Relevant bibliographies by topics / TRIM protein

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Academic literature on the topic 'TRIM protein'

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Published: 1 April 2023

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Journal articles on the topic "TRIM protein"

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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 (April 15, 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 In owl monkeys, the B30.2 domain of Trim5 has been replaced by cyclophilin A (CypA) following a retrotransposition.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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Esposito, Diego, Marios G. Koliopoulos, and Katrin Rittinger. "Structural determinants of TRIM protein function." Biochemical Society Transactions 45, no. 1 (February 8, 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, available structural information on TRIM proteins is still largely restricted to subdomains of many TRIMs in isolation. Nevertheless, applying a combination of structural, biophysical and biochemical approaches has recently allowed important progress to be made towards providing a better understanding of the molecular features that underlie the function of TRIM family proteins and has uncovered an unexpected diversity in the link between self-association and catalytic activity.
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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 functions as an E3 ubiquitin ligase. Current studies have shown that TRIM2 can play roles in neuroprotection, neuronal rapid ischemic tolerance, antiviral responses, neurological diseases, etc. Moreover, based on some studies in tumors, TRIM2 regulates tumor proliferation, migration, invasion, apoptosis, and drug resistance through different mechanisms and plays a critical role in tumor occurrence and development. This review is aimed at providing a systematic and comprehensive summary of research on TRIM2 and at exploring the potential role of TRIM2 as a biomarker and therapeutic target in many kinds of human diseases.
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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 (November 10, 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 order association via additional domains of the tripartite motif. In many of the TRIM family proteins studied thus far, RING dimerization is an important prerequisite for E3 ligase enzymatic activity though the propensity of RING domains to dimerize differs significantly between different TRIMs and can be influenced by other regions of the protein.
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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 (October 13, 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 expression of many TRIM proteins has been observed in CRC tissues and is frequently correlating with poor survival of patients. Notably, some TRIM members can act as tumor suppressors depending on the context and the type of cancer which has been assessed. Mechanistically, most cancer-related TRIMs have a critical impact on cell cycle control, apoptosis, epithelial–mesenchymal transition (EMT), metastasis, and inflammation mainly through directly interfering with diverse oncogenic signaling pathways. In addition, some recent publications have emphasized the emerging role of some TRIM members to act as transcription factors and RNA-stabilizing factors thus adding a further level of complexity to the pleiotropic biological activities of TRIM proteins. The current review focuses on oncogenic signaling processes targeted by different TRIMs and their particular role in the development of CRC. A better understanding of the crosstalk of TRIMs with these signaling pathways relevant for CRC development is an important prerequisite for the validation of TRIM proteins as novel biomarkers and as potential targets of future therapies for CRC.
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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, protein degradation, autophagy mediation, ion channel regulation, congenital heart disease, and cardiomyopathies. In this review, we provide an overview of the TRIM family and discuss its involvement in the regulation of cardiac proteostasis and pathophysiology and its potential therapeutic implications.
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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 (June 16, 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-independent mechanisms that contribute to tumor cell biology in prostate, breast, ovarian and endometrial cancer. Furthermore, we point out common functions of TRIM proteins throughout the group of hormone-driven cancers. An improved understanding of the biological impact of TRIM proteins in cancer may pave the way for improved prognostication and novel therapeutics, ultimately improving cancer care for patients with hormone-driven cancers.
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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 (March 7, 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. Phylogenetic analysis was used to elucidate the evolutionary relationship of TRIM protein among teleost and higher vertebrate species. The results show that the TRIM orthologs of highly distant vertebrates have conserved sequences and domain architectures. The pairwise distance was calculated among teleost species of TRIMs, and the result exhibits very few mismatches at aligned position thus, indicating that the members are not distant from each other. Furthermore, TRIM family of common carp clustered into six groups on the basis of phylogenetic analysis. Additionally, the analysis revealed conserved motifs and functional domains in the subfamily members. The difference in functional domains and motifs is attributed to the evolution of these groups from different ancestors, thus validating the accuracy of clusters in the phylogenetic tree. However, the intron-exon organization is not precisely similar, which suggests duplication of genes and complex alternative splicing. The percentage of secondary structural elements is comparable for members of the same group, but the tertiary conformation is varied and dominated by coiled-coil segments required for catalytic activity. Gene ontology analysis revealed that these proteins are mainly associated with the catalytic activity of ubiquitination, immune system, zinc ion binding, positive regulation of transcription, ligase activity, and cell cycle regulation. Moreover, the biological pathway analyses identified four KEGG and 22 Reactome pathways. The predicted pathways correspond to functional domains, and gene ontology which proposes that proteins with similar structures might perform the same functions.
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Azuma, Kotaro, and Satoshi Inoue. "Efp/TRIM25 and Its Related Protein, TRIM47, in Hormone-Dependent Cancers." Cells 11, no. 15 (August 8, 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. Based on a phylogenetic analysis of the C-terminal region of TRIM family proteins, we focused on TRIM47 as a protein belonging to the same branch as Efp. TRIM47 is a poor prognostic factor in both breast cancer and prostate cancer. Atypical lysine-27-like poly-ubiquitination was involved in the underlying mechanism causing endocrine resistance in breast cancer. We also discuss the functions of Efp and TRIM47 in other types of cancers and innate immunity by introducing substrates the are modified by poly-ubiquitination.
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Huang, Yingjie, Yue Xiao, Xuekang Zhang, Xuan Huang, and Yong Li. "The Emerging Roles of Tripartite Motif Proteins (TRIMs) in Acute Lung Injury." Journal of Immunology Research 2021 (October 19, 2021): 1–9. http://dx.doi.org/10.1155/2021/1007126.

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Acute lung injury (ALI) is an inflammatory disorder of the lung that causes high mortality and lacks any pharmacological intervention. Ubiquitination plays a critical role in the pathogenesis of ALI as it regulates the alveolocapillary barrier and the inflammatory response. Tripartite motif (TRIM) proteins are one of the subfamilies of the RING-type E3 ubiquitin ligases, which contains more than 80 distinct members in humans involved in a broad range of biological processes including antivirus innate immunity, development, and tumorigenesis. Recently, some studies have shown that several members of TRIM family proteins play important regulatory roles in inflammation and ALI. Herein, we integrate emerging evidence regarding the roles of TRIMs in ALI. Articles were selected from the searches of PubMed database that had the terms “acute lung injury,” “ubiquitin ligases,” “tripartite motif protein,” “inflammation,” and “ubiquitination” using both MeSH terms and keywords. Better understanding of these mechanisms may ultimately lead to novel therapeutic approaches by targeting TRIMs for ALI treatment.
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Dissertations / Theses on the topic "TRIM protein"

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Najmabadi, Sepideh. "Drosophila model of myosin myopathy rescued by overexpression of a TRIM-protein family member." Thesis, Högskolan i Skövde, Institutionen för hälsa och lärande, 2019. http://urn.kb.se/resolve?urn=urn:nbn:se:his:diva-17919.

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Laing distal myopathy is inherited in an autosomal dominant manner usually before the age of five that initially involves the dorsiflexion in the ankles’ and in big toes to the finger extensors. Weakness of the flexor muscles in the neck is seen in most affected individuals and mild facial weakness is also often present. Hypertrophic or dilated cardiomyopathy, starting at birth to respectively second or third decade of life, is the symptom in the affected humans.This study performed on Drosophila melanogaster, has evaluated whether feeding MuRF1 enzyme (which has a similar role as ABBA enzyme) to Drosophila larvae, in different concentrations, will have a positive effect on the larvae’s muscular abilities through an analysis of their manifestation, the distance they manage to crawl and the time it takes for them to turn from a ventral up to dorsal up position.The result show no significant impact on larvae ability to turn or crawl between different groups fed with MuRF1 enzyme, nor between the two control groups, wild larvae and mutated larvae. Other studies have proven that there is a significant difference in muscular ability between wild and mutated larvae, so explanations to why this study did not manage to replicate these results were evaluated. The study found that how many days has passed since hatching has a significant impact on performance of turning and crawling for wild larvae that are not treated with enzyme.There are a number of improvement suggestions to the experimental design and the methodology to enable a proper evaluation of the research aim of this thesis. Future research on the topic should implement these and redo the experiments and measurements of this study. In addition, the quantity of larvae that reaches pupa stage should be captured to evaluate whether the MuRF1 enzyme has a positive impact on mutated larvae reaching pupation stage. The most important parts of the improvement proposals to measure the ability of larvae when they are about the same age, as this was proven with statistical significance to have an impact on crawling and turning.
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Zhang, Xuzhe. "Eutherian-specific gene TRIML2 attenuates inflammation in the evolution of placentation." University of Cincinnati / OhioLINK, 2019. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1573576401238203.

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Demange, Antonin. "Protéines à motif tripartite (TRIM) chez le porc (Sus scrofa) et réplication du rétrovirus endogène porcin." Phd thesis, Université Rennes 1, 2013. http://tel.archives-ouvertes.fr/tel-00992386.

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Les études des interactions entre cellules hôtes et rétrovirus ont conduit à définir le concept de restriction virale dont les facteurs constituent une part de l'immunité innée des cellules hôtes. Ces facteurs contribuent au contrôle des rétrovirus endogènes (ERV) dont l'émergence peut être associée à certaines pathologies telles que des leucémies ou des immunodéficiences. Chez le porc, certains ERV (PERV) sont réplicatifs, pourtant aucune pathologie ne leur a, à ce jour, été associée. Les mécanismes de restriction virale impliqués dans ce phénomène ont fait l'objet de nombreuses études. Elles n'ont cependant concerné que certains facteurs. Les protéines porcines à motif tripartite (poTRIM) n'ont ainsi fait l'objet que de peu d'études. Pourtant, de nombreux membres de cette famille participent à la restriction virale chez d'autres organismes que le porc. La présente étude s'intéresse par conséquent aux orthologues porcins de ces protéines et à leur relation avec les PERV. L'élaboration d'une stratégie d'expression de ces protéines dans un modèle humain, sensible à l'infection par le PERV nous a permis d'évaluer et de caractériser les effets des TRIM sur le cycle infectieux du PERV. Cette stratégie a mis en évidence une activité de restriction par TRIM8 tandis que TRIM44 semble au contraire agir en faveur de la réplication virale. En ce qui concerne poTRIM11, elle favorise l'entrée du PERV tout en inhibant son expression. L'étude a également confirmé l'insensibilité du PERV vis-à-vis de poTRIM5α. L'ensemble de ces résultats contribuent à la compréhension de la relation entre la réplication des PERV et le contrôle mené par son hôte.
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Fraser, S. J. "Characterising retroviral restriction by TRIM proteins." Thesis, University College London (University of London), 2016. http://discovery.ucl.ac.uk/1532045/.

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Tripartite motif (TRIM) proteins are numerous in the human proteome, and a number of these molecules are known to restrict retroviral replication. TRIM5α (T5α) is one such factor. It targets the viral capsid and imposes a block to infection between entry and reverse transcription. Capsid recognition is mediated by the C-terminal B30.2 domain, which contains surface-exposed loops of high amino acid variability. Restriction is then effected via proteasome recruitment and the induction of innate immune cascades. Although T5α is well-characterised in this respect, other factors – such as the highly divergent TRIM1 (T1) – remain poorly understood. To further characterise the T1 restriction phenotype, chimeras of this protein and its non-restricting paralogue, T18, were generated by overlapping PCR. The restriction activities of the resulting molecules were then measured using an established flow cytometry assay. These experiments revealed that T1 also binds capsid via the B30.2 domain, although the majority of this region can be functionally replaced. Other aspects of T1 biology addressed in this work include the contribution of N-terminal components to restriction potency, and the relationship between protein expression level and restriction activity. Following a number of attempts to generate a functional chimera of T1 and 5α, the latter half of this thesis explores how the spacing between capsid-binding and effector domains can influence restriction activity. To this end, a panel of mutations were made in the linker 2 (L2) region of T5α, and their effects on restriction measured. These experiments revealed that even small changes in interdomain spacing can have profound phenotypic consequences. Collectively, this work reinforces the notion that TRIM family members share a common overall design, allowing individual components to be shuffled between them. At the same time, each molecule has been shaped by unique evolutionary pressures, which can render them sensitive even to relatively minor modifications.
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Fekete, Richard Alfred. "Characterizing the protein and DNA interactions of the F plasmid DNA binding protein, TraM." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2001. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp04/NQ60291.pdf.

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Marafie, Sulaiman. "TRIM7, a novel binding protein of the mTORC2 component Sin1." Thesis, University of Manchester, 2013. https://www.research.manchester.ac.uk/portal/en/theses/trim7-a-novel-binding-protein-of-the-mtorc2-component-sin1(c344b542-0706-4ec0-be06-ce6683cee52e).html.

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TRIM7 is a member of the TRIM (tripartite motif-containing) protein superfamily. This family has been implicated in many disorders such as genetic diseases, neurological diseases, and cancers. Little is known about the function of TRIM7 except that it interacts with glycogenin and may regulate glycogen biosynthesis. Recently, a yeast two-hybrid protein-protein interaction screen revealed the binding of TRIM7 to Sin1, a protein found in a complex with the mammalian target of rapamycin (mTOR) protein kinase. mTOR can form two complexes, mTORC1 and mTORC2, which are important for cell growth, differentiation, and survival. Sin1 is a core component of mTORC2 and is critical for mTORC2 stability and activity. It was confirmed by co-immunoprecipitation that TRIM7 associates with Sin1 and mTOR in cultured mammalian cells. Furthermore, it was demonstrated that TRIM7 is a phosphoprotein, although it was not directly targeted by mTOR in vitro. Similar to some other TRIM family proteins, it was demonstrated that TRIM7 has a ubiquitin E3 ligase function allowing it to autoubiquitinate both in vitro and in cells. The autoubiquitination of TRIM7 was dependent on its RING domain. Further characterization of TRIM7 indicated that it can both homo-oligomerise as well as hetero-oligomerise with other members of its sub-class of TRIM proteins and that it co-localises with them into discrete cytoplasmic loci. To determine the cellular function of TRIM7, a stable cell line expressing an shRNA directed against TRIM7 was generated. Successful knock down of TRIM7 was achieved and this led to an increase in the protein levels of components of the mTORC2 complex, including Sin1. This coincided with an increase in cell proliferation. In conclusion, this research identifies a novel role for TRIM7 as a ubiquitin ligase involved in regulating cell proliferation and provides a potential link between TRIM7 and the mTOR pathway, a major transducer of proliferative and cell survival signals.
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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.
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Liu, Sunbin. "Investigation of protein-protein interactions within the human spliceosomal U4/U6.U5 tri-snRNP particle." Doctoral thesis, [S.l.] : [s.n.], 2005. http://webdoc.sub.gwdg.de/diss/2005/liu/liu.pdf.

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Xin, Gang. "The role of TREM proteins in lung homeostasis and inflammation." Thesis, Imperial College London, 2011. http://hdl.handle.net/10044/1/9058.

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The family of Triggering Receptors Expressed on Myeloid Cells (TREM) contain novel activating receptors of the Ig super-family that are expressed on myeloid cells. TREM-1 is a transmembrane glycoprotein expressed on blood neutrophils and a subset of monocytes, but not on lymphocytes or other cell types and is upregulated by bacterial and fungal products. TREM-1 signaling potentiates the outcome of Toll-like Receptor (TLR) signaling. Blockade of TREM-1 prevents experimentally induced septic shock. In addition to the membrane-bound form, a soluble TREM-1 molecule (sTREM-1) exists that regulates membrane bound TREM-1 by competing against the, as yet, unknown natural TREM-1 ligand. sTREM-1 is detected at high levels during bacterial infection and asthma and is used as a predictive biomarker for severe inflammation. TREM-2 on, the other hand is not known to be secreted and the membrane bound form is reported to prevent TLR signaling and promote osteoclastogenesis. The expression and function of TREM proteins during respiratory viral infection is not currently known. In this thesis we investigate the hypothesis that TREM-1 signaling contributes to excessive cytokine production during pulmonary viral infection in a murine model and that soluble TREM-1 and membrane bound TREM-2 proteins are anti-inflammatory. We show, for the first time, the following novel mechanisms that significantly increase our understanding of this important receptor family: 1) TREM-1 is highly up-regulated during influenza and the subsequent release of sTREM-1 likely contributes to secondary bacterial super-infection, 2) Blockade of TREM-1 at the onset of viral infection significantly reduces the risk of secondary bacterial pneumonia and 3) TREM-2 expressing macrophages that appear during the resolution of influenza-induced inflammation display a regulatory phenotype that can reduce TLR responsiveness of inflammatory macrophages. Taken together, our data suggests that TREM-1 proteins represent a novel therapeutic target for the alleviation of influenza-induced pathology and that TREM-2 expression identifies a novel population of regulatory macrophages.
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Ruiz, Echartea Maria Elisa. "Pairwise and Multi-Component Protein-Protein Docking Using Exhaustive Branch-and-Bound Tri-Dimensional Rotational Searches." Electronic Thesis or Diss., Université de Lorraine, 2019. http://www.theses.fr/2019LORR0306.

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La détermination des structures tri-dimensionnelles (3D) des complexes protéiques est cruciale pour l’avancement des recherches sur les processus biologiques qui permettent, par exemple, de comprendre le développement de certaines maladies et, si possible, de les prévenir ou de les traiter. Face à l’intérêt des complexes protéiques pour la recherche, les difficultés et le coût élevé des méthodes expérimentales de détermination des structures 3D des protéines ont encouragé l’utilisation de l’informatique pour développer des outils capables de combler le fossé, comme par exemple les algorithmes d’amarrage protéiques. Le problème de l’amarrage protéique a été étudié depuis plus de 40 ans. Cependant, le développement d’algorithmes d’amarrages précis et efficaces demeure un défi à cause de la taille de l’espace de recherche, de la nature approximée des fonctions de score utilisées, et souvent de la flexibilité inhérente aux structures de protéines à amarrer. Cette thèse présente un algorithme pour l’amarrage rigide des protéines, qui utilise une série de recherches exhaustives rotationnelles au cours desquelles seules les orientations sans clash sont quantifiées par ATTRACT. L’espace rotationnel est représenté par une hyper-sphère à quaternion, qui est systématiquement subdivisée par séparation et évaluation, ce qui permet un élagage efficace des rotations qui donneraient des clashs stériques entre les deux protéines. Les contributions de cette thèse peuvent être décrites en trois parties principales comme suit. 1) L’algorithme appelé EROS-DOCK, qui permet d’amarrer deux protéines. Il a été testé sur 173 complexes du jeu de données “Docking Benchmark”. Selon les critères de qualité CAPRI, EROS-DOCK renvoie typiquement plus de solutions de qualité acceptable ou moyenne que ATTRACT et ZDOCK. 2) L’extension de l’algorithme EROS-DOCK pour permettre d’utiliser les contraintes de distance entre atomes ou entre résidus. Les résultats montrent que le fait d’utiliser une seule contrainte inter-résidus dans chaque interface d’interaction est suffisant pour faire passer de 51 à 121 le nombre de cas présentant une solution dans le top-10, sur 173 cas d’amarrages protéine-protéine. 3) L’extension de EROSDOCK à l’amarrage de complexes trimériques. Ici, la méthode proposée s’appuie sur l’hypothèse selon laquelle chacune des trois interfaces de la solution finale doit être similaire à au moins l’une des interfaces trouvées dans les solutions des amarrages pris deux-à-deux. L’algorithme a été testé sur un benchmark de 11 complexes à 3 protéines. Sept complexes ont obtenu au moins une solution de qualité acceptable dans le top-50 des solutions. À l’avenir, l’algorithme EROS-DOCK pourra encore évoluer en intégrant des fonctions de score améliorées et d’autres types de contraintes. De plus il pourra être utilisé en tant que composant dans des workflows élaborés pour résoudre des problèmes complexes d’assemblage multi-protéiques
Determination of tri-dimensional (3D) structures of protein complexes is crucial to increase research advances on biological processes that help, for instance, to understand the development of diseases and their possible prevention or treatment. The difficulties and high costs of experimental methods to determine protein 3D structures and the importance of protein complexes for research have encouraged the use of computer science for developing tools to help filling this gap, such as protein docking algorithms. The protein docking problem has been studied for over 40 years. However, developing accurate and efficient protein docking algorithms remains a challenging problem due to the size of the search space, the approximate nature of the scoring functions used, and often the inherent flexibility of the protein structures to be docked. This thesis presents an algorithm to rigidly dock proteins using a series of exhaustive 3D branch-and-bound rotational searches in which non-clashing orientations are scored using ATTRACT. The rotational space is represented as a quaternion “π-ball”, which is systematically sub-divided in a “branch-and-bound” manner, allowing efficient pruning of rotations that will give steric clashes. The contribution of this thesis can be described in three main parts as follows. 1) The algorithm called EROS-DOCK to assemble two proteins. It was tested on 173 Docking Benchmark complexes. According to the CAPRI quality criteria, EROS-DOCK typically gives more acceptable or medium quality solutions than ATTRACT and ZDOCK. 2)The extension of the EROS-DOCK algorithm to allow the use of atom-atom or residue-residue distance restraints. The results show that using even just one residue-residue restraint in each interaction interface is sufficient to increase the number of cases with acceptable solutions within the top-10 from 51 to 121 out of 173 pairwise docking cases. Hence, EROS-DOCK offers a new improved search strategy to incorporate experimental data, of which a proof-of-principle using data-driven computational restraints is demonstrated in this thesis, and this might be especially important for multi-body complexes. 3)The extension of the algorithm to dock trimeric complexes. Here, the proposed method is based on the premise that all of the interfaces in a multi-body docking solution should be similar to at least one interface in each of the lists of pairwise docking solutions. The algorithm was tested on a home-made benchmark of 11 three-body cases. Seven complexes obtained at least one acceptable quality solution in the top-50. In future, the EROS-DOCK algorithm can evolve by integrating improved scoring functions and other types of restraints. Moreover, it can be used as a component in elaborate workflows to efficiently solve complex problems of multi-protein assemblies
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Books on the topic "TRIM protein"

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Meroni, Germana, ed. TRIM/RBCC Proteins. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4614-5398-7.

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Meroni, Germana. TRIM/RBCC proteins. New York, N.Y: Springer Science+Business Media, 2012.

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The Phoenix trip: Notes on a Quaker mission to Haiphong. Burnsville, N.C: Celo Press, 1985.

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The ultimate Internet terrorist: How hackers, geeks, and phreaks can ruin your trip on the Information Superhighway--and what you can do to protect yourself. Boulder, Colo: Paladin Press, 1998.

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Meroni, Germana. TRIM/RBCC Proteins. Springer London, Limited, 2013.

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Meroni, Germana. TRIM/RBCC Proteins. Springer, 2016.

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Hetz, Claudio, ed. Protein Misfolding Disorders: A Trip into the ER. BENTHAM SCIENCE PUBLISHERS, 2012. http://dx.doi.org/10.2174/97816080501301090101.

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Stefano, Vittorio De. Origins of specificity in protein modification: Reaction patterns of tris-trimesates with human hemoglobin A, water, and n-propylamine. Dept of Chemistry, U of Toronto, 1999.

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Nikravan, Sara, and Frederick Mihm. Pathophysiology and management of functional endocrine tumours in the critically ill. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199600830.003.0264.

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Thyroid hormones act on most tissues via nuclear T3 receptors. Thyroid hormones stimulate oxygen consumption and heat production, influence cell growth and maturation (central nervous system, bone), and modulate metabolism (carbohydrates, lipids, proteins, drugs). Treatment for presumed thyroid disease frequently has to be initiated before the results of diagnostic tests are available. Treatment of hyperthyroidism should result in the reduction of serum thyroid hormone levels and their action on peripheral tissues with concurrent treatment of the precipitating event. In severe hypothyroidism the choice of thyroid hormone (thyroxine or tri-iodothyronine), optimal dosing, and the route of administration remain controversial
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Andersson, Jenny. Bridging the Iron Curtain. Futurology as Dissidence and Control. Oxford University Press, 2018. http://dx.doi.org/10.1093/oso/9780198814337.003.0007.

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East European futurists were part of the transnational networks of futures research. The Ford Foundation sent Daniel Bell on a study trip in 1960 during which he made contact with some of the key milieus of revisionist Marxist thought: the Polska 2000 group led by Andrej Sicinski as well as the group of sociologists under the leadership of Radovan Richta in Prague. After 1968, futurologists helped introduce forms of management and computer science into the planning systems of the socialist economies under the banner of prognostika. The chapter examines the way that East European futurists used the future as a way of constructing an argument about the need to revise Marxism, and how future research became a space of protest and dissidence.
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Book chapters on the topic "TRIM protein"

1

Nisole, Sébastien. "TRIM Protein Family and Viral Restriction." In Encyclopedia of AIDS, 1–8. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4614-9610-6_383-1.

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Nisole, Sébastien. "TRIM Protein Family and Viral Restriction." In Encyclopedia of AIDS, 2062–68. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-7101-5_383.

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Fletcher, Adam J., and Greg J. Towers. "Inhibition of Retroviral Replication by Members of the TRIM Protein Family." In Current Topics in Microbiology and Immunology, 29–66. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-37765-5_2.

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Petrera, Francesca, and Germana Meroni. "TRIM Proteins in Development." In Advances in Experimental Medicine and Biology, 131–41. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4614-5398-7_10.

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Cambiaghi, Valeria, Virginia Giuliani, Sara Lombardi, Cristiano Marinelli, Francesca Toffalorio, and Pier Giuseppe Pelicci. "TRIM Proteins in Cancer." In Advances in Experimental Medicine and Biology, 77–91. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4614-5398-7_6.

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Ikeda, Kazuhiro, and Satoshi Inoue. "Trim Proteins as Ring Finger E3 Ubiquitin Ligases." In Advances in Experimental Medicine and Biology, 27–37. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4614-5398-7_3.

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Yap, Melvyn W., and Jonathan P. Stoye. "TRIM Proteins and the Innate Immune Response to Viruses." In Advances in Experimental Medicine and Biology, 93–104. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4614-5398-7_7.

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Shen, Koning, and Judith Frydman. "The interplay between the chaperonin TRiC and N-terminal region of Huntingtin mediates Huntington’s Disease aggregation and pathogenesis." In Protein Quality Control in Neurodegenerative Diseases, 121–32. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-642-27928-7_10.

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Wang, Hua, Heng Huang, Chris Ding, and Feiping Nie. "Predicting Protein-Protein Interactions from Multimodal Biological Data Sources via Nonnegative Matrix Tri-Factorization." In Lecture Notes in Computer Science, 314–25. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-642-29627-7_33.

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Luche, Sylvie, Mireille Chevallet, Cécile Lelong, and Thierry Rabilloud. "Separation of Proteins by Gel Electrophoresis in the Tris-Taurine-HCl System." In Springer Protocols Handbooks, 211–19. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-59745-198-7_25.

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Conference papers on the topic "TRIM protein"

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Dyer, R. Brian, and Timothy P. Causgrove. "Ultrafast Protein Relaxation: Time-Resolved Infrared Studies of Protein Dynamics Triggered by CO Photodissociation from CO Myoglobin." In International Conference on Ultrafast Phenomena. Washington, D.C.: Optica Publishing Group, 1994. http://dx.doi.org/10.1364/up.1994.tub.4.

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A critical feature of the biological function of heme proteins is the direct coupling of protein motion to the process of binding exogenous ligands to the heme. In carbonmonoxymyoglobin (MbCO), a substantial, specific conformational relaxation is associated with the transition from the ligated to the unligated form of the protein. The analogous tertiary structural changes of the monomer heme subunits of hemoglobin ultimately lead to the R→T quaternary structural transition, the allosteric control mechanism of O2 binding efficiency [1]. We have studied these processes on the earliest timescales, using picosecond, time-resolved infrared (TRIR) spectroscopy. It has long been known that infrared spectra in the amide region are sensitive to protein secondary conformation [2]. Recent advances in equipment and techniques have permitted researchers to quantitatively predict secondary structures from infrared spectra [3,4], particularly in the amide I region [4]. Therefore, it is now possible to study protein motion in time-resolved experiments on dynamics and function. The ligation reactions of small molecules such as CO with the heme site of Mb exemplify the mechanisms available to O2. CO is an ideal candidate for initial time-resolved IR experiments in the amide I region because it is easily photolyzed, little geminate recombination [5], and the structure of both MbCO and unligated Mb have been studied by crystallographic methods [6]. TRIR has already been applied to the stretching vibrations of the bound and free CO ligand [7,8]; dynamics of the protein, however, have yet to be probed by TRIR spectroscopy of the protein vibrations. Here we report results on the motions of the protein in response to ligation reactions, probed in the amide I region centered about 1650 cm-1.
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Saundry, R. H., S. Khumprayoon, and G. F. Savidge. "THE IDENTIFICATION OF A NOVEL FACTOR X ACTIVATOR ACTIVITY IN Mg2+ - ANTICOAGULATED PLASMA." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643293.

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Mg2+ anticoagulated PPP (20mM MgCl2) was applied at RT to a Zn2+ immobilised biscarboxymethylamino Sepharose 4B column and eluted with 20mM Tris, 20mM MgCl2, 2.5mM CaCl2 0.15M NaCl buffer pH 7.4. Following collection of the wash-through fractions, bound proteins were developed through application of linear (0 to 35mM) imidazole gradients.All fractions were screened for F.II, V, IX, X, vWF:Ag, Protein C, Fg, Fn and 2-macroglobulin by ELISA, VIII:Ag by IRMA, and VIII:C by both 1-stage and 2-stage bioassay methods. VIIIrAg (60-90% yield), vWF:Ag (100%), VIII:C 1-stage activity (35%), Fn (> 60%), Fg (> 80%), V (50%) and a2-macroglobulin (> 70%) were located only in the gradient fractions. Two distinct peaks demonstrated shortening of the 2-stage VIII:C assay:- one co-eluting with the 1-stage VIII:C activity and another major peak in the wash-through fractions where antigenic determinants of F.II, IX, X and part of the protein C were located and partially resolved from each other. Only F.II.-Ag co-eluted with the “ 2-stage VIII:C” activity. Similar observations were found in Mg2+ -anticoagulated severe Haemophilia A plasma and in citrated PPP developed with 20mM MgCl2, 20mM Tris buffer. A1(0H)3 treatment abolished the activity from citrate -, but not from Mg2+ -anticoagulated plasma.The relevant fractions showed no activities in F.V, VII, VIII:C, IX or X 1-stage bioassays. They did not clot Fg and did not contain detectable Xa or Ila as assessed by S-2222, S-2238 or S-2288. Following incubation with specific antisera against IgG, II, V, VII:Ag, X, protein C, a- and g- lipoproteins, and plasminogen only anti-II inhibited this "2-stage VIII:C" activity. 2-stage VIII:C assays depend upon Ca2+ -dependent generation of Xa. Since the activity in the wash-through fractions could not be ascribed to VIII, Xa, or Ila the results would indicate the presence of a hitherto undescribed Factor X activator activity.
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Bossard, Carine, Dinorah Friedmann-Morvinski, Conrado Soria, Kristen Espantman, Robert Chalkley, Inder Verma, Alma Burlingame, and Clodagh O'Shea. "Abstract 4061: TRIM-NHL proteins: New potential targets for cancer therapy." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-4061.

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Yonashiro, Kan, and Kouichi Hirata. "Trim Distance between Positions in Nucleotide Sequences for Structural Proteins of SARS-CoV-2." In 2021 10th International Congress on Advanced Applied Informatics (IIAI-AAI). IEEE, 2021. http://dx.doi.org/10.1109/iiai-aai53430.2021.00006.

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Owen, B. A., and W. G. Owen. "ASSOCIATION OF HEPARIN AND FACTOR Xa: INFLUENCE ON THE RATE OF INHIBITION OF FACTOR Xa BY ANTITHROMBIN III-HEPARIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643837.

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Association of heparin non-covalently with bovine factor Xa was analyzed by Superose-12 gel chromatography. In 0.05 M NaCl, 0.02 M Tris, pH 7.5, DEGR-Xa (factor Xa inactivated by dans-Glu-Gly-Arg-CH2Cl) was eluted as a single, sharp peak at Ve/Vt=0-65 (elution volume/internal volume). Mixtures of heparin and DEGR-Xa were eluted as two partially resolved peaks of protein at Ve/Vt=0.59 and 0.65. The fraction of DEGFUXa in the leading peak was directly proportional to [heparin], and at 100 yM heparin the leading peak contained more than half the total protein. When 0.02 M HEPES was substituted for Tris a single, slightly broadened peak at Ve/Vt=0.64 was obtained on chromatography of 100 μM heparin and 10 μM DEGR-Xa. In a buffer system comprising 0.02 M Tris, 0.02 M HEPES, 0.03 M NaCl, pH 7.5, two peaks were eluted at Ve/Vt=0.59 and 0.65. Therefore, Tris increases the affinity of DEGR-Xa for heparin.Solutions buffered with Tris or HEPES were compared for effects on the kinetics of inhibition of factor Xa by antithrombin III-heparin. Reaction mixtures containing 1 nM factor Xa, 30 nM heparin and 600 nM antithrombin III were assayed with S-2222 at intervals of 2-10 sec. Reagent concentrations were chosen (a) to assure pseudo-first-order kinetics, (b) to have [heparin]<< Kq for factor Xa-heparin, and (c) to bind virtually all available heparin to antithrombin III. The same second-order rate constant, Kobs=2.5×107 M−1s−1, was obtained in both buffer systems. We conclude that the association of factor Xa with heparin observed directly by gel chromatography does not contribute to the reaction rate of factor Xa with antithrombin III-heparin.
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Kim, Joongsoo, Rakesh Kumar, and Jung-Mo Ahn. "Tris-Benzamide Analogs for Inhibiting Bcl-2 Proteins in Prostate Cancer." In The 24th American Peptide Symposium. Prompt Scientific Publishing, 2015. http://dx.doi.org/10.17952/24aps.2015.170.

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Mager, J., A. Burgess, R. Pavan, and J. Orzechowski. "Thick Aluminum Coatings Using Axial Plasma Spray for Proton Beam Collimators." In ITSC2004, edited by Basil R. Marple and Christian Moreau. ASM International, 2004. http://dx.doi.org/10.31399/asm.cp.itsc2004p0076.

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Abstract Aluminum coatings minimum 1.8 mm thick are applied to water-cooled proton beam collimators used in the manufacture of medical isotopes on the TRIUMF TR30 cyclotrons in Vancouver, British Columbia, Canada. The sprayed surface of the collimators is made from silver. These collimators are used to trim the proton beam so that only a designated area on the isotope production target is irradiated with protons. Aluminum is used because its activation products at the energies used have short half-lives, thus minimizing the amount of collateral radioactivity produced. The aluminum is sprayed using an Axial III plasma spray torch. In service, the collimators are subject to high heat fluxes due to the proton beam. Service life, heat transfer and application data are provided in this paper.
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Pokidova, Olesya Viktorovna, Nina Sergeevna Emel’yanova, Alexander Vasilievich Kulikov, Alexander Ivanovich Kotelnikov, and Natalia Alekseevna Sanina. "STUDY OF THE TRANSFORMATION OF NITROSYL IRON COMPLEX WITH N-ETHYLTHIOUREA LIGANDS IN MODEL BIOLOGICAL SYSTEMS." In NEW TECHNOLOGIES IN MEDICINE, BIOLOGY, PHARMACOLOGY AND ECOLOGY. Institute of information technology, 2021. http://dx.doi.org/10.47501/978-5-6044060-1-4.52.

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The process of transformation of a mononuclear cationic complex with N-ethylthiourea ligands in Tris-HCl buffer, as well as in a reaction mixture with reduced glutathione and bovine serum albumin, has been studied. It was found that in the presence of glutathione, the complex dimer-izes, while its initial ligands are replaced by glutathione. In the presence of albumin, the decay product of the complex is coordinated with amino acid residues (Cys34 and His39) to form a protein-bound complex.
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Siess, W., and E. G. Lapetina. "SYNERGISM OF Gi-DISSOCIATION AND PROTEIN KINASE C STIMULATION IN PLATELET ACTIVATION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644511.

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Epinephrine or UK 14304 (a specific (α2-adrenoceptor agonist) synergizes with phorbol esters (phorbol 12,13-dibutyrate, PdBu) or bioactive diacylglycerols (sn-1,2-dioctanoylglycerol, DiC8) to induce aggregation and ATP-secretion of platelets. The effect on aggregation is more pronounced than on secretion, and it is observed in aspirinized platelet-rich plasma or suspensions of washed platelets containing ADP-scavengers. No prior shape change is found. In the presence of epinephrine, DiCg induces reversible aggregation and PdBu evokes irreversible aggregation that correlates with the effects, on protein phosphorylation. Epinephrine and UK 14304 neither induce nor enhance the phosphorylation of myosin light chain (20kDa), the substrate of protein kinase C (47kDa), or a 38kDa protein evoked by DiCg) or PdBu. Epinephrine does not cause, stimulation of phospholipase C as reflected by the production of inositol mono-, bis- and tris-phosphate or phosphatidic acid. Even under conditions of maximal aggregation induced by epinephrine plus PdBu, formation of 32p-phOSphatidic acid is not observed. The synergistic action of epinephrine and PdBu does not depend on extracellular Ca2+. Primary aggregation induced by epinephrine, but not platelet aggregation induced by PdBu plus epinephrine, is inhibited by high intracellular concentrations of the calcium chelator quin2. Prostacyclin prevents platelet aggregation but does not affect protein phosphorylation induced by PdBu plus epinephrine.The experiments indicate that α2-adrenoceptor agonists may induce primary aggregation by a mechanism involving release of membrane-bound Ca2+. The synergism with protein kinase C is, however, caused by a mechanism that occurs distally to protein phosphorylation and is not related to Phospholipase C activation and Ca2+-fluxes across the Dlasma membrane or in the cvtosol. Evidence is presented suoportina the view that this mechanism miqht be related to the dissociation of Gi caused by α2-adrenoceptor activation.
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Lei, Ryan Z., Kris R. Paserba, Andrew J. Gellman, Nisha Shukla, and Laura M. Cornaglia. "PFPE Lubricant Bonding to Carbon Overcoats." In STLE/ASME 2001 International Joint Tribology Conference. American Society of Mechanical Engineers, 2001. http://dx.doi.org/10.1115/trib-nano2001-106.

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Abstract Continued reduction in the head-disk spacing of magnetic data storage systems and the resulting increase in the frequency of head-disk contacts will place increasing burdens on the perfluoropolyalkyl ether (PFPE) lubricant and amorphous carbon (a-C) overcoat used to protect the surfaces of magnetic media. In addition, environmental conditions such as temperature, humidity, and contamination that influence the lubricant-overcoat interactions become increasingly important to the tribological performance of the head-disk interface. It is of utmost importance to obtain a fundamental understanding of the molecular interactions at the lubricant-overcoat interface in order to maintain the reliability of future hard disk drives. Recent progress has generated insight into the heterogeneous nature of the a-C overcoat surface, the interaction mechanisms of PFPEs with a-C overcoats, the effects of humidity on lubricant-overcoat interactions, and the evaporation kinetics of PFPE lubricants.
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Reports on the topic "TRIM protein"

1

Droby, Samir, Michael Wisniewski, Ron Porat, and Dumitru Macarisin. Role of Reactive Oxygen Species (ROS) in Tritrophic Interactions in Postharvest Biocontrol Systems. United States Department of Agriculture, December 2012. http://dx.doi.org/10.32747/2012.7594390.bard.

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To elucidate the role of ROS in the tri-trophic interactions in postharvest biocontrol systems a detailed molecular and biochemical investigation was undertaken. The application of the yeast biocontrol agent Metschnikowia fructicola, microarray analysis was performed on grapefruit surface wounds using an Affymetrix Citrus GeneChip. the data indicated that 1007 putative unigenes showed significant expression changes following wounding and yeast application relative to wounded controls. The expression of the genes encoding Respiratory burst oxidase (Rbo), mitogen-activated protein kinase (MAPK) and mitogen-activated protein kinase kinase (MAPKK), G-proteins, chitinase (CHI), phenylalanine ammonia-lyase (PAL), chalcone synthase (CHS) and 4-coumarate-CoA ligase (4CL). In contrast, three genes, peroxidase (POD), superoxide dismutase (SOD) and catalase (CAT), were down-regulated in grapefruit peel tissue treated with yeast cells. The yeast antagonists, Metschnikowia fructicola (strain 277) and Candida oleophila (strain 182) generate relatively high levels of super oxide anion (O2−) following its interaction with wounded fruit surface. Using laser scanning confocal microscopy we observed that the application of M. fructicola and C. oleophila into citrus and apple fruit wounds correlated with an increase in H2O2 accumulation in host tissue. The present data, together with our earlier discovery of the importance of H₂O₂ production in the defense response of citrus flavedo to postharvest pathogens, indicate that the yeast-induced oxidative response in fruit exocarp may be associated with the ability of specific yeast species to serve as biocontrol agents for the management of postharvest diseases. Effect of ROS on yeast cells was also studied. Pretreatment of the yeast, Candida oleophila, with 5 mM H₂O₂ for 30 min (sublethal) increased yeast tolerance to subsequent lethal levels of oxidative stress (50 mM H₂O₂), high temperature (40 °C), and low pH (pH 4). Suppression subtractive hybridization analysis was used to identify genes expressed in yeast in response to sublethal oxidative stress. Transcript levels were confirmed using semi quantitative reverse transcription-PCR. Seven antioxidant genes were up regulated. Pretreatment of the yeast antagonist Candida oleophila with glycine betaine (GB) increases oxidative stress tolerance in the microenvironment of apple wounds. ROS production is greater when yeast antagonists used as biocontrol agents are applied in the wounds. Compared to untreated control yeast cells, GB-treated cells recovered from the oxidative stress environment of apple wounds exhibited less accumulation of ROS and lower levels of oxidative damage to cellular proteins and lipids. Additionally, GB-treated yeast exhibited greater biocontrol activity against Penicillium expansum and Botrytis cinerea, and faster growth in wounds of apple fruits compared to untreated yeast. The expression of major antioxidant genes, including peroxisomal catalase, peroxiredoxin TSA1, and glutathione peroxidase was elevated in the yeast by GB treatment. A mild heat shock (HS) pretreatment (30 min at 40 1C) improved the tolerance of M. fructicola to subsequent high temperature (45 1C, 20–30 min) and oxidative stress (0.4 mol-¹) hydrogen peroxide, 20–60 min). HS-treated yeast cells showed less accumulation of reactive oxygen species (ROS) than non-treated cells in response to both stresses. Additionally, HS-treated yeast exhibited significantly greater (P≥0.0001) biocontrol activity against Penicillium expansum and a significantly faster (Po0.0001) growth rate in wounds of apple fruits stored at 25 1C compared with the performance of untreated yeast cells. Transcription of a trehalose-6-phosphate synthase gene (TPS1) was up regulated in response to HS and trehalose content also increased.
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