Academic literature on the topic 'TRIM18'
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Journal articles on the topic "TRIM18"
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Kimsa, Malgorzata W., B. Strzalka-Mrozik, M. C. Kimsa, et al. "Differential Expression of Tripartite Motif-Containing Family in Normal Human Dermal Fibroblasts in Response to Porcine Endogenous Retrovirus Infection." Folia Biologica 60, no. 3 (2014): 144–51. http://dx.doi.org/10.14712/fb2014060030144.
Full textAbstract:
Antiretroviral restriction factors may play an essential role in the safety of xenotransplantation. Therefore, the present study focused on investigation of the changes in the tripartite motif-containing family (TRIM) gene expression in normal human dermal fibroblasts with and without lipopolysaccharide stimulation in response to porcine endogenous retrovirus infection. Analysis of the expression profile of TRIMs was performed using oligonucleotide microarrays and QRT-PCR. Nine (TRIM1, TRIM2, TRIM5, TRIM14, TRIM16, TRIM18, TRIM22, TRIM27 and TRIM31) statistically significantly differentially expressed genes were found (P < 0.05, one-way ANOVA). In conclusion, comprehensive analysis of retroviral restriction factor gene expression in human dermal fibroblasts before and after porcine endogenous retrovirus infection with and without LPS stimulation may suggest association of the selected TRIMs with antiretroviral activity.
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Panhwar, S. N., C. Huang, Q. Luo, et al. "OVERVIEW OF CLASS-I TRIPARTITE MOTIF (TRIM) PROTEINS SPECIFICALLY TRIM67." Pakistan Journal of Agriculture, Agricultural Engineering and Veterinary Sciences 40, no. 2 (2024): 108–19. https://doi.org/10.47432/2024.40.2.8.
Full textAbstract:
The TRIM family is a group of genes expressed during embryogenesis. This review emphasized data on Class-I TRIM genes, including TRIM1, TRIM9, TRIM36, TRIM46, TRIM67, TRIM18, and TRIM76. This article will discuss the structure and function of these genes and their roles in various physiological processes such as embryonic development, and immune regulation. Class-I TRIM proteins develop as E3 ubiquitin ligases and work with E2 ubiquitin-conjugating enzymes. TRIM9 is expressed in the stem cells of mice and linked to various neuronal functions and neurological diseases. TRIM18 is found in microtubules and cellular filaments. TRIM36 is associated with neuro-pathological mutations, while TRIM46 controls microtubule organisation during axon formation. TRIM67 plays a significant role in neuritis outgrowth, lipid phosphate phosphatase, and colorectal and lung carcinomas. It also involves cell proliferation and induces morphological changes like neuronal differentiation. TRIM67 is important in Plasticity-related gene-1 (PRG-1). Deletion of prog-1 in mice results in epileptic seizures, indicating the significance of TRIM67 in brain development and growth. TRIM76 is associated with cardiac diseases. Further identification and characterisation of novel TRIM members will provide new insights into the functions of these essential proteins in health and disease.
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Yap, Melvyn W., Mark P. Dodding, and Jonathan P. Stoye. "Trim-Cyclophilin A Fusion Proteins Can Restrict Human Immunodeficiency Virus Type 1 Infection at Two Distinct Phases in the Viral Life Cycle." Journal of Virology 80, no. 8 (2006): 4061–67. http://dx.doi.org/10.1128/jvi.80.8.4061-4067.2006.
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ABSTRACT The Trim5α protein from several primates restricts retroviruses in a capsid (CA)-dependent manner. In owl monkeys, the B30.2 domain of Trim5 has been replaced by cyclophilin A (CypA) following a retrotransposition. Restriction of human immunodeficiency virus type 1 (HIV-1) by the resulting Trim5-CypA fusion protein depends on CA binding to CypA, suggesting both that the B30.2 domain might be involved in CA binding and that the tripartite RING motif, B-BOX, and coiled coil (RBCC) motif domain can function independently of the B30.2 domain in restriction. To investigate the potential of RBCCs from other Trims to participate in restricting HIV-1, CypA was fused to the RBCC of Trim1, Trim18, and Trim19 and tested for restriction. Despite low identity within the RBCC domain, all fusion proteins were found to restrict HIV-1 but not the nonbinding G89V mutant, indicating that the overall structure of RBCC and not its primary sequence was important for the restriction function. The critical interaction between CA and Trim-CypA appears to take place soon after viral entry. Quantitative PCR analysis of viral reverse transcriptase products revealed that the different fusion proteins block HIV-1 at two distinct stages of its life cycle, either prior to reverse transcription or just before integration. With Trim1 and Trim18, this timing is dependent on the length of the Trim component of the fusion protein. These observations suggest that restriction factor binding can have different mechanistic consequences.
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Tran, Pham-Tue-Hung, Mir Himayet Kabir, Naveed Asghar, et al. "Identification of TRIM21 and TRIM14 as Antiviral Factors Against Langat and Zika Viruses." Viruses 17, no. 5 (2025): 644. https://doi.org/10.3390/v17050644.
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Flaviviruses are usually transmitted to humans via mosquito or tick bites, whose infections may lead to severe diseases and fatality. During intracellular infection, they remodel the endoplasmic reticulum (ER) membrane to generate compartments scaffolding the replication complex (RC) where replication of the viral genome takes place. In this study, we purified the ER membrane fraction of virus infected cells to identify the proteins that were enriched during flavivirus infection. We found that tripartite motif-containing proteins (TRIMs) including TRIM38, TRIM21, and TRIM14 were significantly enriched during infection with mosquito-borne (West Nile virus strain Kunjin and Zika virus (ZIKV)) and tick-borne (Langat virus (LGTV)) flaviviruses. Further characterizations showed that TRIM21 and TRIM14 act as restriction factors against ZIKV and LGTV, while TRIM38 hinders ZIKV infection. These TRIMs worked as interferon-stimulated genes to mediate IFN-I response against LGTV and ZIKV infections. Restriction of ZIKV by TRIM14 and TRIM38 coincides with their colocalization with ZIKV NS3. TRIM14-mediated LGTV restriction coincides with its colocalization with LGTV NS3 and NS5 proteins. However, TRIM21 did not colocalize with ZIKV and LGTV NS3 or NS5 protein suggesting its antiviral activity is not dependent on direct targeting the viral enzyme. Finally, we demonstrated that overexpression of TRIM21 and TRIM14 restricted LGTV replication.
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De La Cruz-Herrera, Carlos F., Michael H. Tatham, Umama Z. Siddiqi, et al. "Changes in SUMO-modified proteins in Epstein-Barr virus infection identifies reciprocal regulation of TRIM24/28/33 complexes and the lytic switch BZLF1." PLOS Pathogens 19, no. 7 (2023): e1011477. http://dx.doi.org/10.1371/journal.ppat.1011477.
Full textAbstract:
SUMO modifications regulate the function of many proteins and are important in controlling herpesvirus infections. We performed a site-specific proteomic analysis of SUMO1- and SUMO2-modified proteins in Epstein-Barr virus (EBV) latent and lytic infection to identify proteins that change in SUMO modification status in response to EBV reactivation. Major changes were identified in all three components of the TRIM24/TRIM28/TRIM33 complex, with TRIM24 being rapidly degraded and TRIM33 being phosphorylated and SUMOylated in response to EBV lytic infection. Further experiments revealed TRIM24 and TRIM33 repress expression of the EBV BZLF1 lytic switch gene, suppressing EBV reactivation. However, BZLF1 was shown to interact with TRIM24 and TRIM33, resulting in disruption of TRIM24/TRIM28/TRIM33 complexes, degradation of TRIM24 and modification followed by degradation of TRIM33. Therefore, we have identified TRIM24 and TRIM33 as cellular antiviral defence factors against EBV lytic infection and established the mechanism by which BZLF1 disables this defence.
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Sebastian, Sarah, Christian Grütter, Caterina Strambio de Castillia та ін. "An Invariant Surface Patch on the TRIM5α PRYSPRY Domain Is Required for Retroviral Restriction but Dispensable for Capsid Binding". Journal of Virology 83, № 7 (2009): 3365–73. http://dx.doi.org/10.1128/jvi.00432-08.
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ABSTRACT TRIM5α is a retrovirus restriction factor in the host cell cytoplasm that blocks infection before provirus establishment. Restriction activity requires capsid (CA)-specific recognition by the PRYSPRY domain of TRIM5α. To better understand the restriction mechanism, nine charge-cluster-to-triple-alanine mutants in the TRIM5α PRYSPRY domain were assessed for CA-specific restriction activity. Five mutants distributed along the TRIM5α PRYSPRY primary sequence disrupted restriction activity against N-tropic murine leukemia virus and equine infectious anemia virus. Modeling of the TRIM5α PRYSPRY domain based on the crystal structures of PRYSPRY-19q13.4.1, GUSTAVUS, and TRIM21 identified a surface patch where disruptive mutants clustered. All mutants in this patch retained CA-binding activity, a reticular distribution in the cytoplasm, and steady-state protein levels comparable to those of the wild type. Residues in the essential patch are conserved in TRIM5α orthologues and in closely related paralogues. The same surface patch in the TRIM18 and TRIM20 PRYSPRY domains is the site of mutants causing Opitz syndrome and familial Mediterranean fever. These results indicate that, in addition to CA-specific binding, the PRYSPRY domain possesses a second function, possibly binding of a cofactor, that is essential for retroviral restriction activity by TRIM5α.
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Margalit, Liad, Carmit Strauss, Ayellet Tal, and Sharon Schlesinger. "Trim24 and Trim33 Play a Role in Epigenetic Silencing of Retroviruses in Embryonic Stem Cells." Viruses 12, no. 9 (2020): 1015. http://dx.doi.org/10.3390/v12091015.
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Embryonic stem cells (ESC) have the ability to epigenetically silence endogenous and exogenous retroviral sequences. Trim28 plays an important role in establishing this silencing, but less is known about the role other Trim proteins play. The Tif1 family is a sub-group of the Trim family, which possess histone binding ability in addition to the distinctive RING domain. Here, we have examined the interaction between three Tif1 family members, namely Trim24, Trim28 and Trim33, and their function in retroviral silencing. We identify a complex formed in ESC, comprised of these three proteins. We further show that when Trim33 is depleted, the complex collapses and silencing efficiency of both endogenous and exogenous sequences is reduced. Similar transcriptional activation takes place when Trim24 is depleted. Analysis of the H3K9me3 chromatin modification showed a decrease in this repressive mark, following both Trim24 and Trim33 depletion. As Trim28 is an identified binding partner of the H3K9 methyltransferase ESET, this further supports the involvement of Trim28 in the complex. The results presented here suggest that a complex of Tif1 family members, each of which possesses different specificity and efficiency, contributes to the silencing of retroviral sequences in ESC.
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Toka, Felix N., Kiera Dunaway, Matylda Mielcarska, Felicia Smaltz, and Magdalena Bossowska-Nowicka. "Expression pattern of TRIM genes in bovine macrophages stimulated with PAMPs." Journal of Immunology 198, no. 1_Supplement (2017): 129.7. http://dx.doi.org/10.4049/jimmunol.198.supp.129.7.
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Abstract In mammals innate immune mechanisms form the first line of defence against invading pathogens. Detection of viruses early in infection relies on intracellular receptors that sense microbial molecular patterns, subsequently leading to gene transcription that eventually produces IFN type I and II. Type I and II IFNs act to prevent replication of viruses. Tripartite Motif-containing (TRIM) proteins belong to a superfamily of RING-domain E3 ubiquitin ligases. They represent a novel class of antiviral molecules involved in innate immunity. These enzymes function in a wide variety of important cellular processes, particularly in innate antiviral response mechanisms. We studied the expression profile of 46 TRIM genes in a bovine macrophage cell line BoMac using RT2 PCR. PAMPs were used to imitate 2 important groups of pathogens. PolyI:C was used in place of viral dsRNA, LPS was used in place of Gram-negative bacteria, Pam3CSK4 was used in place of Gram-positive and negative bacteria, PolyI:C-LyoVec was used in place of viral sRNA and CpG was used in place of bacterial and viral DNA. Of the 46 TRIM genes, only 8 bovine TRIM genes were upregulated following stimulation of BoMac with individual PAMPs. PolyI:C induce upregulation of TRIM21, TRIM25 and TRIM56. All three TRIMs are known for their antiviral activity in human cell lines and mice. Pam3CSK4 and LPS, both upregulated TRIM10. PolyI:C-LyoVec upregulated TRIM9, TRIM40 and TRIM55. TRIM40 is an anti-inflammatory molecule. CpG upregulated TRIM40 and TRIM29. High expression of TRIM29 is regarded as a poor prognostic in many tumors, but no antimicrobial role has been described yet for TRIM29. Data will be discussed in the context of antiviral role of TRIMs in bovine viral infections.
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Rybakowska, Paulina, Nina Wolska, Arkadiusz Klopocki, et al. "Multiple TRIM proteins are targets of autoimmune response in lupus and Sjogren's syndrome. (HUM7P.308)." Journal of Immunology 192, no. 1_Supplement (2014): 184.17. http://dx.doi.org/10.4049/jimmunol.192.supp.184.17.
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Abstract TRIM21 belongs to the large family of tripartite motif containing proteins, and is often targeted by autoantibodies in lupus and Sjogren’s syndrome. Considering the significant protein domain homology between different TRIM proteins, we hypothesized that additional TRIM proteins are targets of autoimmunity. Based on the literature, in this study we investigated autoantibody responses to TRIM38. While 9% of lupus patients (n=149) had anti-TRIM38 antibodies, the incidence in Sjogren’s syndrome patients (n=150) was 12%, and in controls (n=50) it was 4%. With respect to TRIM21, the incidence was 62%, 68%, and 4% respectively. In Sjogren’s syndrome patients, the presence of anti-TRIM38 antibodies was closely associated with the increased severity of dry eye parameters. Epitope mapping studies showed that anti-TRIM21 antibodies reacted with the RING, Coiled coil and PRY-SPRY domains of TRIM21, whereas anti-TRIM38 antibodies reacted only with the Coiled coil and PRY-SPRY domains of TRIM38. All anti-TRIM38 positive patients also had anti-TRIM21 antibodies. Affinity purified anti-TRIM21 antibodies from lupus patients did not immunoprecipitate TRIM38, indicating lack of cross-reactivity at B cell level. However, we observed T cell cross-reactivity between TRIM21298-312 and TRIM38302-316. Our study suggests that immune responses to TRIM proteins can evolve through epitope spreading and contribute towards exacerbating the pathogenesis in autoimmune disorders.
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Agarwal, Neeraj, Sebastien Rinaldetti, Bassem B. Cheikh, et al. "TRIM28 is a transcriptional activator of the mutant TERT promoter in human bladder cancer." Proceedings of the National Academy of Sciences 118, no. 38 (2021): e2102423118. http://dx.doi.org/10.1073/pnas.2102423118.
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Bladder cancer (BC) has a 70% telomerase reverse transcriptase (TERT or hTERT in humans) promoter mutation prevalence, commonly at −124 base pairs, and this is associated with increased hTERT expression and poor patient prognosis. We inserted a green fluorescent protein (GFP) tag in the mutant hTERT promoter allele to create BC cells expressing an hTERT-GFP fusion protein. These cells were used in a fluorescence-activated cell sorting–based pooled CRISPR-Cas9 Kinome knockout genetic screen to identify tripartite motif containing 28 (TRIM28) and TRIM24 as regulators of hTERT expression. TRIM28 activates, while TRIM24 suppresses, hTERT transcription from the mutated promoter allele. TRIM28 is recruited to the mutant promoter where it interacts with TRIM24, which inhibits its activity. Phosphorylation of TRIM28 through the mTOR complex 1 (mTORC1) releases it from TRIM24 and induces hTERT transcription. TRIM28 expression promotes in vitro and in vivo BC cell growth and stratifies BC patient outcome. mTORC1 inhibition with rapamycin analog Ridaforolimus suppresses TRIM28 phosphorylation, hTERT expression, and cell viability. This study may lead to hTERT-directed cancer therapies with reduced effects on normal progenitor cells.
Dissertations / Theses on the topic "TRIM18"
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FERNANDES, LAGES INES. "Identification of Deubiquitinases (DUBs) associated with TRIM18/MID1." Doctoral thesis, Università degli Studi di Trieste, 2023. https://hdl.handle.net/11368/3042038.
Full textAbstract:
Ubiquitination is a post-translation modification process crucial to control protein degradation, localization, and activity. Tripartite Motif (TRIM) proteins participate in the ubiquitination process behaving as E3 ubiquitin ligases, responsible for the specific recognition of the substrate to be ubiquitinated. In the opposite process, Deubiquitinating enzymes (DUBs) can deconjugate the ubiquitin from the protein target. The antagonism of DUBs and E3s is essential to maintain protein homeostasis and signaling in cells.
In this project, we focused on TRIM18 (also named MID1) that when mutated causes the Xlinked form of Opitz G/BBB Syndrome (XLOS). MID1 controls the ubiquitin-mediated proteasomal degradation of the catalytic subunit of PP2A (PP2AC), one of the major phosphatases in the cell. Although MID1 mutations lead to an increase in PP2AC levels, the exact mechanism remains unclear. The main objective of this project was to find DUBs that
work in conjunction with MID1 rescuing the increase of PP2Ac level observed upon its mutations.
We specifically silenced 24 DUBs and analyzed the protein abundance of PP2AC. A decrease in the protein target levels will be indicative of a suitable DUB candidate to further study. We also made the opposite assay, overexpressing the same 24 DUBs, in this case, the DUBs overexpression should increase the PP2Ac protein. From both screenings, we found USP8 as a good candidate, which we confirmed in further assays, to modulate the PP2AC levels.
Consistently with the regulation of PP2AC, USP8 overexpression alters 4E-BP1 phosphorylation levels, affecting the mTOR pathway. To conclude USP8/MID1 is a functional pair controlling the degradative fate of PP2AC.
Furthermore, we noticed that in Mouse Embryo Fibroblasts from Mid1 KO, the Usp8 protein levels were up regulated. We found that USP8 levels are decreased in both the cytoplasmic and nuclear fractions when MID1 was overexpressed, recovering the USP8 levels when using the ΔRING form of MID1 (the non-catalytic form). Moreover, the nuclear fraction of PP2AC decreased when MID1 was overexpressed and increased when USP8 was overexpressed.
To conclude we discovered a new DUB/TRIM pair that works in a highly coordinated manner. MID1 controls the levels of USP8 in the cytoplasm and nucleus, and both MID1/USP8 control the levels of PP2AC, a mutual substrate, in the nucleus fraction. These findings will be relevant in basic knowledge and for the future investigation of potential therapeutic.<br>Ubiquitination is a post-translation modification process crucial to control protein degradation, localization, and activity. Tripartite Motif (TRIM) proteins participate in the ubiquitination process behaving as E3 ubiquitin ligases, responsible for the specific recognition of the substrate to be ubiquitinated. In the opposite process, Deubiquitinating enzymes (DUBs) can deconjugate the ubiquitin from the protein target. The antagonism of DUBs and E3s is essential to maintain protein homeostasis and signaling in cells.
In this project, we focused on TRIM18 (also named MID1) that when mutated causes the Xlinked form of Opitz G/BBB Syndrome (XLOS). MID1 controls the ubiquitin-mediated proteasomal degradation of the catalytic subunit of PP2A (PP2AC), one of the major phosphatases in the cell. Although MID1 mutations lead to an increase in PP2AC levels, the exact mechanism remains unclear. The main objective of this project was to find DUBs that
work in conjunction with MID1 rescuing the increase of PP2Ac level observed upon its mutations.
We specifically silenced 24 DUBs and analyzed the protein abundance of PP2AC. A decrease in the protein target levels will be indicative of a suitable DUB candidate to further study. We also made the opposite assay, overexpressing the same 24 DUBs, in this case, the DUBs overexpression should increase the PP2Ac protein. From both screenings, we found USP8 as a good candidate, which we confirmed in further assays, to modulate the PP2AC levels.
Consistently with the regulation of PP2AC, USP8 overexpression alters 4E-BP1 phosphorylation levels, affecting the mTOR pathway. To conclude USP8/MID1 is a functional pair controlling the degradative fate of PP2AC.
Furthermore, we noticed that in Mouse Embryo Fibroblasts from Mid1 KO, the Usp8 protein levels were up regulated. We found that USP8 levels are decreased in both the cytoplasmic and nuclear fractions when MID1 was overexpressed, recovering the USP8 levels when using the ΔRING form of MID1 (the non-catalytic form). Moreover, the nuclear fraction of PP2AC decreased when MID1 was overexpressed and increased when USP8 was overexpressed.
To conclude we discovered a new DUB/TRIM pair that works in a highly coordinated manner. MID1 controls the levels of USP8 in the cytoplasm and nucleus, and both MID1/USP8 control the levels of PP2AC, a mutual substrate, in the nucleus fraction. These findings will be relevant in basic knowledge and for the future investigation of potential therapeutic.
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ZANCHETTA, MELANIA EVA. "BRAF35 as target of MID1/TRIM18 E3 ligase activity." Doctoral thesis, Università degli Studi di Trieste, 2016. http://hdl.handle.net/11368/2908069.
Full textAbstract:
TRIM proteins are a family of ubiquitin E3 ligase enzymes characterized by the presence of a conserved N-terminus, the tripartite motif, which consists of a RING finger domain, two B-box motifs and an alpha-helical Coiled-coil region (RBCC). We focused our attention on TRIM18/MID1, the gene responsible for the X-linked form of Opitz G/BBB syndrome, a congenital disease characterized by defects in midline development and mental retardation. More recently, MID1 has also been found as overexpressed in some aggressive prostate cancers. The role of MID1 within the cell and the target(s) of its E3 ubiquitin activity during cellular processes are still not completely unravelled. In order to better investigate MID1 function and to find new cellular partners for this protein a two hybrid assay was performed in our laboratory. By means of this screening, BRCA2-Associated Factor 35 (BRAF35 or HMG20b) was identified as a novel MID1 interacting protein.
BRAF35 is a non-canonical High-Mobility-Group (HMG) protein that has a role in both neuronal differentiation and in cell cycle progression. Moreover BRAF35 sumoylation has been shown to be fundamental for its antineurogenic activity and is inhibited by the interaction with its homologue iBraf. The aim of the project was to characterise the functional role of MID1/BRAF35 interaction and to understand if MID1, as an E3 ubiquitin ligase, regulates BRAF35 during cytokinesis. The first evidence obtained from the preliminary screening was confirmed through MBP pull-down assay and co-immunoprecipitation, identifying the coiled-coil region of both proteins as responsible for the binding. We further investigated on a possible regulation of BRAF35 by the ubiquitin proteasome system and we recognized BRAF35 as a poly-ubiquitinated protein and we found that its abundance is regulated in a proteasome-dependent manner. In addition, overexpression of MID1 or its domain-deleted mutants altered BRAF35 stability and post-translational modification suggesting a MID1-dependent BRAF35 ubiquitination that implicates also K63-polyUb dependent signalling involvement.
Additionally, we found that MID1 and BRAF35 colocalize not only during interphase but also at the intercellular bridge during cytokinesis. Consistent with this observation, we observed a cell cycle-related regulation of BRAF35 protein level.
Moreover, MID1 depletion rescued the cytokinetic defect caused by BRAF35 silencing, leading to a decrease of binucleation, but promoted a blebbing phenotype in dividing cells. This indicates that a fine regulation of the two proteins for the completion of cytokinesis is required and suggests an additional and new role for MID1 in cytokinesis regulation.
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MASCARO, MARTINA. "Ruolo di TRIM18, gene che causa la sindrome di Opitz, nel controllo della ciliogenesi attraverso l'autofagia." Doctoral thesis, Università degli Studi di Trieste, 2021. http://hdl.handle.net/11368/2996095.
Full textAbstract:
TRIM18/MID1 è una E3-Ubiquitina ligasi appartenente alla famiglia di proteine TRIM che si localizza sui microtubuli. Le mutazioni con perdita di funzione nel gene MID1 sono state associate alla forma legata all'X della sindrome di Opitz, una malattia genetica caratterizzata da difetti nello sviluppo della linea mediana ventrale. All'interno della cellula, MID1 esiste come un complesso macromolecolare microtubulare, costituito da diversi interattori non tutti ancora identificati. Tra questi, α4 è una delle subunità regolatorie della proteina fosfatasi 2A (PP2A). È stato riportato che MID1 riduce il pool microtubulare dei livelli proteici della subunità catalitica di PP2A (PP2Ac), portando così all'ipofosforilazione dei suoi substrati. Le cellule prive di MID1 mostrano livelli aumentati di PP2Ac e una ridotta associazione tra mTOR e Raptor, portando a una downregulazione della via di segnalazione di mTORC1. Ciò suggerisce che MID1 può agire a monte della segnalazione di mTORC1. Tuttavia, i meccanismi patogenetici della sindrome di Opitz non sono ancora stati del tutto compresi, ma alcune caratteristiche cliniche sono condivise con un'altra classe di patologie in cui i geni che controllano le dinamiche del ciglio primario sono mutati, ovvero le ciliopatie. Detto questo, abbiamo ipotizzato che MID1 possa essere coinvolto nella regolazione dei processi in cui il ciglio primario è direttamente o indirettamente coinvolto.
Il ruolo di MID1 nel ciglio primario è stato studiato in una linea di cellule epiteliali umane e in fibroblasti di embrioni di topo (MEF) wild-type e Mid1-/Y. I dati mostrano che la overespressione di MID1 e la delezione di Mid1 nelle cellule di topo causano entrambe difetti della ciliogenesi e/o della lunghezza del ciglio primario, suggerendo un ruolo nella regolazione dell'assemblaggio di questo organello. Essendo le dinamiche del ciglio primario regolate dall'autofagia, controllata a sua volta anche attraverso la segnalazione di mTORC1, ci siamo chiesti se i difetti del ciglio primario causati da MID1 potessero essere dovute ad alterazioni nella via dell'autofagia. Analizzando gli stessi modelli cellulari, abbiamo osservato alterazioni nell'autofagia basale e nel flusso autofagico indotto dalla mancanza di nutrienti nelle cellule che overesprimono MID1 e nei MEF deleti per Mid1.
I miei risultati indicano che MID1 è un regolatore negativo sia della ciliogenesi che dell'allungamento del ciglio, a seconda del tipo di cellula e delle condizioni di coltura, nonché un regolatore dell'autofagia, come riportato per altri membri della famiglia TRIM. Presi insieme i nostri risultati possono far comprendere i meccanismi patogenetici della sindrome di Opitz e suggeriamo di considerare questa malattia come una nuova ciliopatia.<br>TRIM18/MID1 is an E3 Ubiquitin ligase belonging to the TRIM family of proteins that localises on microtubules. Loss-of-function mutations in the MID1 gene have been associated with the X-linked form of Opitz G/BBB syndrome, a genetic disorder characterised by defects in ventral midline development. Within the cell, MID1 exists as a microtubular macromolecular complex, consisting of several MID1 interactors not all identified yet. Among them, α4 is one of the regulatory subunits of Protein Phosphatase 2A (PP2A). MID1 has been reported to decrease the microtubular pool of PP2A catalytic subunit (PP2Ac) protein levels, thus leading to hypo-phosphorylation of its target proteins. MID1-lacking cells show increased levels of PP2Ac and a reduced association between mTOR and Raptor, leading to a downregulation of the mTORC1 signalling complex. This suggest that MID1 may act upstream of the mTORC1 signalling. Nevertheless, Opitz syndrome pathogenetic mechanisms have not been understood yet, but some clinical features are shared with another class of pathologies where genes controlling primary cilium dynamics are mutated, i.e. ciliopathies. Given this, we hypothesised that MID1 might be involved in the regulation of processes in which the primary cilium is directly or indirectly involved.
The role of MID1 in primary cilium was investigate in a human epithelial cell line and in wild-type and Mid1-/Y Mouse Embryo Fibroblasts (MEFs). The data show that MID1 overexpression and Mid1 depletion both cause impairment in primary ciliogenesis and/or primary cilia length, suggesting a role in the regulation of ciliary assembly. Being primary cilium dynamics regulated by autophagy, also controlled through mTORC1 signalling, we asked whether primary cilia impairments caused by MID1 could be due to misregulations in the autophagy pathway. By analysing the same cellular models, we observed alterations in basal autophagy and in the starvation-induced autophagy flux in MID1-overexpressing cells and in Mid1-/Y MEFs.
My results indicate that MID1 is a negative regulator of both ciliogenesis and ciliary elongation – depending on cell type and culture condition – as well as a regulator of autophagy pathway, as reported for other members of the TRIM family. Taken together our results can give new insights on the Opitz syndrome pathogenetic mechanisms and we can suggest to consider this disease as a new ciliopathy.
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Basu, Shrivastava Meenakshi. "Régulation de la stabilité de NFATc3 par SUMO et les E3 ubiquitine-ligases Trim39 et Trim17." Thesis, Montpellier, 2020. http://www.theses.fr/2020MONTT043.
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Les facteurs de transcription NFAT (facteur nucléaire des cellules T activées) jouent un rôle physiologique important dans le développement et le fonctionnement de nombreux organes, notamment dans le système immunitaire et le système nerveux. Par conséquent, leur dérégulation a été impliquée dans diverses maladies humaines telles que le cancer, les maladies neurodégénératives et les maladies auto-immunes. La régulation de l'activité de NFAT par translocation nucléo-cytoplasmique a été largement étudiée. En revanche, la régulation du niveau protéique de NFAT par le système ubiquitine-protéasome est encore mal comprise. Pourtant, les protéines NFAT ont une durée de vie courte et la régulation de leur stabilité est donc essentielle pour le contrôle de leur activité.Dans une étude précédente, mon groupe a montré que l'E3 ubiquitine-ligase Trim17 se lie à NFATc3 mais ne favorise pas son ubiquitination et tend plutôt à stabiliser la protéine. Les résultats préliminaires obtenus suggéraient que Trim39, un partenaire de Trim17, pourrait être une E3 ubiquitine-ligase pour NFATc3 et que la SUMOylation de NFATc3 modulait sa stabilité. L'objectif de ma thèse était donc de comprendre les mécanismes par lesquels Trim39, Trim17 et SUMO régulent la stabilité de NFATc3.Au cours de ma thèse, j'ai caractérisé Trim39 comme une E3 ubiquitine-ligase de NFATc3. En effet, mes résultats indiquent que la surexpression de Trim39, mais pas de son mutant inactif, induit l'ubiquitination de NFATc3 dans les cellules. En revanche, la déplétion de Trim39 endogène diminue le niveau d'ubiquitination de NFATc3. La protéine Trim39 recombinante induit directement l'ubiquitination de NFATc3 in vitro. De plus, la surexpression de Trim39 diminue les niveaux protéiques de NFATc3 alors que la déplétion de Trim39 les augmente. J'ai également montré que Trim17 inhibe l'ubiquitination de NFATc3 induite par Trim39, à la fois dans les cellules et in vitro. Trim17 agit à la fois en réduisant l'activité E3 ubiquitine-ligase intrinsèque de Trim39 et en empêchant l'interaction entre NFATc3 et Trim39. En outre, j'ai montré qu'un mutant de NFATc3 ne pouvant être SUMOylé est moins ubiquitiné et plus stable que la forme sauvage de NFATc3, ce qui suggère que la SUMOylation de NFATc3 est importante pour son ubiquitination et sa dégradation. En outre, j'ai identifié un motif d'interaction à SUMO (SIM) dans la séquence de Trim39, par lequel Trim39 lie les polymères de SUMO2. La mutation de ce SIM dans Trim39 ou des sites consensus de SUMOylation dans NFATc3 diminue l'interaction entre Trim39 et NFATc3, et l'ubiquitination de NFATc3 induite par Trim39. Ces résultats suggèrent fortement que Trim39 reconnaît et ubiquitine préférentiellement les formes SUMOylées de NFATc3 et agit donc comme une « E3 ubiquitine-ligase guidée par SUMO » (STUbL) pour NFATc3. Enfin, nous avons mesuré l'impact de ces mécanismes sur la fonction physiologique de NFATc3. J'ai tout d'abord montré que Trim39 diminue l'activité transcriptionnelle de NFATc3. En outre, à l'aide de cultures primaires de neurones granulaires du cervelet, nous avons montré que la mutation des sites de SUMOylation de NFATc3 et la déplétion de Trim39 endogène aggravent l'apoptose neuronale, probablement en stabilisant la protéine NFATc3. En conclusion, l’ensemble de mes données indiquent que Trim39 module l'apoptose neuronale en agissant comme une STUbL pour NFATc3 et en contrôlant sa stabilité<br>NFAT (Nuclear factor of activated T cells) transcription factors play important physiological roles in the development and function of many organs, notably in the immune system and nervous system. As a consequence, their dysregulation has been implicated in various human diseases such as cancer, neurodegenerative diseases, and auto-immune diseases. The regulation of NFAT activity by calcium-dependent nuclear-cytoplasmic shuttling has been extensively studied. In contrast, the regulation of NFAT protein level by the ubiquitin-proteasome system is still poorly understood. However, NFATs are short-lived proteins and regulation of their stability is critical for controlling their activity.In a previous study, my group has shown that the E3 ubiquitin-ligase Trim17 binds NFATc3 but does not promote its ubiquitination and rather stabilizes it. Preliminary results suggested that Trim39, a partner of Trim17, might be an E3 ubiquitin-ligase for NFATc3 and that SUMOylation of NFATc3 might modulate its stability. Therefore, the goal of my PhD was to understand the mechanisms through which Trim39, Trim17, and SUMO regulate the stability of NFATc3.During my PhD, I have characterized Trim39 as an E3 ubiquitin-ligase of NFATc3. Indeed, my results indicate that overexpression of Trim39, but not its inactive mutant, induces the ubiquitination of NFATc3 in cells. In contrast, silencing of endogenous Trim39 decreases the ubiquitination level of NFATc3. Recombinant Trim39 directly induces the ubiquitination of NFATc3 in vitro. Moreover, overexpression of Trim39 decreases the protein levels of NFATc3 whereas the silencing of Trim39 increases it. I have also shown that Trim17, which can bind Trim39, inhibits Trim39-mediated ubiquitination of NFATc3, both in cells and in vitro. Trim17 acts by both reducing the intrinsic E3 ubiquitin-ligase activity of Trim39 and by preventing the interaction between NFATc3 and Trim39. Furthermore, I found that a SUMOylation-deficient mutant of NFATc3 is less ubiquitinated and more stable than the wild type NFATc3, suggesting that SUMOylation of NFATc3 is important for its ubiquitination and degradation. Importantly, I identified one SUMO interacting motif (SIM) in the sequence of Trim39 through which Trim39 binds SUMO2 polymers via one of these SIMs. Mutation of this SIM in Trim39 or SUMOylation consensus sites in NFATc3 decreased the interaction between Trim39 and NFATc3, and the ubiquitination of NFATc3 mediated by Trim39. These results strongly suggest that Trim39 binds and ubiquitinates preferentially the SUMOylated forms of NFATc3 and therefore acts as a SUMO-targeted E3 ubiquitin-ligase (STUbL) for NFATc3. Finally, we have measured the impact of these mechanisms on the physiological function of NFATc3. I first found that Trim39 decreases the transcriptional activity of NFATc3. Furthermore, using primary cultures of cerebellar granule neurons as a model, we have shown that the mutation of the SUMOylation sites of NFATc3 and silencing of endogenous Trim39 enhances neuronal apoptosis, probably by stabilizing the NFATc3 protein. Taken together, these data indicate that Trim39 modulates neuronal apoptosis by acting as a STUbL for NFATc3 and by controlling its stability
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Buberl, Cilli Dana [Verfasser]. "Expressionsanalyse der putativen E3 Ligasen Trim23 und Trim7 in der frühen Neuralentwicklung von Xenopus laevis / Cilli Dana Buberl." Halle, 2017. http://d-nb.info/1137867698/34.
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Borle, Pawar Ankush [Verfasser], Norbert [Akademischer Betreuer] Frey, and Dennis [Gutachter] Schade. "Functional characterization of TRIM24 and TRIM32 proteins in the heart through their interaction with Dysbindin / Ankush Borle Pawar ; Gutachter: Dennis Schade ; Betreuer: Norbert Frey." Kiel : Universitätsbibliothek Kiel, 2019. http://d-nb.info/1220691259/34.
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Locke, Matthew. "TRIM32 in Genetic Disease." Thesis, University of Oxford, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.514962.
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VENUTO, SANTINA. "Dissecting the TRIM8 role in the pathogenesis of glioma." Doctoral thesis, Università degli Studi di Foggia, 2019. http://hdl.handle.net/11369/382357.
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I gliomi umani sono un gruppo eterogeneo di tumori cerebrali maligni primari, la cui patogenesi molecolare risulta ancora parzialmente sconosciuta. Pertanto, la comprensione dei meccanismi molecolari alla base della loro insorgenza e del loro decorso può portare a una migliore scelta di terapie appropriate e a migliori risultati prognostici, attraverso l'identificazione di nuovi geni specifici associati al glioma. Le proteine appartenenti alla famiglia “tripartite motif” (TRIM) sono coinvolte in diversi processi biologici, tra cui la regolazione trascrizionale, il controllo della progressione del ciclo cellulare, la proliferazione e il differenziamento cellulare. Alterazioni dell’espressione delle proteine TRIM sono associate a una varietà di patologie quali disturbi dello sviluppo, malattie infiammatorie e tumori. Tra le circa 80 proteine identificate appartenenti alla famiglia delle TRIM, TRIM8 è una E3 ubiquitina-ligasi coinvolta in vari processi patologici, quali ipertrofia, risposta antivirale, encefalopatia e sviluppo di diverse forme di cancro. Abbiamo recentemente identificato TRIM8 come un gene differenzialmente espresso nei gliomi, la cui espressione è correlata a un esito clinico sfavorevole nei pazienti con glioma. Per ottenere informazioni approfondite sulle funzioni di TRIM8, ne abbiamo studiato il “trascrittoma” e l' “interattoma” in cellule staminali neurali embrionali di topo, usando l’RNA-Sequencing e la spettrometria di massa, e successivamente analizzando i dati ottenuti mediante programmi bioinformatici. Sono state quindi eseguite analisi funzionali, biochimiche e cellulari, per esplorare il ruolo TRIM8 in differenti processi biologici. Il nostro studio ci ha permesso di identificare vie di segnale correlate alla neurotrasmissione e al sistema nervoso centrale (SNC), fornendo ulteriori prove dell'esistenza di una relazione funzionale tra TRIM8 e STAT3, con possibili implicazioni nello sviluppo e nella progressione del glioma. Abbiamo successivamente dimostrato che TRIM8 interagisce con KIFC1 e KIF11/Eg5, due importanti regolatori dell'assemblaggio del fuso mitotico e della riorganizzazione del citoscheletro. Approfondendo lo studio sul ruolo di TRIM8 nel processo mitotico, abbiamo verificato che TRIM8 localizza a livello del fuso mitotico durante la progressione della mitosi e svolge un ruolo chiave nella separazione dei centrosomi all’inizio della divisione mitotica, con un conseguente ritardo nella progressione della mitosi e un impatto sulla stabilità cromosomica. I nostri risultati confermano il ruolo di TRIM8 nelle funzioni cerebrali attraverso la deregolazione di geni appartenenti al pathway JAK-STAT e coinvolti in diverse funzioni del SNC. Inoltre, abbiamo identificato la funzione fisiologica di TRIM8 nello sviluppo del fuso mitotico, evidenziando un ruolo emergente di TRIM8 nella regolazione della mitosi.<br>Human gliomas are a heterogeneous group of primary malignant brain tumors, whose molecular pathogenesis is not yet solved. Therefore, understanding the molecular mechanisms underlying their aggressive behavior may lead to better management, appropriate therapies, and good outcomes through the identification of novel specific glioma-associated genes. Members of the tripartite motif (TRIM) proteins family are involved in many biological processes, including transcriptional regulation, cell proliferation and differentiation and cell cycle progression. Alterations of TRIM proteins are associated with a variety of pathologies like developmental disorders, inflammatory diseases and cancers. Among TRIMs protein family, TRIM8 encodes an E3 ubiquitin ligase involved in various pathological processes, including hypertrophy, antiviral defense, encephalopathy, and cancer development. We have identified TRIM8 as a gene aberrantly expressed in gliomas, whose expression correlates with unfavorable clinical outcome in glioma patients. To gain insights into the TRIM8 functions, we profiled the TRIM8 transcriptome and interactome in primary mouse embryonic neural stem cells using RNA-sequencing and proteomics, followed by bioinformatics analysis. Functional analysis, including biochemical and cellular assays were then performed to explore TRIM8 roles in different pathways. Our study firstly identified enriched pathways related to the neurotransmission and to the central nervous system (CNS) functions, providing additional evidence about the existence of a functional interactive crosstalk between TRIM8 and STAT3 with possible implications in the development and progression of glioma. Then, we found that TRIM8 interacts with KIFC1 and KIF11/Eg5, two master regulators of mitotic spindle assembly and cytoskeleton reorganization. Exploring the TRIM8 role in the mitotic spindle machinery, we showed that TRIM8 localizes at the mitotic spindle during mitosis and plays a role in centrosome separation at the beginning of mitosis with a subsequent delay of the mitotic progression and impact on chromosomal stability. Our results substantiate the role of TRIM8 in the brain functions through the deregulation of genes involved in different CNS-related pathways, including JAK-STAT. Moreover, we provided insights on the physiological function of TRIM8 in the mitotic spindle machinery, pointing to an emerging role for TRIM8 in the regulation of mitosis
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Crichton, Jennifer E. "The Role of the E3-ubiquitin Ligase Trim17 in the Mitochondrial Cell Death Pathway." Thèse, Université d'Ottawa / University of Ottawa, 2013. http://hdl.handle.net/10393/23715.
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The upregulation of apoptosis is a hallmark of several neurodegenerative disorders including ischemic stroke. In neurons, as in other cell types, Bax and tBid are critical regulators of the intrinsic pathway upstream of mitochondrial outer membrane permeabilization (MOMP) and caspase activation. The characterization of the molecular events that occur during the early stages is therefore extremely important from a therapeutic standpoint. Here I show that two independent genetic pilot screens looking for novel regulators of Bax activation identified a common hit in the E3 ubiquitin ligase Trim17. Knockdown of Trim17 was found to protect against tBid-induced death in primary cortical neurons and allowed for the maintenance of mitochondrial function and oxidative phosphorylation under this apoptotic stress. The RING-domain of Trim17 was found to interact with Opa1 in mouse brain extracts. Furthermore, Opa1 co-immunoprecipitated with exogenously expressed full-length Trim17 from HEK293 cells. Knockdown of Trim17 in neurons increased Opa1 protein levels under steady-state conditions. These results suggest that Trim17 regulates Bax-dependent apoptosis in neurons via the modulation of Opa1 levels.
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Simpson, Shmona. "Genetic, structural, and functional exploration of the restrictive capacity of TRIM proteins against immunodeficiency viruses." Thesis, University of Oxford, 2017. https://ora.ox.ac.uk/objects/uuid:1af588ba-603a-4f39-9443-bb1a95d983f5.
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HIV-2 differs from HIV-1 in that many infected people experience normal survival, whilst only 20% progress rapidly to AIDS. Understanding mechanisms of delayed HIV-2 disease progression could provide new insights into HIV control. The Caio Community Cohort was established in Guinea-Bissau in the setting of high HIV-2 prevalence. This thesis investigates the role of polymorphic host restriction factors of the TRIM family in HIV-2 outcome. TRIM proteins are a family of E3 ubiquitin-ligases, where closely-related TRIM5α and TRIM22 are thought to inhibit HIV-1 transcription, uncoating and budding. There was an association between TRIM5α amino acid substitution R136Q and reduced HIV-2 viral load/prolonged survival. Conversely, P479L was enriched among HIV-2 infected participants and progressors with CD4+ T cell decline. TRIM22 was highly polymorphic in this cohort, revealing three novel coding variants. Although most substitutions were located in the putative virus-interacting PRYSPRY domain, two in the coiled-coil, D155N and R242T, showed significant and divergent associations with survival. R242T was enriched in HIV-2 infected participants, who progressed to death at twice the rate of wild-type controls. In silico studies predicted D282, D360, and R321 of TRIM22 to be highly conserved, exposed residues, for which polymorphisms would be deleterious. When aligned with sequences from the potent HIV-1 restriction factor, rhesus macaque TRIM5α, TRIM22 substitutions R321K, T415I, and D360Y were spatially relevant to residues involved in HIV-1 restriction. The role of TRIM22 in HIV restriction was supported by in vitro pilot studies showing that TRIM22 was upregulated by HIV-1 infection in a lymphoid cell line and co-localised with the HIV-1 capsid protein p24. Overexpression of TRIM22 resulted in the restriction of VSV-G pseudotyped HIV-1 and SIVmac. The R242T substitution diminished TRIM22's restriction of HIV-1 and SIVmac: protein analysis suggested that this may be due to the inability of the R242T mutant to fully dimerise.
Books on the topic "TRIM18"
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David, Cameron-Smith, ed. Professor Trim's ultimate food energy guide. Allen & Unwin, 2003.
Find full textBook chapters on the topic "TRIM18"
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Gooch, Jan W. "Trimer." In Encyclopedic Dictionary of Polymers. Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_12131.
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Moss, Joel, and Martha Vaughan. "ARD1/TRIM23." In Encyclopedia of Signaling Molecules. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_644.
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Moss, Joel, Michaela U. Gack, and Martha Vaughan. "ARD1/TRIM23." In Encyclopedia of Signaling Molecules. Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4614-6438-9_644-1.
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Biswas-Fiss, Esther E., Stephanie Affet, Malissa Ha, et al. "ARD1/TRIM23." In Encyclopedia of Signaling Molecules. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_644.
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Hall, Christine M., Amaka C. Offiah, Francesca Forzano, Mario Lituania, Gen Nishimura, and Valérie Cormier-Daire. "Odontochondrodysplasia, TRIP11-Related." In Fetal and Perinatal Skeletal Dysplasias, 2nd ed. CRC Press, 2024. http://dx.doi.org/10.1201/9781003166948-44.
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Templeton, J. L. "Tungsten Trimer Synthesis." In Inorganic Reactions and Methods. John Wiley & Sons, Inc., 2007. http://dx.doi.org/10.1002/9780470145296.ch64.
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Grosso, Monica, Ilias Cheimariotis, Marcin Stepniak, Chiara Lodi, and Alessandro Marotta. "The Role of TRIMIS as a Policy Support Tool." In Lecture Notes in Mobility. Springer Nature Switzerland, 2025. https://doi.org/10.1007/978-3-031-85578-8_103.
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Abstract TRIMIS is a transport policy support tool that provides open-access information on transport research and innovation. It supports the vision of a clean, connected, and competitive European transport system and exemplifies the European Commission’s commitment to open science. TRIMIS collects, curates, analyses, and disseminates European and non-European data on transport research and innovation. It also analyses technology trends and research and innovation capacities in the transport sector. TRIMIS maintains an open database of almost 9,000 transport research and innovation projects and programmes, including Horizon Europe, Horizon 2020, FP7, Interreg, Connecting Europe Facility, and projects funded by Member States. This paper aims to provide an overall understanding of TRIMIS, its objectives, ecosystem, and details on how it contributes to supporting EU transport policy.
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Hirota, E., K. Kuchitsu, T. Steimle, J. Vogt, and N. Vogt. "39 C3H6F6 Difluoromethane trimer." In Molecules Containing Three or Four Carbon Atoms and Molecules Containing Five or More Carbon Atoms. Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-41504-3_40.
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Demaison, J. "143 H6O3 Water trimer." In Symmetric Top Molecules. Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-540-47532-3_145.
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Seong, Hongje, Seoung Wug Oh, Brian Price, Euntai Kim, and Joon-Young Lee. "One-Trimap Video Matting." In Lecture Notes in Computer Science. Springer Nature Switzerland, 2022. http://dx.doi.org/10.1007/978-3-031-19818-2_25.
Full textConference papers on the topic "TRIM18"
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Kim, Jungheon, and Dongkun Shin. "Delayed TRIM for Reducing Trim Overhead." In 2024 13th Non-Volatile Memory Systems and Applications Symposium (NVMSA). IEEE, 2024. http://dx.doi.org/10.1109/nvmsa63038.2024.10693664.
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Liu, Zichuan, Ke Wang, Mingyuan Wu, Lantao Yu, Klara Nahrstedt, and Xin Lu. "I-Matting: Improved Trimap-Free Image Matting." In 2024 IEEE International Conference on Multimedia and Expo (ICME). IEEE, 2024. http://dx.doi.org/10.1109/icme57554.2024.10687689.
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Alfaqeeh, Mosab. "TriMod Fusion for Multimodal Named Entity Recognition in Social Media." In 2024 34th International Conference on Collaborative Advances in Software and COmputiNg (CASCON). IEEE, 2024. https://doi.org/10.1109/cascon62161.2024.10837944.
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Zamani, Lachin, and Reza Azmi. "TriMAE: Fashion Visual Search with Triplet Masked Auto Encoder Vision Transformer." In 2024 14th International Conference on Computer and Knowledge Engineering (ICCKE). IEEE, 2024. https://doi.org/10.1109/iccke65377.2024.10874812.
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Metzler, M., IJ Diets, J. Hoyer, et al. "TRIM28 haploinsufficiency predisposes to Wilms tumor." In 32. Jahrestagung der Kind-Philipp-Stiftung für pädiatrisch onkologische Forschung. Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0039-1687131.
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Duan, Wenyang, Hongsen Zhang, Limin Huang, et al. "Numerical Simulation of Trim Optimization on Resistance Performance Based on CFD Method." In ASME 2019 38th International Conference on Ocean, Offshore and Arctic Engineering. American Society of Mechanical Engineers, 2019. http://dx.doi.org/10.1115/omae2019-96181.
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Abstract In response to the gradually stringent carbon emission requirements of the International Maritime Organization (IMO), the energy-saving methods of the shipping industry have received increasing attention. Today how to reduce fuel consumptions so as to lower carbon emissions to improve the economic and environmental benefits of ships has become a hot topic. As one of the most easily implemented energy-saving methods, trim optimization has caught more and more researchers’ eyes. In this paper, a commercial CFD software STAR-CCM+ was adopted to analyze the influence of trim on the resistance performance of VLCC ship mainly with fixed model method under various typical conditions of the design draft and the ballast draft respectively. The grid convergence was studied at the design draft and the typical numerical simulations were verified by the experimental results before carrying out various numerical simulations of trim optimization. Seven different kinds of trim conditions, which correspond to the changing process of the full scale ship from trimming by stern 4m to bow 4m, were simulated with 3 different speeds of design draft and ballast draft. The changes of total resistance, frictional resistance and residual resistance were analyzed to explore the effect of trims on the ship’s resistance. The variation of ship’s wetted surface area and waterplane area under different trim angles were studied. It was found that under the condition of low Froude number, both the simulation of free trim and sink method and the fixed model method can achieve good accuracy with the method of fixed model reducing the simulation time obviously. Both conditions of the design draft and ballast draft had a certain reduction effect of total resistance for trimming by bow properly, of which the change of frictional resistance is dominant in the decrease of total resistance at design draft while the change of residual resistance is the main cause at ballast draft. The optimum trims were found and the optimal total resistance reduction effects were evaluated. The optimal total resistance reduction effect increased with speed whether at the design or the ballast draft and the reduction effects were more obvious at ballast draft. Meanwhile, it was found that the changes of wetted surface area and the waterplane area with different trims were close to the variation tendency of the frictional resistance.
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Saetti, Umberto, and Jonathan Rogers. "A Motion Primitive Perspective on Rotorcraft Regime Recognition." In Vertical Flight Society 76th Annual Forum & Technology Display. The Vertical Flight Society, 2020. http://dx.doi.org/10.4050/f-0076-2020-16266.
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An alternative approach to regime recognition that is based on the notion of motion primitives is developed. The algorithm developed is non-causal and leverages the ideas of maneuvers and trims as defined in a motion primitive context. The algorithm functions in three major steps. Given a state and control input time history obtained from flight data, the first step consists of classifying the state and control time history into trim and maneuver segments. The second step leverages the information in the trim state and control vectors to classify each trim segment into a particular trim condition based on conditional (if-else-if) logic. The third step entails the classification of each maneuver segment (flown between two trim segments) as a particular maneuver condition. Importantly, maneuver classification leverages dynamic time warping in order to compensate for rate and time duration variations. Accuracy of the proposed algorithm is evaluated using SH-60B simulated flight data. Operation of the algorithm is also demonstrated using real-world piloted flight test data from a generic utility helicopter.
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Fong, Ka-Wing, Jonathan Zhao, Bin Zheng, and Jindan Yu. "Abstract 1521: Role of Trim28 in prostate cancer." 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.am2018-1521.
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Kirkby, David R., and David T. Delpy. "An optoelectronic cross-correlator using a gain modulated avalanche photodiode for measurement of the tissue temporal point spread function." In Advances in Optical Imaging and Photon Migration. Optica Publishing Group, 1996. http://dx.doi.org/10.1364/aoipm.1996.trit108.
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A small and relatively inexpensive optoelectronic cross-correlator, using an avalanche photodiode (APD) detector and without any moving parts has been developed to measure the temporal point spread function (TPSF) of light in tissue. From the TPSF, it is in principle possible to determine the optical properties of the tissue. Currently a temporal response of 275 ps full width half maximum (FWHM) has been achieved. Measurements of the TPSF of a tissue phantom using a synchroscan streak camera and the cross-correlator show excellent agreement, although the achievable signal to noise ratio currently limits the ability of the cross-correlator to detect the low intensity sections of a TPSF.
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Zhang, Changming, Mukherjee Subhas, Tucker-Burden Carol, Monica Chau, Jun Kong, and Daniel Brat. "Abstract 2516: TRIM8 modulates stem-like cells in glioblastoma." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-2516.
Full textReports on the topic "TRIM18"
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Strathman, James. Extraboard Management: TriMet Case Study. Portland State University Library, 2012. http://dx.doi.org/10.15760/trec.4.
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Kalberer, Jennifer L., and Jennifer C. Spanich. Evaluation of the TRIMAX 280 System. Defense Technical Information Center, 2002. http://dx.doi.org/10.21236/ada405546.
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Trumble, E. F. TRIMPWR: A post processor for TRIMHX. Office of Scientific and Technical Information (OSTI), 1989. http://dx.doi.org/10.2172/6975898.
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Trumble, E. F. Validation and verification summary report for GRIMHX and TRIMHX. Office of Scientific and Technical Information (OSTI), 1990. http://dx.doi.org/10.2172/10156331.
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Trumble, E. F. Validation and verification summary report for GRIMHX and TRIMHX. Office of Scientific and Technical Information (OSTI), 1990. http://dx.doi.org/10.2172/5038892.
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Fries, Joseph. Helicopter Trim Analysis. Defense Technical Information Center, 1996. http://dx.doi.org/10.21236/ada310293.
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Brooks, Stephen. Integrated Fields of Permanent Magnet Dipole Trims. Office of Scientific and Technical Information (OSTI), 2021. http://dx.doi.org/10.2172/1895098.
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Minden, M. L., and T. R. O'Meara. Range-Doppler, Target-Referencing Imaging Systems (RD-TRIMS). Defense Technical Information Center, 1990. http://dx.doi.org/10.21236/ada360123.
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Strathman, James, Joseph Broach, and Steve Callas. Evaluation of Short Duration Unscheduled Absences Among Transit Operators: TriMet Case Study. Portland State University Library, 2009. http://dx.doi.org/10.15760/trec.141.
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Mills, John R. An Introduction To PC-TRIM. U.S. Department of Agriculture, Forest Service, Pacific Northwest Research Station, 1989. http://dx.doi.org/10.2737/pnw-rn-491.
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