Log in

Relevant bibliographies by topics / RuvB-like / Journal articles

To see the other types of publications on this topic, follow the link: RuvB-like.

Journal articles on the topic 'RuvB-like'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 28 journal articles for your research on the topic 'RuvB-like.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

Kanemaki, Masato, Yumiko Kurokawa, Toru Matsu-ura, et al. "TIP49b, a New RuvB-like DNA Helicase, Is Included in a Complex Together with Another RuvB-like DNA Helicase, TIP49a." Journal of Biological Chemistry 274, no. 32 (1999): 22437–44. http://dx.doi.org/10.1074/jbc.274.32.22437.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

Qiu, Xiao-Bo, Yi-Ling Lin, Kelly C. Thome, et al. "An Eukaryotic RuvB-like Protein (RUVBL1) Essential for Growth." Journal of Biological Chemistry 273, no. 43 (1998): 27786–93. http://dx.doi.org/10.1074/jbc.273.43.27786.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

Kakugawa, Satoshi, Masayuki Shimojima, Gabriele Neumann, Hideo Goto, and Yoshihiro Kawaoka. "RuvB-Like Protein 2 Is a Suppressor of Influenza A Virus Polymerases." Journal of Virology 83, no. 13 (2009): 6429–34. http://dx.doi.org/10.1128/jvi.00293-09.

Full text

Abstract:

ABSTRACT In pro- and eukaryotic cells, RuvB-like protein 2 (RBL2) resolves Holliday junction recombination intermediates. Here, we identified RBL2 as a suppressor of influenza A virus replication. Human RBL2 appears to interfere with the oligomerization of the viral nucleoprotein, a critical step in the assembly of viral replication complexes.

APA, Harvard, Vancouver, ISO, and other styles

4

Rodríguez, Carlos F., and Oscar Llorca. "RPAP3 C-Terminal Domain: A Conserved Domain for the Assembly of R2TP Co-Chaperone Complexes." Cells 9, no. 5 (2020): 1139. http://dx.doi.org/10.3390/cells9051139.

Full text

Abstract:

The Rvb1-Rvb2-Tah1-Pih1 (R2TP) complex is a co-chaperone complex that works together with HSP90 in the activation and assembly of several macromolecular complexes, including RNA polymerase II (Pol II) and complexes of the phosphatidylinositol-3-kinase-like family of kinases (PIKKs), such as mTORC1 and ATR/ATRIP. R2TP is made of four subunits: RuvB-like protein 1 (RUVBL1) and RuvB-like 2 (RUVBL2) AAA-type ATPases, RNA polymerase II-associated protein 3 (RPAP3), and the Protein interacting with Hsp90 1 (PIH1) domain-containing protein 1 (PIH1D1). R2TP associates with other proteins as part of a complex co-chaperone machinery involved in the assembly and maturation of a growing list of macromolecular complexes. Recent progress in the structural characterization of R2TP has revealed an alpha-helical domain at the C-terminus of RPAP3 that is essential to bring the RUVBL1 and RUVBL2 ATPases to R2TP. The RPAP3 C-terminal domain interacts directly with RUVBL2 and it is also known as RUVBL2-binding domain (RBD). Several human proteins contain a region homologous to the RPAP3 C-terminal domain, and some are capable of assembling R2TP-like complexes, which could have specialized functions. Only the RUVBL1-RUVBL2 ATPase complex and a protein containing an RPAP3 C-terminal-like domain are found in all R2TP and R2TP-like complexes. Therefore, the RPAP3 C-terminal domain is one of few components essential for the formation of all R2TP and R2TP-like co-chaperone complexes.

APA, Harvard, Vancouver, ISO, and other styles

5

Gospodinov, Anastas, and Boyka Anachkova. "Lack of Effect of RuvB-Like Proteins on DNA Damage Signaling Activation." Zeitschrift für Naturforschung C 65, no. 1-2 (2010): 148–52. http://dx.doi.org/10.1515/znc-2010-1-223.

Full text

Abstract:

Ataxia telangiectasia mutated (ATM) kinase is a central player in cellular response to DNA damage. Phosphorylation of the histone H2AX by ATM is required for the accumulation of repair proteins at the sites of double-strand breaks. Recently, it was reported that the histone acetyltransferase Tat interactive protein-60 (TIP60) is required to acetylate ATM prior to its activation. The RuvB-like proteins TIP48 and TIP49 are known to be necessary for the assembly and functional activity of the TIP60 acetyltransferase complex. In the present communication, we investigated the requirements of TIP48 and TIP49 for ATM activation by monitoring the cell cycle distribution and H2AX phosphorylation after irradiation of TIP48- and TIP49-depleted cells. We found that neither the cell cycle nor γ-H2AX were affected in TIP48- and TIP49-silenced cells, suggesting that the TIP60 chromatin modifi cation complex is not engaged in DNA damage signaling upstream of ATM.

APA, Harvard, Vancouver, ISO, and other styles

6

Magalska, Adriana, Anna Katharina Schellhaus, Daniel Moreno-Andrés, et al. "RuvB-like ATPases Function in Chromatin Decondensation at the End of Mitosis." Developmental Cell 31, no. 3 (2014): 305–18. http://dx.doi.org/10.1016/j.devcel.2014.09.001.

Full text

APA, Harvard, Vancouver, ISO, and other styles

7

Niewiarowski, Andrew, Alison S. Bradley, Jayesh Gor, Adam R. McKay, Stephen J. Perkins, and Irina R. Tsaneva. "Oligomeric assembly and interactions within the human RuvB-like RuvBL1 and RuvBL2 complexes." Biochemical Journal 429, no. 1 (2010): 113–25. http://dx.doi.org/10.1042/bj20100489.

Full text

Abstract:

The two closely related eukaryotic AAA+ proteins (ATPases associated with various cellular activities), RuvBL1 (RuvB-like 1) and RuvBL2, are essential components of large multi-protein complexes involved in diverse cellular processes. Although the molecular mechanisms of RuvBL1 and RuvBL2 function remain unknown, oligomerization is likely to be important for their function together or individually, and different oligomeric forms might underpin different functions. Several experimental approaches were used to investigate the molecular architecture of the RuvBL1–RuvBL2 complex and the role of the ATPase-insert domain (domain II) for its assembly and stability. Analytical ultracentrifugation showed that RuvBL1 and RuvBL2 were mainly monomeric and each monomer co-existed with small proportions of dimers, trimers and hexamers. Adenine nucleotides induced hexamerization of RuvBL2, but not RuvBL1. In contrast, the RuvBL1–RuvBL2 complexes contained single- and double-hexamers together with smaller forms. The role of domain II in complex assembly was examined by size-exclusion chromatography using deletion mutants of RuvBL1 and RuvBL2. Significantly, catalytically competent dodecameric RuvBL1–RuvBL2, complexes lacking domain II in one or both proteins could be assembled but the loss of domain II in RuvBL1 destabilized the dodecamer. The composition of the RuvBL1–RuvBL2 complex was analysed by MS. Several species of mixed RuvBL1/2 hexamers with different stoichiometries were seen in the spectra of the RuvBL1–RuvBL2 complex. A number of our results indicate that the architecture of the human RuvBL1–RuvBL2 complex does not fit the recent structural model of the yeast Rvb1–Rvb2 complex.

APA, Harvard, Vancouver, ISO, and other styles

8

Mu, Xin, Yajing Fu, Yiping Zhu, et al. "HIV-1 Exploits the Host Factor RuvB-like 2 to Balance Viral Protein Expression." Cell Host & Microbe 18, no. 2 (2015): 233–42. http://dx.doi.org/10.1016/j.chom.2015.06.018.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

Makino, Yasutaka, Masato Kanemaki, Yumiko Kurokawa, Takehiko Koji, and Taka-aki Tamura. "A Rat RuvB-like Protein, TIP49a, Is a Germ Cell-enriched Novel DNA Helicase." Journal of Biological Chemistry 274, no. 22 (1999): 15329–35. http://dx.doi.org/10.1074/jbc.274.22.15329.

Full text

APA, Harvard, Vancouver, ISO, and other styles

10

Gorynia, Sabine, Pedro M. Matias, Susana Gonçalves, et al. "Expression, purification, crystallization and preliminary X-ray analysis of the human RuvB-like protein RuvBL1." Acta Crystallographica Section F Structural Biology and Crystallization Communications 62, no. 1 (2005): 61–66. http://dx.doi.org/10.1107/s1744309105041400.

Full text

APA, Harvard, Vancouver, ISO, and other styles

11

Sawitzke, J. A., and F. W. Stahl. "Phage lambda has an analog of Escherichia coli recO, recR and recF genes." Genetics 130, no. 1 (1992): 7–16. http://dx.doi.org/10.1093/genetics/130.1.7.

Full text

Abstract:

Abstract The RecF pathway catalyzes generalized recombination in Escherichia coli that is mutant for recBC, sbcB and sbcC. This pathway operating on conjugational recombination requires the recA, recF, recJ, recN, recO, recQ, recR, ruvA, ruvB and ruvC genes. In contrast, lambda mutant for its own recombination genes, int, red alpha and red beta, requires only the recA and recJ genes to recombine efficiently in recBC sbcB sbcC cells. Deletion of an open reading frame in the ninR region of lambda results in an additional requirement for recO, recR and recF in order to recombine in recBC sbcB sbcC mutant cells. This function, designated orf for recO-, recR- and recF-like function, is largely RecF pathway specific.

APA, Harvard, Vancouver, ISO, and other styles

12

Rousseau, Benoît, Ludovic Ménard, Valérie Haurie, et al. "Overexpression and role of the ATPase and putative DNA helicase RuvB-like 2 in human hepatocellular carcinoma." Hepatology 46, no. 4 (2007): 1108–18. http://dx.doi.org/10.1002/hep.21770.

Full text

APA, Harvard, Vancouver, ISO, and other styles

13

Hong, Soomin, Junghyun Jo, Hyung Joon Kim, et al. "RuvB-Like Protein 2 (Ruvbl2) Has a Role in Directing the Neuroectodermal Differentiation of Mouse Embryonic Stem Cells." Stem Cells and Development 25, no. 18 (2016): 1376–85. http://dx.doi.org/10.1089/scd.2016.0076.

Full text

APA, Harvard, Vancouver, ISO, and other styles

14

Wang, Cheng-Wei, Wan-Chieh Chen, Li-Jing Lin, Chung-Tsai Lee, Tung-Hai Tseng, and Wei-Ming Leu. "OIP30, a RuvB-Like DNA Helicase 2, is a Potential Substrate for the Pollen-Predominant OsCPK25/26 in Rice." Plant and Cell Physiology 52, no. 9 (2011): 1641–56. http://dx.doi.org/10.1093/pcp/pcr094.

Full text

APA, Harvard, Vancouver, ISO, and other styles

15

Zimmermann, Fabian, Marina Serna, Artur Ezquerra, Rafael Fernandez-Leiro, Oscar Llorca та Jens Luders. "Assembly of the asymmetric human γ-tubulin ring complex by RUVBL1-RUVBL2 AAA ATPase". Science Advances 6, № 51 (2020): eabe0894. http://dx.doi.org/10.1126/sciadv.abe0894.

Full text

Abstract:

The microtubule nucleator γ-tubulin ring complex (γTuRC) is essential for the function of microtubule organizing centers such as the centrosome. Since its discovery over two decades ago, γTuRC has evaded in vitro reconstitution and thus detailed structure-function studies. Here, we show that a complex of RuvB-like protein 1 (RUVBL1) and RUVBL2 “RUVBL” controls assembly and composition of γTuRC in human cells. Likewise, RUVBL assembles γTuRC from a minimal set of core subunits in a heterologous coexpression system. RUVBL interacts with γTuRC subcomplexes but is not part of fully assembled γTuRC. Purified, reconstituted γTuRC has nucleation activity and resembles native γTuRC as revealed by its cryo–electron microscopy (cryo-EM) structure at ~4.0-Å resolution. We further use cryo-EM to identify features that determine the intricate, higher-order γTuRC architecture. Our work finds RUVBL as an assembly factor that regulates γTuRC in cells and allows production of recombinant γTuRC for future in-depth mechanistic studies.

APA, Harvard, Vancouver, ISO, and other styles

16

Gohshi, T., M. Shimada, S. Kawahire, et al. "Molecular Cloning of Mouse p47, a Second Group Mammalian RuvB DNA Helicase-Like Protein: Homology with Those from Human and Saccharomyces cerevisiae." Journal of Biochemistry 125, no. 5 (1999): 939–46. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a022372.

Full text

APA, Harvard, Vancouver, ISO, and other styles

17

Wang, Yimeng, Jianhong Zhou, Samuel G. Mackintosh, and Yuchun Du. "RuvB-Like Protein 2 Interacts with the NS1 Protein of Influenza A Virus and Affects Apoptosis That Is Counterbalanced by Type I Interferons." Viruses 13, no. 6 (2021): 1038. http://dx.doi.org/10.3390/v13061038.

Full text

Abstract:

The NS1 protein of influenza A virus (IAV) plays important roles in viral pathogenesis and host immune response. Through a proteomic approach, we have identified RuvB-like proteins 1 and 2 (RuvBL1 and RuvBL2) as interacting partners of the NS1 protein of IAVs. Infection of human lung A549 cells with A/PR/8/34 (PR8) virus resulted in reductions in the protein levels of RuvBL2 but not RuvBL1. Further studies with RuvBL2 demonstrated that the NS1-RuvBL2 interaction is RNA-independent, and RuvBL2 binds the RNA-binding domain of the NS1. Infection of interferon (IFN)-deficient Vero cells with wild-type or delNS1 PR8 virus reduced RuvBL2 protein levels and induced apoptosis; delNS1 virus caused more reductions in RuvBL2 protein levels and induced more apoptosis than did wild-type virus. Knockdown of RuvBL2 by siRNAs induced apoptosis and overexpression of RuvBL2 resulted in increased resistance to infection-induced apoptosis in Vero cells. These results suggest that a non-NS1 viral element or elements induce apoptosis by suppressing RuvBL2 protein levels, and the NS1 inhibits the non-NS1 viral element-induced apoptosis by maintaining RuvBL2 abundance in infected cells in the absence of IFN influence. In contrast to Vero cells, infection of IFN-competent A549 cells with PR8 virus caused reductions in RuvBL2 protein levels but did not induce apoptosis. Concomitantly, pretreatment of Vero cells with a recombinant IFN resulted in resistance to infection-induced apoptosis. These results demonstrate that the infection-induced, RuvBL2-regulated apoptosis in infected cells is counterbalanced by IFN survival signals. Our results reveal a novel mechanism underlying the infection-induced apoptosis that can be modulated by the NS1 and type I IFN signaling in IAV-infected cells.

APA, Harvard, Vancouver, ISO, and other styles

18

Ju, Dapeng, Wei Zhang, Jiawei Yan, et al. "Chemical perturbations reveal that RUVBL2 regulates the circadian phase in mammals." Science Translational Medicine 12, no. 542 (2020): eaba0769. http://dx.doi.org/10.1126/scitranslmed.aba0769.

Full text

Abstract:

Transcriptional regulation lies at the core of the circadian clockwork, but how the clock-related transcription machinery controls the circadian phase is not understood. Here, we show both in human cells and in mice that RuvB-like ATPase 2 (RUVBL2) interacts with other known clock proteins on chromatin to regulate the circadian phase. Pharmacological perturbation of RUVBL2 with the adenosine analog compound cordycepin resulted in a rapid-onset 12-hour clock phase-shift phenotype at human cell, mouse tissue, and whole-animal live imaging levels. Using simple peripheral injection treatment, we found that cordycepin penetrated the blood-brain barrier and caused rapid entrainment of the circadian phase, facilitating reduced duration of recovery in a mouse jet-lag model. We solved a crystal structure for human RUVBL2 in complex with a physiological metabolite of cordycepin, and biochemical assays showed that cordycepin treatment caused disassembly of an interaction between RUVBL2 and the core clock component BMAL1. Moreover, we showed with spike-in ChIP-seq analysis and binding assays that cordycepin treatment caused disassembly of the circadian super-complex, which normally resides at E-box chromatin loci such as PER1, PER2, DBP, and NR1D1. Mathematical modeling supported that the observed type 0 phase shifts resulted from derepression of E-box clock gene transcription.

APA, Harvard, Vancouver, ISO, and other styles

19

Ohdate, Hidezumi, Chun Ren Lim, Tetsuro Kokubo, Kenichi Matsubara, Yukio Kimata, and Kenji Kohno. "Impairment of the DNA Binding Activity of the TATA-binding Protein Renders the Transcriptional Function of Rvb2p/Tih2p, the Yeast RuvB-like Protein, Essential for Cell Growth." Journal of Biological Chemistry 278, no. 17 (2003): 14647–56. http://dx.doi.org/10.1074/jbc.m213220200.

Full text

APA, Harvard, Vancouver, ISO, and other styles

20

Doyon, Yannick, William Selleck, William S. Lane, Song Tan, and Jacques Côté. "Structural and Functional Conservation of the NuA4 Histone Acetyltransferase Complex from Yeast to Humans." Molecular and Cellular Biology 24, no. 5 (2004): 1884–96. http://dx.doi.org/10.1128/mcb.24.5.1884-1896.2004.

Full text

Abstract:

ABSTRACT The NuA4 histone acetyltransferase (HAT) multisubunit complex is responsible for acetylation of histone H4 and H2A N-terminal tails in yeast. Its catalytic component, Esa1, is essential for cell cycle progression, gene-specific regulation and has been implicated in DNA repair. Almost all NuA4 subunits have clear homologues in higher eukaryotes, suggesting that the complex is conserved throughout evolution to metazoans. We demonstrate here that NuA4 complexes are indeed present in human cells. Tip60 and its splice variant Tip60b/PLIP were purified as stable HAT complexes associated with identical polypeptides, with 11 of the 12 proteins being homologs of yeast NuA4 subunits. This indicates a highly conserved subunit composition and the identified human proteins underline the role of NuA4 in the control of mammalian cell proliferation. ING3, a member of the ING family of growth regulators, links NuA4 to p53 function which we confirmed in vivo. Proteins specific to the human NuA4 complexes include ruvB-like helicases and a bromodomain-containing subunit linked to ligand-dependent transcription activation by the thyroid hormone receptor. We also demonstrate that subunits MRG15 and DMAP1 are present in distinct protein complexes harboring histone deacetylase and SWI2-related ATPase activities, respectively. Finally, analogous to yeast, a recombinant trimeric complex formed by Tip60, EPC1, and ING3 is sufficient to reconstitute robust nucleosomal HAT activity in vitro. In conclusion, the NuA4 HAT complex is highly conserved in eukaryotes, in which it plays primary roles in transcription, cellular response to DNA damage, and cell cycle control.

APA, Harvard, Vancouver, ISO, and other styles

21

Castorena, Carlos M., James G. MacKrell, Jonathan S. Bogan, Makoto Kanzaki, and Gregory D. Cartee. "Clustering of GLUT4, TUG, and RUVBL2 protein levels correlate with myosin heavy chain isoform pattern in skeletal muscles, but AS160 and TBC1D1 levels do not." Journal of Applied Physiology 111, no. 4 (2011): 1106–17. http://dx.doi.org/10.1152/japplphysiol.00631.2011.

Full text

Abstract:

Skeletal muscle is a heterogeneous tissue. To further elucidate this heterogeneity, we probed relationships between myosin heavy chain (MHC) isoform composition and abundance of GLUT4 and four other proteins that are established or putative GLUT4 regulators [Akt substrate of 160 kDa (AS160), Tre-2/Bub2/Cdc 16-domain member 1 (TBC1D1), Tethering protein containing an UBX-domain for GLUT4 (TUG), and RuvB-like protein two (RUVBL2)] in 12 skeletal muscles or muscle regions from Wistar rats [adductor longus, extensor digitorum longus, epitrochlearis, gastrocnemius (mixed, red, and white), plantaris, soleus, tibialis anterior (red and white), tensor fasciae latae, and white vastus lateralis]. Key results were 1) significant differences found among the muscles (range of muscle expression values) for GLUT4 (2.5-fold), TUG (1.7-fold), RUVBL2 (2.0-fold), and TBC1D1 (2.7-fold), but not AS160; 2) significant positive correlations for pairs of proteins: GLUT4 vs. TUG ( R = 0.699), GLUT4 vs. RUVBL2 ( R = 0.613), TUG vs. RUVBL2 ( R = 0.564), AS160 vs. TBC1D1 ( R = 0.293), and AS160 vs. TUG ( R = 0.246); 3) significant positive correlations for %MHC-I: GLUT4 ( R = 0.460), TUG ( R = 0.538), and RUVBL2 ( R = 0.511); 4) significant positive correlations for %MHC-IIa: GLUT4 ( R = 0.293) and RUVBL2 ( R = 0.204); 5) significant negative correlations for %MHC-IIb vs. GLUT4 ( R = −0.642), TUG ( R = −0.626), and RUVBL2 ( R = −0.692); and 6) neither AS160 nor TBC1D1 significantly correlated with MHC isoforms. In 12 rat muscles, GLUT4 abundance tracked with TUG and RUVBL2 and correlated with MHC isoform expression, but was unrelated to AS160 or TBC1D1. Our working hypothesis is that some of the mechanisms that regulate GLUT4 abundance in rat skeletal muscle also influence TUG and RUVBL2 abundance.

APA, Harvard, Vancouver, ISO, and other styles

22

Gorynia, Sabine. "RuvB-like 1 - [Isoform 1]." Targeted Protein Database, May 19, 2008. http://dx.doi.org/10.2970/tpdb.2008.144.

Full text

APA, Harvard, Vancouver, ISO, and other styles

23

Haurie, V., A. Grigoletto, and J. Rosenbaum. "RUVBL1 (RuvB-like 1 (E. coli))." Atlas of Genetics and Cytogenetics in Oncology and Haematology, no. 3 (November 2011). http://dx.doi.org/10.4267/2042/44703.

Full text

APA, Harvard, Vancouver, ISO, and other styles

24

Grigoletto, A., V. Haurie, and J. Rosenbaum. "RUVBL2 (RuvB-like 2 (E. coli))." Atlas of Genetics and Cytogenetics in Oncology and Haematology, no. 3 (November 2011). http://dx.doi.org/10.4267/2042/44704.

Full text

APA, Harvard, Vancouver, ISO, and other styles

25

Silva, Sara T. N., José A. Brito, Rocío Arranz, et al. "X-ray structure of full-length human RuvB-Like 2 – mechanistic insights into coupling between ATP binding and mechanical action." Scientific Reports 8, no. 1 (2018). http://dx.doi.org/10.1038/s41598-018-31997-z.

Full text

APA, Harvard, Vancouver, ISO, and other styles

26

Yan, Tao, Fang Liu, Jiajia Gao, et al. "Multilevel regulation of RUVBL2 expression predicts poor prognosis in hepatocellular carcinoma." Cancer Cell International 19, no. 1 (2019). http://dx.doi.org/10.1186/s12935-019-0974-z.

Full text

Abstract:

Abstract Background Hepatocellular carcinoma (HCC) is the second-most lethal cancer worldwide with a complex pathogenesis. RuvB-like 2 (RUVBL2) was previously found to contribute to hepatocarcinogenesis. However, its expression, regulation and clinical significance have not been systematically evaluated in a large number of clinical samples. Methods Here, we performed a comprehensive analysis of RUVBL2 based on multiple datasets from 371 liver cancer patients of The Cancer Genome Atlas (TCGA) and on immunohistochemical staining in 153 subjects. In addition, the aberrant signaling pathways caused by RUVBL2 overexpression were investigated. Results We demonstrated that promoter hypomethylation, copy number gain, MYC amplification and CTNNB1 mutation were all responsible for RUVBL2 overexpression in HCC. High levels of RUVBL2 mRNA were associated with shorter recurrence-free survival time (RFS) but not overall survival time (OS). Furthermore, RUVBL2 protein was overexpressed in the nucleus and cytoplasm of HCC samples. Univariate and multivariate survival analyses showed that strong nuclear and cytoplasmic staining of RUVBL2 independently predicted worse OS and RFS with a 2.03-fold and a 1.71-fold increase in the hazard ratio, respectively. High levels of RUVBL2 promoted carcinogenesis through the heat shock protein 90 (HSP90)-Cell Division Cycle 37 (CDC37), AKT serine/threonine kinase (AKT) and mitogen-activated protein kinase (ERK/MAPK) pathways. Conclusion The deregulation of RUVBL2 in HCC is influenced at the genomic, epigenetic and transcriptional levels. Our findings highlight the potential roles of RUVBL2 as a promising prognostic marker as well as a therapeutic target for HCC.

APA, Harvard, Vancouver, ISO, and other styles

27

Liu, Qi, Wei Jiang, Yun Chen, Manyu Zhang, Xiaoling Geng, and Quan Wang. "Study on Circulating Antigens in Serum of Mice With Experimental Acute Toxoplasmosis." Frontiers in Microbiology 11 (January 18, 2021). http://dx.doi.org/10.3389/fmicb.2020.612252.

Full text

Abstract:

Toxoplasma gondii is a ubiquitous apicomplexan protozoan parasite that can infect all warm-blooded animals, causing toxoplasmosis. Thus, efficient diagnosis methods for acute T. gondii infection are essential for its management. Circulating antigens (CAgs) are reliable diagnostic indicators of acute infection. In this study, we established a mouse model of acute T. gondii infection and explored new potential diagnostic factors. CAgs levels peaked 60 h after T. gondii inoculation and 31 CAgs were identified by immunoprecipitation-liquid chromatography-tandem mass spectrometry, among which RuvB-like helicase (TgRuvBL1), ribonuclease (TgRNaseH1), and ribosomal protein RPS2 (TgRPS2) were selected for prokaryotic expression. Polyclonal antibodies against these three proteins were prepared. Results from indirect enzyme-linked immunosorbent assay indicated that anti-rTgRuvBL1, anti-rTgRNase H1, and anti-rTgRPS2 mouse sera were recognized by natural excretory-secretory antigens from T. gondii tachyzoites. Moreover, immunofluorescence assays revealed that TgRuvBL1 was localized in the nucleus, while TgRNase H1 and TgRPS2 were in the apical end. Western blotting data confirmed the presence of the three proteins in the sera of the infected mice. Moreover, mice immunized with rTgRuvBL1 (10.0 ± 0.30 days), TgRNaseH1 (9.67 ± 0.14 days), or rTgRPS2 (11.5 ± 0.34 days) had slightly longer lifespan when challenged with a virulent T. gondii RH strain. Altogether, these findings indicate that these three proteins can potentially be diagnostic candidates for acute toxoplasmosis. However, they hold poor protective potential against highly virulent T. gondii infection.

APA, Harvard, Vancouver, ISO, and other styles

28

Zang, Xupeng, Ting Gu, Qun Hu, et al. "Global Transcriptomic Analyses Reveal Genes Involved in Conceptus Development During the Implantation Stages in Pigs." Frontiers in Genetics 12 (February 24, 2021). http://dx.doi.org/10.3389/fgene.2021.584995.

Full text

Abstract:

Prenatal mortality remains a significant concern to the pig farming industry around the world. Spontaneous fetal loss ranging from 20 to 45% by term occur after fertilization, with most of the loss happening during the implantation period. Since the factors regulating the high mortality rates of early conceptus during implantation phases are poorly understood, we sought to analyze the overall gene expression changes during this period, and identify the molecular mechanisms involved in conceptus development. This work employed Illumina’s next-generation sequencing (RNA-Seq) and quantitative real-time PCR to analyze differentially expressed genes (DEGs). Soft clustering was subsequently used for the cluster analysis of gene expression. We identified 8236 DEGs in porcine conceptus at day 9, 12, and 15 of pregnancy. Annotation analysis of these genes revealed rRNA processing (GO:0006364), cell adhesion (GO:1904874), and heart development (GO:0007507), as the most significantly enriched biological processes at day 9, 12, and 15 of pregnancy, respectively. In addition, we found various genes, such as T-complex 1, RuvB-like AAA ATPase 2, connective tissue growth factor, integrins, interferon gamma, SLA-1, chemokine ligand 9, PAG-2, transforming growth factor beta receptor 1, and Annexin A2, that play essential roles in conceptus morphological development and implantation in pigs. Furthermore, we investigated the function of PAG-2 in vitro and found that PAG-2 can inhibit trophoblast cell proliferation and migration. Our analysis provides a valuable resource for understanding the mechanisms of conceptus development and implantation in pigs.

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!