Relevant bibliographies by topics / IFITM-2

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Academic literature on the topic 'IFITM-2'

Author: Grafiati
Published: 10 March 2023
Last updated: 31 July 2025

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Journal articles on the topic "IFITM-2"

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Yu, Jingyou, and Shan-Lu Liu. "The Inhibition of HIV-1 Entry Imposed by Interferon Inducible Transmembrane Proteins Is Independent of Co-Receptor Usage." Viruses 10, no. 8 (2018): 413. http://dx.doi.org/10.3390/v10080413.

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Interferon inducible transmembrane proteins (IFITMs) are one of several IFN-stimulated genes (ISGs) that restrict entry of enveloped viruses, including flaviviruses, filoviruses and retroviruses. It has been recently reported that in U87 glioblastoma cells IFITM proteins inhibit HIV-1 entry in a co-receptor-dependent manner, that is, IFITM1 is more inhibitory on CCR5 tropic HIV-1 whereas IFITM2/3 confers a greater suppression of CXCR4 counterparts. However, how entry of HIV-1 with distinct co-receptor usage is modulated by different IFITM orthologs in physiologically relevant CD4+ T cells and
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Franz, Sergej, Fabian Pott, Thomas Zillinger, et al. "Human IFITM3 restricts chikungunya virus and Mayaro virus infection and is susceptible to virus-mediated counteraction." Life Science Alliance 4, no. 7 (2021): e202000909. http://dx.doi.org/10.26508/lsa.202000909.

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Interferon-induced transmembrane (IFITM) proteins restrict membrane fusion and virion internalization of several enveloped viruses. The role of IFITM proteins during alphaviral infection of human cells and viral counteraction strategies are insufficiently understood. Here, we characterized the impact of human IFITMs on the entry and spread of chikungunya virus and Mayaro virus and provide first evidence for a CHIKV-mediated antagonism of IFITMs. IFITM1, 2, and 3 restricted infection at the level of alphavirus glycoprotein-mediated entry, both in the context of direct infection and cell-to-cell
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Minakshi, Rinki. "Interferon-Induced Transmembrane Protein: A Moonlighting Protein Against SARS-CoV-2 Infection or in Support of Invasive Ductal Breast Carcinoma?" Asian Pacific Journal of Cancer Care 5, S1 (2020): 241–42. http://dx.doi.org/10.31557/apjcc.2020.5.s1.241-242.

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The interferon-induced transmembrane proteins (IFITMs), widely acting against invading viruses are ubiquitously expressed on the cellular membranes, were previously known for their prominent role in tumorigenesis. Studies productively showed that the entry restriction on SARS-CoV spike glycoprotein agreeably involved the action of frontier IFITM1, 2 and 3. On the contrary, overexpression of IFITM3 has been reported in Invasive ductal breast carcinoma (IDC) tissue specimens where lentivirus-delivered shRNA resulted in targeted silencing of IFITM3 mRNA expression. Despite acting protective again
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Mak, Nelly S. C., Jingyan Liu, Dan Zhang, et al. "Alternative splicing expands the antiviral IFITM repertoire in Chinese rufous horseshoe bats." PLOS Pathogens 20, no. 12 (2024): e1012763. https://doi.org/10.1371/journal.ppat.1012763.

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Species-specific interferon responses are shaped by the virus-host arms race. The human interferon-induced transmembrane protein (IFITM) family consists of three antiviral IFITM genes that arose by gene duplication. These genes restrict virus entry and are key players in antiviral interferon responses. The unique IFITM repertoires in different species influence their resistance to viral infections, but the role of IFITMs in shaping the enhanced antiviral immunity of reservoir bat species is unclear. Here, we identified an IFITM gene in Chinese rufous horseshoe bat, a natural host of severe acu
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Dimech, Christina, and Bhushan Nagar. "Towards a structural characterization of the IFIT antiviral complex." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C246. http://dx.doi.org/10.1107/s2053273314097538.

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Our first line of defense against viral pathogens is the innate immune system. Interferon-induced proteins with tetratricopeptide repeats (IFITs) are innate immune effector molecules that are thought to confer antiviral defense through the formation of the IFIT `Interactome', a multiprotein complex made up of IFIT1, IFIT2, IFIT3 and several other host factors1. Through IFIT1, this complex has the ability to distinguish self from non-self nucleic acids such as virus-derived RNA bearing 5´-triphosphate or viral mRNA lacking 2´-O methylation on the first two nucleotides1,2. We have limited inform
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Hickford, D., A. Pask, G. Shaw, and M. B. Renfree. "264. Primordial germ cell specification in a marsupial, the tammar wallaby." Reproduction, Fertility and Development 20, no. 9 (2008): 64. http://dx.doi.org/10.1071/srb08abs264.

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Primordial germ cells (PGCs) are the precursors of the gametes. In the mouse, PGCs are specified within the proximal epiblast in response to signals from the extraembryonic membranes during early gastrulation. Epiblast cells competent to form PGCs express Ifitm3. A subset of these cells then express Blimp1, a marker of PGC precursors. Once lineage-restricted, PGCs express Stella. Germ cells entering the gonads express VASA protein, which is a component of the germ plasm in animals in which germ cells are specified by the inheritance of maternal determinatives. Almost all of the research on mam
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Confort, Marie-Pierre, Maëva Duboeuf, Adrien Thiesson, et al. "IFITMs from Naturally Infected Animal Species Exhibit Distinct Restriction Capacities against Toscana and Rift Valley Fever Viruses." Viruses 15, no. 2 (2023): 306. http://dx.doi.org/10.3390/v15020306.

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Rift Valley Fever virus (RVFV) and Toscana virus (TOSV) are two pathogenic arthropod-borne viruses responsible for zoonotic infections in both humans and animals; as such, they represent a growing threat to public and veterinary health. Interferon-induced transmembrane (IFITM) proteins are broad inhibitors of a large panel of viruses belonging to various families and genera. However, little is known on the interplay between RVFV, TOSV, and the IFITM proteins derived from their naturally infected host species. In this study, we investigated the ability of human, bovine, and camel IFITMs to rest
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Campbell, Robert A., Jesse W. Rowley, Andrew S. Weyrich, and Matthew T. Rondina. "Surface Ifitms on Megakaryocytes and Platelets Regulate Fibrinogen Endocytosis Under Inflammatory Conditions." Blood 126, no. 23 (2015): 1034. http://dx.doi.org/10.1182/blood.v126.23.1034.1034.

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Abstract Background IFITM proteins (IFITM-1, -2, and -3) mediate cellular resistance to influenza, dengue, and other viruses. IFITM expression on human platelets has not been previously recognized. Our laboratory recently demonstrated that IFITMs are robustly expressed by human platelets and megakaryocytes after stimulation by pathogens and inflammatory mediators and restrict viral infection. IFITMs, which are interferon inducible, also mediate clathrin localization and associated protein endocytosis. Nevertheless, whether IFITMs regulate protein endocytosis by platelets and megakaryocytes rem
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Das, Tandrila, and Howard C. Hang. "Discovery and Characterization of IFITM S-Palmitoylation." Viruses 15, no. 12 (2023): 2329. http://dx.doi.org/10.3390/v15122329.

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Interferon-induced transmembrane proteins (IFITM1, 2 and 3) are important host antiviral defense factors. They are active against viruses like the influenza A virus (IAV), dengue virus (DENV), Ebola virus (EBOV), Zika virus (ZIKV) and severe acute respiratory syndrome coronavirus (SARS-CoV). In this review, we focus on IFITM3 S-palmitoylation, a reversible lipid modification, and describe its role in modulating IFITM3 antiviral activity. Our laboratory discovered S-palmitoylation of IFITMs using chemical proteomics and demonstrated the importance of highly conserved fatty acid-modified Cys res
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Smith, S. E., M. S. Gibson, R. S. Wash, et al. "Chicken Interferon-Inducible Transmembrane Protein 3 Restricts Influenza Viruses and LyssavirusesIn Vitro." Journal of Virology 87, no. 23 (2013): 12957–66. http://dx.doi.org/10.1128/jvi.01443-13.

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Interferon-inducible transmembrane protein 3 (IFITM3) is an effector protein of the innate immune system. It confers potent, cell-intrinsic resistance to infection by diverse enveloped viruses bothin vitroandin vivo, including influenza viruses, West Nile virus, and dengue virus. IFITM3 prevents cytosolic entry of these viruses by blocking complete virus envelope fusion with cell endosome membranes. Although the IFITM locus, which includesIFITM1, -2, -3, and -5, is present in mammalian species, this locus has not been unambiguously identified or functionally characterized in avian species. Her
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Dissertations / Theses on the topic "IFITM-2"

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D'Auria, Raffaella. "BAG3 extracellulare: target cellulari e molecolari." Doctoral thesis, Universita degli studi di Salerno, 2016. http://hdl.handle.net/10556/2355.

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2014 - 2015<br>Bcl-2-associated athanogene 3 (BAG3) belongs to the family of co-chaperone proteins that interact with the heat shock protein 70 (Hsp70) and is involved in a number of cellular processes including proliferation and apoptosis. BAG3 contains the BAG domain which interacts with the ATPase domain of Hsp70. BAG3 is also characterized by the presence of a WW domain, two conserved Ile-Pro-Val (IPV) motifs and a proline-rich (PXXP) repeat that mediate the binding to partners different from Hsp70. These diverse and multiple interactions underlie the ability of BAG3 to modulate major biol
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Conference papers on the topic "IFITM-2"

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"Welcome Message from the General Chair of IFITA 2010 - Volume 2." In 2010 International Forum on Information Technology and Applications (IFITA). IEEE, 2010. http://dx.doi.org/10.1109/ifita.2010.364.

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