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Journal articles on the topic 'TRIM protein'

Author: Grafiati

Published: 1 April 2023

Last updated: 31 July 2025

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1

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 In owl monkeys, the B30.2 domain of Trim5 has been replaced by cyclophilin A (CypA) following a retrotransposition.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

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Xiao, Maolin, Jianjun Li, Qingyuan Liu, Xiangbiao He, Zongke Yang, and Delin Wang. "Expression and Role of TRIM2 in Human Diseases." BioMed Research International 2022 (August 23, 2022): 1–14. http://dx.doi.org/10.1155/2022/9430509.

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Tripartite motif (TRIM) protein family proteins contain more than 80 members in humans, and most of these proteins exhibit E3 ubiquitin ligase activity mediated through a RING finger domain. Their biological functions are very complex, and they perform diverse functions in cell evolution processes, such as intracellular signaling, development, apoptosis, protein quality control, innate immunity, autophagy, and carcinogenesis. Tripartite motif-containing protein 2 (TRIM2), a member of the TRIM superfamily, is an 81 kDa multidomain protein, also known as CMT2R or RNF86, located at 4q31.3. TRIM2

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Pauletto, Eleonora, Nils Eickhoff, Nuno Padrão, Christine Blattner, and Wilbert Zwart. "TRIMming Down Hormone-Driven Cancers: The Biological Impact of TRIM Proteins on Tumor Development, Progression and Prognostication." Cells 10, no. 6 (2021): 1517. http://dx.doi.org/10.3390/cells10061517.

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The tripartite motif (TRIM) protein family is attracting increasing interest in oncology. As a protein family based on structure rather than function, a plethora of biological activities are described for TRIM proteins, which are implicated in multiple diseases including cancer. With hormone-driven cancers being among the leading causes of cancer-related death, TRIM proteins have been described to portrait tumor suppressive or oncogenic activities in these tumor types. This review describes the biological impact of TRIM proteins in relation to hormone receptor biology, as well as hormone-indep

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Hage, Adam, Mikhaila Janes, and Sonja M. Best. "A No-Brainer! The Therapeutic Potential of TRIM Proteins in Viral and Central Nervous System Diseases." Viruses 17, no. 4 (2025): 562. https://doi.org/10.3390/v17040562.

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Tripartite motif (TRIM) proteins comprise an important class of E3 ubiquitin ligases that regulate numerous biological processes including protein expression, cellular signaling pathways, and innate immunity. This ubiquitous participation in fundamental aspects of biology has made TRIM proteins a focus of study in many fields and has illuminated the negative impact they exert when functioning improperly. Disruption of TRIM function has been linked to the success of various pathogens and separately to the occurrence and development of several neurodegenerative diseases, making TRIM proteins an

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Chiang, De Chen, and Beow Keat Yap. "TRIM25, TRIM28 and TRIM59 and Their Protein Partners in Cancer Signaling Crosstalk: Potential Novel Therapeutic Targets for Cancer." Current Issues in Molecular Biology 46, no. 10 (2024): 10745–61. http://dx.doi.org/10.3390/cimb46100638.

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Aberrant expression of TRIM proteins has been correlated with poor prognosis and metastasis in many cancers, with many TRIM proteins acting as key oncogenic factors. TRIM proteins are actively involved in many cancer signaling pathways, such as p53, Akt, NF-κB, MAPK, TGFβ, JAK/STAT, AMPK and Wnt/β-catenin. Therefore, this review attempts to summarize how three of the most studied TRIMs in recent years (i.e., TRIM25, TRIM28 and TRIM59) are involved directly and indirectly in the crosstalk between the signaling pathways. A brief overview of the key signaling pathways involved and their general c

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Wu, Wangxi, Jinyu Yang, Tian Yu, Zhuoling Zou, and Xuan Huang. "The Role and Mechanism of TRIM Proteins in Gastric Cancer." Cells 13, no. 24 (2024): 2107. https://doi.org/10.3390/cells13242107.

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Tripartite motif (TRIM) family proteins, distinguished by their N-terminal region that includes a Really Interesting New Gene (RING) domain with E3 ligase activity, two B-box domains, and a coiled-coil region, have been recognized as significant contributors in carcinogenesis, primarily via the ubiquitin–proteasome system (UPS) for degrading proteins. Mechanistically, these proteins modulate a variety of signaling pathways, including Wnt/β-catenin, PI3K/AKT, and TGF-β/Smad, contributing to cellular regulation, and also impact cellular activities through non-signaling mechanisms, including modu

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Bruyns, Eddy, Anne Marie-Cardine, Henning Kirchgessner та ін. "T Cell Receptor (TCR) Interacting Molecule (TRIM), A Novel Disulfide-linked Dimer Associated with the TCR–CD3–ζ Complex, Recruits Intracellular Signaling Proteins to the Plasma Membrane". Journal of Experimental Medicine 188, № 3 (1998): 561–75. http://dx.doi.org/10.1084/jem.188.3.561.

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The molecular mechanisms regulating recruitment of intracellular signaling proteins like growth factor receptor–bound protein 2 (Grb2), phospholipase Cγ1, or phosphatidylinositol 3-kinase (PI3-kinase) to the plasma membrane after stimulation of the T cell receptor (TCR)– CD3–ζ complex are not very well understood. We describe here purification, tandem mass spectrometry sequencing, molecular cloning, and biochemical characterization of a novel transmembrane adaptor protein which associates and comodulates with the TCR–CD3–ζ complex in human T lymphocytes and T cell lines. This protein was terme

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Liu, Yilin. "The Role of TRIM Proteins in Antiviral Defense." Highlights in Science, Engineering and Technology 74 (December 29, 2023): 1655–60. http://dx.doi.org/10.54097/a127xa83.

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The Tripartite motif (TRIM) protein family is classified among a cohort of E3 ubiquitin ligase families. A large percentage of TRIM proteins are E3 ubiquitin ligase active and take part in a number of cellular functions. By adding ubiquitin molecules to target proteins via a variety of techniques, it can change those proteins. The important role of the TRIM protein in controlling pattern recognition receptor signaling pathways and the defense mechanisms of mammals against viruses, with a focus on protecting the host from viral infections, has been clarified by recent study. In addition to trig

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Azuma, Kotaro, and Satoshi Inoue. "Efp/TRIM25 and Its Related Protein, TRIM47, in Hormone-Dependent Cancers." Cells 11, no. 15 (2022): 2464. http://dx.doi.org/10.3390/cells11152464.

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Increasing attention has been paid to the biological roles of tripartite motif-containing (TRIM) family proteins, which typically function as E3 ubiquitin ligases. Estrogen-responsive finger protein (Efp), a member of the TRIM family proteins, also known as TRIM25, was originally identified as a protein induced by estrogen and plays critical roles in promoting endocrine-related cancers, including breast cancer, endometrial cancer, and prostate cancer. The pathophysiological importance of Efp made us interested in the roles of other TRIM family proteins that share a similar structure with Efp.

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Nenasheva, V. V., E. A. Stepanenko, and V. Z. Tarantul. "Multi-Directional Mechanisms of Action of <i>TRIM</i> Family Genes in the Response of the Innate Immune System to Bacterial Infections (Review)." Biohimiâ 89, no. 7 (2024): 1229–47. https://doi.org/10.31857/s0320972524070076.

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Multigene TRIM family is an important component of the innate immune system. For a long time, it was believed that the main function of the genes of this family is the antiviral defense of the host organism. The question of their participation in the response of the immune system to bacterial invasion remained less studied. This review represents the first comprehensive analysis of the mechanisms of action of TRIM family genes in response to bacterial infections, which expands the existing understanding of the role of TRIM in the functioning of the innate immune system. Upon the infection with

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Esposito, Diego, Marios G. Koliopoulos, and Katrin Rittinger. "Structural determinants of TRIM protein function." Biochemical Society Transactions 45, no. 1 (2017): 183–91. http://dx.doi.org/10.1042/bst20160325.

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Tripartite motif (TRIM) proteins constitute one of the largest subfamilies of Really Interesting New Gene (RING) E3 ubiquitin ligases and contribute to the regulation of numerous cellular activities, including innate immune responses. The conserved TRIM harbours a RING domain that imparts E3 ligase activity to TRIM family proteins, whilst a variable C-terminal region can mediate recognition of substrate proteins. The knowledge of the structure of these multidomain proteins and the functional interplay between their constituent domains is paramount to understanding their cellular roles. To date

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Joshi, Mansi, Pranay Dey, and Abhijit De. "Recent advancements in targeted protein knockdown technologies—emerging paradigms for targeted therapy." Exploration of Targeted Anti-tumor Therapy 4, no. 6 (2023): 1227–48. http://dx.doi.org/10.37349/etat.2023.00194.

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A generalized therapeutic strategy for various disease conditions, including cancer, is to deplete or inactivate harmful protein targets. Various forms of protein or gene silencing molecules, e.g., small molecule inhibitors, RNA interference (RNAi), and microRNAs (miRNAs) have been used against druggable targets. Over the past few years, targeted protein degradation (TPD) approaches have been developed for direct degradation of candidate proteins. Among the TPD approaches, proteolysis targeting chimeras (PROTACs) have emerged as one of the most promising approaches for the selective eliminatio

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Fiorentini, Filippo, Diego Esposito, and Katrin Rittinger. "Does it take two to tango? RING domain self-association and activity in TRIM E3 ubiquitin ligases." Biochemical Society Transactions 48, no. 6 (2020): 2615–24. http://dx.doi.org/10.1042/bst20200383.

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TRIM proteins form a protein family that is characterized by a conserved tripartite motif domain comprising a RING domain, one or two B-box domains and a coiled-coil region. Members of this large protein family are important regulators of numerous cellular functions including innate immune responses, transcriptional regulation and apoptosis. Key to their cellular role is their E3 ligase activity which is conferred by the RING domain. Self-association is an important characteristic of TRIM protein activity and is mediated by homodimerization via the coiled-coil region, and in some cases higher

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Vu, Trung, Annaliese Fowler, and Nami McCarty. "Comprehensive Analysis of the Prognostic Significance of the TRIM Family in the Context of TP53 Mutations in Cancers." Cancers 15, no. 15 (2023): 3792. http://dx.doi.org/10.3390/cancers15153792.

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The p53 protein is an important tumor suppressor, and TP53 mutations are frequently associated with poor prognosis in various cancers. Mutations in TP53 result in a loss of p53 function and enhanced expression of cell cycle genes, contributing to the development and progression of cancer. Meanwhile, several tripartite motif (TRIM) proteins are known to regulate cell growth and cell cycle transition. However, the prognostic values between TP53 and TRIM family genes in cancer are unknown. In this study, we analyzed the relationship between the TP53 mutations and TRIM family proteins and evaluate

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Marzano, Flaviana, Mariano Francesco Caratozzolo, Graziano Pesole, Elisabetta Sbisà, and Apollonia Tullo. "TRIM Proteins in Colorectal Cancer: TRIM8 as a Promising Therapeutic Target in Chemo Resistance." Biomedicines 9, no. 3 (2021): 241. http://dx.doi.org/10.3390/biomedicines9030241.

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Colorectal cancer (CRC) represents one of the most widespread forms of cancer in the population and, as all malignant tumors, often develops resistance to chemotherapies with consequent tumor growth and spreading leading to the patient’s premature death. For this reason, a great challenge is to identify new therapeutic targets, able to restore the drugs sensitivity of cancer cells. In this review, we discuss the role of TRIpartite Motifs (TRIM) proteins in cancers and in CRC chemoresistance, focusing on the tumor-suppressor role of TRIM8 protein in the reactivation of the CRC cells sensitivity

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Sayyad, Zuberwasim, Dhiraj Acharya, and Michaela U. Gack. "TRIM Proteins: Key Regulators of Immunity to Herpesvirus Infection." Viruses 16, no. 11 (2024): 1738. http://dx.doi.org/10.3390/v16111738.

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Herpesviruses are ubiquitous DNA viruses that can establish latency and cause a range of mild to life-threatening diseases in humans. Upon infection, herpesviruses trigger the activation of several host antiviral defense programs that play critical roles in curbing virus replication and dissemination. Recent work from many groups has integrated our understanding of TRIM (tripartite motif) proteins, a specific group of E3 ligase enzymes, as pivotal orchestrators of mammalian antiviral immunity. In this review, we summarize recent advances in the modulation of innate immune signaling by TRIM pro

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Esposito, Jessica Elisabetta, Vincenzo De Iuliis, Francesco Avolio, et al. "Dissecting the Functional Role of the TRIM8 Protein on Cancer Pathogenesis." Cancers 14, no. 9 (2022): 2309. http://dx.doi.org/10.3390/cancers14092309.

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TRIM/RBCC are a large family of proteins that include more than 80 proteins, most of which act as E3 ligases and catalyze the direct transfer of Ubiquitin, SUMO and ISG15 on specific protein substrates. They are involved in oncogenesis processes and in cellular immunity. On this topic, we focus on TRIM8 and its multiple roles in tumor pathologies. TRIM8 inhibits breast cancer proliferation through the regulation of estrogen signaling. TRIM8 downregulation in glioma is involved in cell proliferation, and it is related to patients’ survival. Several studies suggested that TRIM8 regulates the p53

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Bhaduri, Utsa, and Giuseppe Merla. "Ubiquitination, Biotech Startups, and the Future of TRIM Family Proteins: A TRIM-Endous Opportunity." Cells 10, no. 5 (2021): 1015. http://dx.doi.org/10.3390/cells10051015.

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Ubiquitination is a post-translational modification that has pivotal roles in protein degradation and diversified cellular processes, and for more than two decades it has been a subject of interest in the biotech or biopharmaceutical industry. Tripartite motif (TRIM) family proteins are known to have proven E3 ubiquitin ligase activities and are involved in a multitude of cellular and physiological events and pathophysiological conditions ranging from cancers to rare genetic disorders. Although in recent years many kinds of E3 ubiquitin ligases have emerged as the preferred choices of big phar

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Zhang, Yongqi, Ying Guan, Shuxiang Wang, Chunyan Guan, and Xiaoli Liu. "Tripartite motif family – its role in tumor progression and therapy resistance: a review." Current Opinion in Oncology 36, no. 2 (2024): 102–14. http://dx.doi.org/10.1097/cco.0000000000001021.

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Purpose of review In this review, we summarized published articles on the role of tripartite motif (TRIM) family members in the initiation and development of human malignancies. Recent findings The ubiquitin-proteasome system (UP-S) plays a critical role in cellular activities, and UP-S dysregulation contributes to tumorigenesis. One of the key regulators of the UP-S is the tripartite motif TRIM protein family, most of which are active E3 ubiquitin ligases. TRIM proteins are critical for the biological functions of cancer cells, including migration, invasion, metastasis, and therapy resistance

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Crunkhorn, Sarah. "TRIM family protein protects the kidney." Nature Reviews Drug Discovery 14, no. 5 (2015): 312. http://dx.doi.org/10.1038/nrd4629.

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Chen, Yufang, Ziyan Li, Jingyao Zeng, Zhiyi Xu, and Meihua Wang. "TRIM 16 gene expression regulates the growth and metastasis of human esophageal cancer." Tropical Journal of Pharmaceutical Research 19, no. 10 (2020): 2047–53. http://dx.doi.org/10.4314/tjpr.v19i10.4.

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Purpose: To investigate the effect of tripartite membrane protein TRIM) 16 gene silencing on human esophageal cancer (KYSE-270) cell proliferation, invasion and metastasis.Methods: Short interfering RNA (siRNA) TRIM 16 silencing fragment was transfected into KYSE-270 cells. Transfection efficiency was determined using real-time quantitative polymerase chain reaction (qRT-PCR). Cell proliferation, invasiveness and migration were measured by 3-(4,5-dimethylthiazol2-yl)- 2,5-diphenyl tetrazolium bromide (MTT) assay, Transwell invasion assay, and scratch test, respectively. Protein expressions of

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Yondola, Mark A., and Patrick Hearing. "The Adenovirus E4 ORF3 Protein Binds and Reorganizes the TRIM Family Member Transcriptional Intermediary Factor 1 Alpha." Journal of Virology 81, no. 8 (2007): 4264–71. http://dx.doi.org/10.1128/jvi.02629-06.

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ABSTRACT One of the most interesting functions attributed to the adenovirus early region 4 open reading frame 3 (E4 ORF3) protein is its reorganization of promyelocytic leukemia (PML) protein nuclear bodies. These normally punctate structures are reorganized by E4 ORF3 into tracks that eventually surround viral replication centers. PML rearrangement is an evolutionarily conserved function of E4 ORF3, yet its cause and functional relevance remain mysteries. The E4 ORF3 protein coimmunoprecipitates with the PML protein, yet E4 ORF3 still forms tracks in cells that lack PML. The PML protein is a

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Shen, Sheng, Ran Yan, Zhanglian Xie, et al. "Tripartite Motif-Containing Protein 65 (TRIM65) Inhibits Hepatitis B Virus Transcription." Viruses 16, no. 6 (2024): 890. http://dx.doi.org/10.3390/v16060890.

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Tripartite motif (TRIM) proteins, comprising a family of over 100 members with conserved motifs, exhibit diverse biological functions. Several TRIM proteins influence viral infections through direct antiviral mechanisms or by regulating host antiviral innate immune responses. To identify TRIM proteins modulating hepatitis B virus (HBV) replication, we assessed 45 human TRIMs in HBV-transfected HepG2 cells. Our study revealed that ectopic expression of 12 TRIM proteins significantly reduced HBV RNA and subsequent capsid-associated DNA levels. Notably, TRIM65 uniquely downregulated viral pregeno

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Aizaz, Muhammad, Yusra Sajid Kiani, Maryum Nisar, Shijuan Shan, Rehan Zafar Paracha, and Guiwen Yang. "Genomic Analysis, Evolution and Characterization of E3 Ubiquitin Protein Ligase (TRIM) Gene Family in Common Carp (Cyprinus carpio)." Genes 14, no. 3 (2023): 667. http://dx.doi.org/10.3390/genes14030667.

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Tripartite motifs (TRIM) is a large family of E3 ubiquitin ligases that play an important role in ubiquitylation. TRIM proteins regulate a wide range of biological processes from cellular response to viral infection and are implicated in various pathologies, from Mendelian disease to cancer. Although the TRIM family has been identified and characterized in tetrapods, but the knowledge about common carp and other teleost species is limited. The genes and proteins in the TRIM family of common carp were analyzed for evolutionary relationships, characterization, and functional annotation. Phylogen

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Jacques, David, Cy Jeffries, Matthew Caines, et al. "TRIM protein domain topology and implications for antiviral immunity." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C243. http://dx.doi.org/10.1107/s2053273314097563.

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The tripartite motif (TRIM) proteins are a large family of >100 members, several of which have important roles in antiviral immunity and innate immune signaling. TRIM5α associates with incoming HIV-1 capsids, interfering with controlled disassembly and targeting them for degradation by the proteasome. TRIM21 is a cytosolic antibody receptor, which also targets incoming viral capsids for proteasomal degradation. TRIM25 is also involved in innate immunity, being essential for the ubiquitination of RIG-I. Recent positive selection analysis has predicted another 10 TRIM proteins with antiviral

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Fernandes, Alexandre P., Ana Águeda-Pinto, Ana Pinheiro, Hugo Rebelo, and Pedro J. Esteves. "Evolution of TRIM5 and TRIM22 in Bats Reveals a Complex Duplication Process." Viruses 14, no. 2 (2022): 345. http://dx.doi.org/10.3390/v14020345.

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The innate immunological response in mammals involves a diverse and complex network of many proteins. Over the last years, the tripartite motif-containing protein 5 (TRIM5) and 22 (TRIM22) have shown promise as restriction factors of a plethora of viruses that infect primates. Although there have been studies describing the evolution of these proteins in a wide range of mammals, no prior studies of the TRIM6/34/5/22 gene cluster have been performed in the Chiroptera order. Here, we provide a detailed analysis of the evolution of this gene cluster in several bat genomes. Examination of differen

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Hernández-Sarmiento, Lady Johana, Y. S. Tamayo-Molina, Juan Felipe Valdés-López, and Silvio Urcuqui-Inchima. "Interleukin 27, Similar to Interferons, Modulates Gene Expression of Tripartite Motif (TRIM) Family Members and Interferes with Mayaro Virus Replication in Human Macrophages." Viruses 16, no. 6 (2024): 996. http://dx.doi.org/10.3390/v16060996.

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Background: The Tripartite motif (TRIM) family includes more than 80 distinct human genes. Their function has been implicated in regulating important cellular processes, including intracellular signaling, transcription, autophagy, and innate immunity. During viral infections, macrophages are key components of innate immunity that produce interferons (IFNs) and IL27. We recently published that IL27 and IFNs induce transcriptional changes in various genes, including those involved in JAK-STAT signaling. Furthermore, IL27 and IFNs share proinflammatory and antiviral pathways in monocyte-derived m

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Salerno-Kochan, Anna, Andreas Horn, Pritha Ghosh, et al. "Molecular insights into RNA recognition and gene regulation by the TRIM-NHL protein Mei-P26." Life Science Alliance 5, no. 8 (2022): e202201418. http://dx.doi.org/10.26508/lsa.202201418.

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The TRIM-NHL protein Meiotic P26 (Mei-P26) acts as a regulator of cell fate in Drosophila. Its activity is critical for ovarian germline stem cell maintenance, differentiation of oocytes, and spermatogenesis. Mei-P26 functions as a post-transcriptional regulator of gene expression; however, the molecular details of how its NHL domain selectively recognizes and regulates its mRNA targets have remained elusive. Here, we present the crystal structure of the Mei-P26 NHL domain at 1.6 Å resolution and identify key amino acids that confer substrate specificity and distinguish Mei-P26 from closely re

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Sui, Baokun, Jiaxin Zheng, Zhenfang Fu, Ling Zhao, and Ming Zhou. "TRIM72 restricts lyssavirus infection by inducing K48-linked ubiquitination and proteasome degradation of the matrix protein." PLOS Pathogens 20, no. 2 (2024): e1011718. http://dx.doi.org/10.1371/journal.ppat.1011718.

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The tripartite motif (TRIM) protein family is the largest subfamily of E3 ubiquitin ligases, playing a crucial role in the antiviral process. In this study, we found that TRIM72, a member of the TRIM protein family, was increased in neuronal cells and mouse brains following rabies lyssavirus (RABV) infection. Over-expression of TRIM72 significantly reduced the viral titer of RABV in neuronal cells and mitigated the pathogenicity of RABV in mice. Furthermore, we found that TRIM72 over-expression effectively prevents the assembly and/or release of RABV. In terms of the mechanism, TRIM72 promotes

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Zhang, Jing-rui, Xin-xin Li, Wan-ning Hu, and Chang-yi Li. "Emerging Role of TRIM Family Proteins in Cardiovascular Disease." Cardiology 145, no. 6 (2020): 390–400. http://dx.doi.org/10.1159/000506150.

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Ubiquitination is one of the basic mechanisms of cell protein homeostasis and degradation and is accomplished by 3 enzymes, E1, E2, and E3. Tripartite motif-containing proteins (TRIMs) constitute the largest subfamily of RING E3 ligases, with >70 current members in humans and mice. These members are involved in multiple biological processes, including growth, differentiation, and apoptosis as well as disease and tumorigenesis. Accumulating evidence has shown that many TRIM proteins are associated with various cardiac processes and pathologies, such as heart development, signal transduction,

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Riddihough, Guy, and Stella M. Hurtley. "A protein to trim too-long telomeres." Science 355, no. 6325 (2017): 591.9–592. http://dx.doi.org/10.1126/science.355.6325.591-i.

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Kirchgessner, Henning, Jes Dietrich, Jeanette Scherer та ін. "The Transmembrane Adaptor Protein Trim Regulates T Cell Receptor (Tcr) Expression and Tcr-Mediated Signaling via an Association with the Tcr ζ Chain". Journal of Experimental Medicine 193, № 11 (2001): 1269–84. http://dx.doi.org/10.1084/jem.193.11.1269.

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T cell receptor (TCR)-interacting molecule (TRIM) is a recently identified transmembrane adaptor protein, which is exclusively expressed in T cells. Here we demonstrate that in mature T cells, TRIM preferentially interacts with the TCR via the TCR-ζ chains and to a lesser extent via the CD3-ε/γ heterodimer. Transient or stable overexpression of TRIM in Jurkat T cells results in enhancement of TCR expression on the cell surface and elevated induction of Ca2+ mobilization after T cell activation. TRIM-mediated upregulation of TCR expression results from inhibition of spontaneous TCR internalizat

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Eberhardt, Wolfgang, Kristina Haeussler, Usman Nasrullah, and Josef Pfeilschifter. "Multifaceted Roles of TRIM Proteins in Colorectal Carcinoma." International Journal of Molecular Sciences 21, no. 20 (2020): 7532. http://dx.doi.org/10.3390/ijms21207532.

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Colorectal cancer (CRC) is one of the most frequently diagnosed tumor in humans and one of the most common causes of cancer-related death worldwide. The pathogenesis of CRC follows a multistage process which together with somatic gene mutations is mainly attributed to the dysregulation of signaling pathways critically involved in the maintenance of homeostasis of epithelial integrity in the intestine. A growing number of studies has highlighted the critical impact of members of the tripartite motif (TRIM) protein family on most types of human malignancies including CRC. In accordance, abundant

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Guan, Xiaotao, Jun Li, Xingru Lü, Yu Dong, Weimin Chen, and Xuemei Li. "Expression, purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal NHL domain of human TRIM2." Acta Crystallographica Section F Structural Biology Communications 70, no. 5 (2014): 673–75. http://dx.doi.org/10.1107/s2053230x14008127.

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The tripartite motif-containing protein 2 (TRIM2) functions as an E3 ubiquitin ligase. Loss of function of TRIM2 has been shown to result in early-onset axonal neuropathy. As a member of the TRIM–NHL family of proteins, TRIM2 has a conserved modular architecture that includes N-terminal RING finger and B-box domains, a middle coiled-coil domain and a C-terminal NHL domain. To characterize the functional role of its NHL domain from the perspective of structural biology, a truncation of human TRIM2 (residues 465–744) was expressed, purified and crystallized. Rod-shaped crystals were obtained tha

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Basu-Shrivastava, Meenakshi, Alina Kozoriz, Solange Desagher, and Iréna Lassot. "To Ubiquitinate or Not to Ubiquitinate: TRIM17 in Cell Life and Death." Cells 10, no. 5 (2021): 1235. http://dx.doi.org/10.3390/cells10051235.

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TRIM17 is a member of the TRIM family, a large class of RING-containing E3 ubiquitin-ligases. It is expressed at low levels in adult tissues, except in testis and in some brain regions. However, it can be highly induced in stress conditions which makes it a putative stress sensor required for the triggering of key cellular responses. As most TRIM members, TRIM17 can act as an E3 ubiquitin-ligase and promote the degradation by the proteasome of substrates such as the antiapoptotic protein MCL1. Intriguingly, TRIM17 can also prevent the ubiquitination of other proteins and stabilize them, by bin

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Li, Chuanyou. "Gene Expression Profiling of TRIM Family in Individuals with Latent versus Active Tuberculosis and Reveals Potential Biomarkers for Diagnosis." Journal of Immunology 202, no. 1_Supplement (2019): 190.65. http://dx.doi.org/10.4049/jimmunol.202.supp.190.65.

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Abstract Tripartite motif (TRIM) protein family plays important regulatory roles in innate immune and inflammatory responses. Their dysregulation causes several diseases classified as virus infective diseases, cancers, immunological diseases, neuropsychiatric disorders, or developmental disorders. Nevertheless, the role and function of many members of TRIM family in tuberculosis (TB) remains largely unknown. Our study employed qRT-PCR to first profile the mRNA expression levels of 72 members of TRIM family in patients with active TB, latent tuberculosis infection (LTBI) and healthy individuals

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Stoll, Guido A., Shun-ichiro Oda, Zheng-Shan Chong, Minmin Yu, Stephen H. McLaughlin, and Yorgo Modis. "Structure of KAP1 tripartite motif identifies molecular interfaces required for retroelement silencing." Proceedings of the National Academy of Sciences 116, no. 30 (2019): 15042–51. http://dx.doi.org/10.1073/pnas.1901318116.

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Transcription of transposable elements is tightly regulated to prevent genome damage. KRAB domain-containing zinc finger proteins (KRAB-ZFPs) and KRAB-associated protein 1 (KAP1/TRIM28) play a key role in regulating retrotransposons. KRAB-ZFPs recognize specific retrotransposon sequences and recruit KAP1, inducing the assembly of an epigenetic silencing complex, with chromatin remodeling activities that repress transcription of the targeted retrotransposon and adjacent genes. Our biophysical and structural data show that the tripartite motif (TRIM) of KAP1 forms antiparallel dimers, which furt

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D'Amico, Francesca, Rishov Mukhopadhyay, Huib Ovaa, and Monique P. C. Mulder. "Targeting TRIM Proteins: A Quest towards Drugging an Emerging Protein Class." ChemBioChem 22, no. 12 (2021): 2011–31. http://dx.doi.org/10.1002/cbic.202000787.

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Jimenez-Moyano, Esther, Alba Ruiz, Henrik N. Kløverpris, et al. "Nonhuman TRIM5 Variants Enhance Recognition of HIV-1-Infected Cells by CD8+T Cells." Journal of Virology 90, no. 19 (2016): 8552–62. http://dx.doi.org/10.1128/jvi.00819-16.

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ABSTRACTTripartite motif-containing protein 5 (TRIM5) restricts human immunodeficiency virus type 1 (HIV-1) in a species-specific manner by uncoating viral particles while activating early innate responses. Although the contribution of TRIM5 proteins to cellular immunity has not yet been studied, their interactions with the incoming viral capsid and the cellular proteasome led us to hypothesize a role for them. Here, we investigate whether the expression of two nonhuman TRIM5 orthologs, rhesus TRIM5α (RhT5) and TRIM-cyclophilin A (TCyp), both of which are potent restrictors of HIV-1, could enh

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Williams, Felix Preston, Kevin Haubrich, Cecilia Perez-Borrajero, and Janosch Hennig. "Emerging RNA-binding roles in the TRIM family of ubiquitin ligases." Biological Chemistry 400, no. 11 (2019): 1443–64. http://dx.doi.org/10.1515/hsz-2019-0158.

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Abstract TRIM proteins constitute a large, diverse and ancient protein family which play a key role in processes including cellular differentiation, autophagy, apoptosis, DNA repair, and tumour suppression. Mostly known and studied through the lens of their ubiquitination activity as E3 ligases, it has recently emerged that many of these proteins are involved in direct RNA binding through their NHL or PRY/SPRY domains. We summarise the current knowledge concerning the mechanism of RNA binding by TRIM proteins and its biological role. We discuss how RNA-binding relates to their previously descr

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Jensen, Kirsten, Carol Shiels, and Paul S. Freemont. "PML protein isoforms and the RBCC/TRIM motif." Oncogene 20, no. 49 (2001): 7223–33. http://dx.doi.org/10.1038/sj.onc.1204765.

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Huang, Yisha, Jiajia Xuan, Jiayan Liang, et al. "A TRIM Family-Based Strategy for TRIMCIV Target Prediction in a Pan-Cancer Context with Multi-Omics Data and Protein Docking Integration." Biology 14, no. 7 (2025): 742. https://doi.org/10.3390/biology14070742.

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The TRIM CIV subfamily, distinguished by its C-terminal PRY-SPRY domains, constitutes nearly half of the human TRIM family and plays pivotal roles in cancer progression through ubiquitination. Identifying TRIM CIV substrates and interactors has emerged as a critical approach for elucidating tumorigenesis. Current protein–protein interaction (PPI) prediction models face challenges, including an inherent deficiency of negative datasets, biased feature integration, and the absence of a cancer-specific interaction context. To achieve the precise identification of TRIMCIV targets, we developed TRIM

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Kar, Alak Kanti, Felipe Diaz-Griffero, Yuan Li, Xing Li та Joseph Sodroski. "Biochemical and Biophysical Characterization of a Chimeric TRIM21-TRIM5α Protein". Journal of Virology 82, № 23 (2008): 11669–81. http://dx.doi.org/10.1128/jvi.01559-08.

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ABSTRACT The tripartite motif (TRIM) protein, TRIM5α, is an endogenous factor in primates that recognizes the capsids of certain retroviruses after virus entry into the host cell. TRIM5α promotes premature uncoating of the capsid, thus blocking virus infection. Low levels of expression and tendencies to aggregate have hindered the biochemical, biophysical, and structural characterization of TRIM proteins. Here, a chimeric TRIM5α protein (TRIM5Rh-21R) with a RING domain derived from TRIM21 was expressed in baculovirus-infected insect cells and purified. Although a fraction of the TRIM5Rh-21R pr

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Ylinen, Laura M. J., Zuzana Keckesova, Benjamin L. J. Webb, Robert J. M. Gifford, Timothy P. L. Smith, and Greg J. Towers. "Isolation of an Active Lv1 Gene from Cattle Indicates that Tripartite Motif Protein-Mediated Innate Immunity to Retroviral Infection Is Widespread among Mammals." Journal of Virology 80, no. 15 (2006): 7332–38. http://dx.doi.org/10.1128/jvi.00516-06.

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ABSTRACT Lv1/TRIM5α (tripartite motif 5α) has recently emerged as an important factor influencing species-specific permissivity to retroviral infection in a range of primates, including humans. Old World monkey TRIM5α blocks human immunodeficiency virus type 1 (HIV-1) infectivity, and the human and New World monkey TRIM5α proteins are inactive against HIV-1 but active against divergent murine (N-tropic murine leukemia virus [MLV-N]) and simian (simian immunodeficiency virus from rhesus macaque [SIVmac]) retroviruses, respectively. Here we demonstrate antiviral activity of the first nonprimate

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Kölsch, Uwe, Börge Arndt, Dirk Reinhold, et al. "Normal T-Cell Development and Immune Functions in TRIM-Deficient Mice." Molecular and Cellular Biology 26, no. 9 (2006): 3639–48. http://dx.doi.org/10.1128/mcb.26.9.3639-3648.2006.

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ABSTRACT The transmembrane adaptor molecule TRIM is strongly expressed within thymus and in peripheral CD4+ T cells. Previous studies suggested that TRIM is an integral component of the T-cell receptor (TCR)/CD3 complex and might be involved in regulating TCR cycling. To elucidate the in vivo function of TRIM, we generated TRIM-deficient mice by homologous recombination. TRIM−/− mice develop normally and are healthy and fertile. However, the animals show a mild reduction in body weight that appears to be due to a decrease in the size and/or cellularity of many organs. The morphology and anatom

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Sharma, Mona, Ke Liu, Jianchao Wei, Zhiyong Ma, and Yafeng Qiu. "Mechanistic Role of TRIM26 in Viral Infection and Host Defense." Genes 15, no. 11 (2024): 1476. http://dx.doi.org/10.3390/genes15111476.

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Tripartite motif protein 26 (TRIM26) is an E3 ubiquitin ligase and a member of the TRIM family. Similar to other TRIM proteins, TRIM26 consists of three domains, collectively termed RBCC: a Really Interesting New Gene (RING) domain, one B-Box domain, and a C terminal domain consisting of a PRY/SPRY domain. The PRY/SPRY domain exhibits relatively higher conservation compared with the RING and B-Box domains, suggesting potentially similar roles across TRIM26 proteins from various species. TRIM26 either directly interacts with viral proteins or modulates immune responses to engage with a viral in

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O'Connor, Christopher, Thomas Pertel, Seth Gray та ін. "p62/Sequestosome-1 Associates with and Sustains the Expression of Retroviral Restriction Factor TRIM5α". Journal of Virology 84, № 12 (2010): 5997–6006. http://dx.doi.org/10.1128/jvi.02412-09.

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ABSTRACT TRIM5 proteins mediate a potent block to the cross-species transmission of retroviruses, the most well known being the TRIM5α protein from rhesus macaques, which potently inhibits human immunodeficiency virus type 1 (HIV-1) infection. This restriction occurs at an early stage in the replication cycle and is mediated by the binding of TRIM5 proteins to determinants present in the retroviral capsid. TRIM5α, as well as other TRIM family proteins, has been shown to be regulated by interferons (IFN). Here we show that TRIM5α associates with another IFN-induced gene, sequestosome-1/p62 (p62

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Keown, Jeremy R., Joy Yang, Moyra M. Black, and David C. Goldstone. "The RING domain of TRIM69 promotes higher-order assembly." Acta Crystallographica Section D Structural Biology 76, no. 10 (2020): 954–61. http://dx.doi.org/10.1107/s2059798320010499.

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Members of the TRIM protein family have been shown to inhibit a range of viral infections. Recently, TRIM69 was identified as a potent inhibitor of Vesicular stomatitis Indiana virus infection, with its inhibition being dependent upon multimerization. Using SEC-MALLS analysis, it is demonstrated that the assembly of TRIM69 is mediated through the RING domain and not the Bbox domain as has been shown for other TRIM proteins. Using X-ray crystallography, the structure of the TRIM69 RING domain has been determined to a resolution of 2.1 Å, the oligomerization interface has been identified and reg

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Tozawa, Takafumi, Kohichi Matsunaga, Tetsuro Izumi, et al. "Ubiquitination-coupled liquid phase separation regulates the accumulation of the TRIM family of ubiquitin ligases into cytoplasmic bodies." PLOS ONE 17, no. 8 (2022): e0272700. http://dx.doi.org/10.1371/journal.pone.0272700.

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Many members of the tripartite motif (TRIM) family of ubiquitin ligases localize in spherical, membrane-free structures collectively referred to as cytoplasmic bodies (CBs) in a concentration-dependent manner. These CBs may function as aggresome precursors or storage compartments that segregate potentially harmful excess TRIM molecules from the cytosolic milieu. However, the manner in which TRIM proteins accumulate into CBs is unclear. In the present study, using TRIM32, TRIM5α and TRIM63 as examples, we demonstrated that CBs are in a liquid droplet state, resulting from liquid-liquid phase se

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Allouch, Awatef, Cristina Di Primio, Emanuele Alpi, et al. "The TRIM Family Protein KAP1 Inhibits HIV-1 Integration." Cell Host & Microbe 9, no. 6 (2011): 484–95. http://dx.doi.org/10.1016/j.chom.2011.05.004.

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