofibromatose Typ 2-assoziierten Tumorentstehung. Die vergleichende Beobachtung von PIK3R3, AOF2 (KDM1A, LSD1) Interaktionen auf NF2 Isoformlevel offenbart eine Bevorzugung von Isoform 7 bei zytoplasmatischer Lokalisation, wohingegen Isoform 1 PPIs an der Membran lokalisiert sind. Das modifizierungsabhängige und isoformspezifische PPI Netzwerk ermöglichte neue Hypothesen zu molekularen Pathomechanismen.
Alterations in phosphorylation-dependent signalling pathways, accumulation of aggregated proteins in the brain and neuronal apoptosis are common to neurodegeneration and implicate overlapping molecular mechanism. To gain insight into involved pathways, a modified yeast-two hybrid (Y2H) system was applied to screen 71 proteins associated with neurological disorders in a proteome-wide manner. For 21 of these proteins interactions were identified including 5 phosphorylation-dependent ones. In total, the network connected 79 proteins through 90 protein-protein interactions (PPIs). A fraction of these Y2H PPIs was tested in secondary interaction assays with a validation rate of 66 %. The described network-based approach successfully identified proteins associated with more than one disorder and cellular functions connected to specific disorders. In particular, the network revealed Ser/Thr kinase-dependent PPIs between the Parkinson protein 7 (PARK7, DJ1) and the E3 ligase components ASB3 and RNF31 (HOIP). The function of these proteins further substantiates the established connection between Parkinson’s disease (PD) and ubiquitination-mediated proteasome (dis)functions. Neurofibromin 2 (NF2, merlin) isoforms and PARK7 were identified as PI3K regulatory subunit p55-gamma (PIK3R3) interactors. These PPIs required Tyr kinase coexpression in the modified Y2H system and functional PIK3R3 pTyr-recognition modules (SH2 domains) in co-IP and Venus PCA experiments. This finding implicates the PI3K/AKT survival pathway in PD-associated neuronal apoptosis and Neurofibromatosis type 2-associated tumour formation. Investigation of PIK3R3, AOF2 (KDM1A, LSD1) and EMILIN1 PPIs on NF2 isoform level revealed preferential isoform 7 binding and cytoplasmic or membrane localisation of these PPIs for isoform 7 or 1, respectively. The generated modification-dependent and isoform-specific PPI network triggered many hypotheses on the molecular mechanisms implicated in neurological disorders.
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Sperka, Tobias [Verfasser]. "Ein neuer, regulierter Komplex des NF2-Tumorsuppressor-Genproduktes Merlin mit p190RhoGAP und p120RasGAP / Forschungszentrum Karlsruhe GmbH, Karlsruhe. Tobias Sperka." Karlsruhe : FZKA, 2006. http://d-nb.info/978199979/34.

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Boin, Alizée. "Le rôle de la voie Hippo dans la fonction suppresseur de tumeur associée au gène NF2 et la régulation de Yap par Merlin dans les cellules de Schwann." Thesis, Paris 11, 2014. http://www.theses.fr/2014PA112282.

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Les schwannomes sont des tumeurs bénignes se développant à partir d’une hyper-prolifération des cellules de Schwann suite à l’inactivation bi-allélique du gène NF2. Signe pathogonomique d’une pathologie rare et héréditaire, la Neurofibromatose de type 2 (NF2), ils peuvent aussi apparaître de façon sporadique. Hormis la chirurgie ou la radiothérapie, peu d’options pharmacologiques sont proposées aux patients porteurs de schwannomes, principalement à cause du peu de cibles thérapeutiques identifiées. Dans les cellules de Schwann, le phénotype cellulaire associé à la perte NF2 est une perte d’inhibition de la prolifération par le contact. Deux fonctions majeures de Merlin, produit de NF2, ont émergé au cours de ces dix dernières années. La première, démontrée par notre groupe, concerne la régulation de l’expression membranaire des récepteurs à activité tyrosine kinase (RTK) qui s’accumulent à la membrane plasmique des schwannomes humains. Le second implique Merlin dans la régulation de la voie de signalisation Hippo. Cette dernière, activée par le contact cellulaire réprime l’activité de deux co-facteurs de transcription, Yap et Taz, et régule ainsi et aussi l’inhibition de contact. Les mécanismes moléculaires par lesquels Merlin inhibe l’activité de Yap/Taz sont toutefois méconnus. Le but de nos études a été de déterminer une signature moléculaire associée à la croissance des schwannomes humains et l’importance relative de Yap/Taz. Dans une analyse protéomique à grande échelle sur des biopsies humaines, nous avons identifié à la fois l’activation spécifique de cinq RTKs que sont le PDGFRβ, Her2, Her3, Axl et Tie2 ainsi qu’une accumulation nucléaire spécifique de Yap. Nous montrons que sur la totalité des protéines étudiées, seules Yap, le PDGFRβ et P-Her3 corrèlent avec la prolifération des cellules de schwannomes humain. De plus, Yap induit la transcription des RTK activés (à l’exception de Tie2). Nous plaçons donc Yap au centre des mécanismes de régulation de la croissance des schwannomes humains et proposons que son inhibition pourrait représenter une nouvelle et prometteuse stratégie thérapeutique pour réduire la croissance de ces tumeurs. Nous apportons une nouvelle lecture des fonctions de Merlin, qui, par une potentielle interaction directe avec Yap, inhibe spécifiquement sa translocation dans le noyau indépendamment d’une régulation par la densité cellulaire ou par la voie Hippo. Par ailleurs, Merlin ne semble pas essentiel à l’activation de la voie Hippo dans les cellules de Schwann soulignant une fonction nouvelle et inattendue de Merlin dans la régulation de Yap et de la voie Hippo. Enfin nous avons étudié le rôle d’AmotL1, un puissant partenaire de Merlin et membre de la voie Hippo, dans la migration et la progression des cancers du sein. Nous mettons en évidence une fonction antagoniste de Merlin et AmotL1 dans la promotion de ces mécanismes soulignant une autre fonction nouvelle de Merlin en tant que suppresseur de la progression de cancers non associés à NF2
Schwannomas are benign tumors arising from Schwann cell hyper-proliferation under NF2 bi-allelic inactivation. They appear in the context of a rare hereditary disease called Neurofibromatosis type 2 (NF2) or in sporadic cases. To this day, surgery and radiotherapy remain the only options to treat these patients, mainly due to the lack of therapeutical targets identified. The NF2 loss associated cellular phenotype is the loss of cell contact inhibition. Two main functions of Merlin, the NF2 product, have emerged in the last decade. The first was shown by our group and consists in the accumulation of tyrosine kinase receptors (RTK) at the plasma membrane in schwannomas. The second involves Merlin in the regulation of the Hippo signaling pathway. This pathway is activated by cell contact and inactivates a couple of transcription co-factors, Yap and Taz, then participating in cell contact inhibition of proliferation. However, the mechanisms by which Merlin inactivates Yap and Taz remain unknown. In our studies, we aimed to determine both the molecular signature of human schwannomas taking advantage of a large proteomic study, and the relative importance of Yap in the tumor suppressor function of Merlin. We could show both a specific activation of five RTKs : PDGFRβ, Her 3, Her2, Axl and Tie2 and a specific nuclear accumulation of Yap in human schwannoma. Among all the protein studied, Yap, PDGFRβ and P-Her3 are the only ones to correlate with the proliferation of human schwannoma cells. Furthermore, the activated RTK (excepted Tie2) are transcriptional targets of Yap. Hence, we found Yap as a pivotal regulator of schwannoma growth and proposed its inhibition as a new and promising therapeutical target to reduce human schwannoma growth. In addition, we show that Merlin specifically inhibits Yap nuclear translocation into the nucleus of Schwann cells by a direct interaction which is independent from the regulation by cell density and by the Hippo pathway. Moreover, Merlin expression seems not to be essential for Hippo activation in Schwann cells which brings a new and unexpected role of Merlin in Yap and Hippo regulation. In the end, we studied the role of AmotL1, a strong Hippo partner of Merlin in the migration and progression of breast cancer. We could show an antagonist function of Merlin and AmotL1 in the promotion of these mechanisms highlighting a new progression suppressor function of Merlin in cancer which are not linked to NF2 mutations
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Books on the topic "NF2/Merlin"

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Cole, Banumathi Kuppusami. Membrane distribution of the NF2 tumor suppressor, Merlin. 2007.

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Morris, Zachary Scott. Regulation of EGFR by the NF2 tumor supressor, Merlin. 2009.

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Book chapters on the topic "NF2/Merlin"

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Mota, Mateus, Rajeev S. Samant, and Lalita A. Shevde. "Merlin (NF2)." In Encyclopedia of Signaling Molecules, 3089–100. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101780.

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Mota, Mateus, Rajeev S. Samant, and Lalita A. Shevde. "Merlin (NF2)." In Encyclopedia of Signaling Molecules, 1–11. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_101780-1.

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Hanemann, C. O. "Function of Merlin in Genesis of Tumours and Other Symptoms of NF2." In Neurofibromatoses, 167–76. Basel: KARGER, 2008. http://dx.doi.org/10.1159/000126615.

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Takeshima, Hideo, and Hideyuki Saya. "Detection of Binding Proteins of Merlin, the NF2 Tumor Suppressor Gene Product." In Brain Tumor, 269–76. Tokyo: Springer Japan, 1996. http://dx.doi.org/10.1007/978-4-431-66887-9_28.

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Ren, L., and C. Khanna. "Merlin/NF2 Tumor Suppressor and Ezrin–Radixin–Moesin (ERM) Proteins in Cancer Development and Progression." In Cancer Genome and Tumor Microenvironment, 93–115. New York, NY: Springer New York, 2009. http://dx.doi.org/10.1007/978-1-4419-0711-0_5.

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Conference papers on the topic "NF2/Merlin"

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Papadas, T., S. Nikou, H. Papadaki, and G. Tsinias. "Immunhistochemischer Nachweis von NF2/Merlin und LATS1 beim Larynxkarzinom." In Abstract- und Posterband – 90. Jahresversammlung der Deutschen Gesellschaft für HNO-Heilkunde, Kopf- und Hals-Chirurgie e.V., Bonn – Digitalisierung in der HNO-Heilkunde. Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0039-1685895.

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Papadas, T., S. Nikou, H. Papadaki, and G. Tsinias. "Immunohistochemical expression of NF2/Merlin and LATS1 in laryngeal carcinoma." In Abstract- und Posterband – 90. Jahresversammlung der Deutschen Gesellschaft für HNO-Heilkunde, Kopf- und Hals-Chirurgie e.V., Bonn – Digitalisierung in der HNO-Heilkunde. Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0039-1686041.

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Yi, Chunling, and Joseph Kissil. "Abstract 1128: The tumor suppressive function of Merlin/Nf2 is mediated by a novel tight junction-associated protein complex." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-1128.

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Cocciadiferro, Letizia, Vitale Miceli, Orazia M. Granata, and Giuseppe Carruba. "Abstract 1852: Merlin/NF2 is associated with elevated aromatase expression and estrogen formation in human liver tissues and liver cancer cells: An unifying model for hepatocellular carcinoma development and progression." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-1852.

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Reports on the topic "NF2/Merlin"

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Ramesh, Vijaya, and Anat Stemmer-Rachamimov. Role of Merlin/NF2 in mTOR Signaling and Meningioma Growth. Fort Belvoir, VA: Defense Technical Information Center, April 2012. http://dx.doi.org/10.21236/ada566365.

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Derewenda, Zygmunt W. Structure-Function Relationships in Merlin, the Product of the NF2 Causal Gene. Fort Belvoir, VA: Defense Technical Information Center, October 2004. http://dx.doi.org/10.21236/ada429527.

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Yogesha, Sollepura. Structure-Guided Insights into the Function of Merlin in Neurofibromatosis 2 (NF2). Fort Belvoir, VA: Defense Technical Information Center, August 2011. http://dx.doi.org/10.21236/ada608430.

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Yogesha, Sollepura. Structure-Guided Insights into the Function of Merlin in Neurofibromatosis 2 (NF2). Fort Belvoir, VA: Defense Technical Information Center, February 2011. http://dx.doi.org/10.21236/ada542511.

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McClatchey, Andrea I. Utilization of a NF2-Mutant Mouse Strain to Investigate the Cellular and Molecular Function of the NF2 Tumor Suppressor, Merlin. Fort Belvoir, VA: Defense Technical Information Center, October 2001. http://dx.doi.org/10.21236/ada399194.

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McClatchey, Andrea I. Utilization of a Nf2-Mutant Mouse strain to Investigate the Cellular and Molecular Function of the NF2 Tumor Suppressor, Merlin. Fort Belvoir, VA: Defense Technical Information Center, October 2002. http://dx.doi.org/10.21236/ada412822.

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McClatchey, Andrea I. Utilization of a NF2-Mutant Mouse Strain to Investigate the Cellular and Molecular Function of the NF2 Tumor Suppressor Merlin. Fort Belvoir, VA: Defense Technical Information Center, October 2003. http://dx.doi.org/10.21236/ada420954.

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Tomoda, Toshifumi, and Michael E. Barish. Novel Role of Merlin Tumor Suppressor in Autophagy and its Implication in Treating NF2-Associated Tumors. Fort Belvoir, VA: Defense Technical Information Center, April 2014. http://dx.doi.org/10.21236/ada608945.

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Tomoda, Toshifumi, Jr Jhung, Hirota Donald, and Yuki. Novel Role of Merlin Tumor Suppressor in Autophagy and its Implication in Treating NF2-Associated Tumors. Fort Belvoir, VA: Defense Technical Information Center, April 2012. http://dx.doi.org/10.21236/ada563285.

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Barish, Michael E., Toshifumi Tomoda, Akiko Sumitomo, and Yuki Hirota. Novel Role of Merlin Tumor Suppressor in Autophagy and its Implication in Treating NF2-Associated Tumors. Fort Belvoir, VA: Defense Technical Information Center, April 2013. http://dx.doi.org/10.21236/ada592192.

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