The Structure of Rat Liver Vault at 3.5 Angstrom Resolution

Tanaka, Hideaki; Kato, Kuniki; Yamashita, Eiki; Sumizawa, Tomoyuki; Zhou, Yong; Yao, Min; Iwasaki, Katsunori; Yoshimura, Masato; Tsukihara, Tomitake

doi:10.1126/science.1164975

Cited by 135 publications

(211 citation statements)

References 30 publications

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“…1B). It was proposed that the interactions between the 42-turn-long cap helix domains of MVP are essential for stabilizing the vault particle (13).…”

Section: Introductionmentioning

confidence: 99%

“…In the vault particle, the TEP1 protein was shown to be important for vRNA binding and stabilization of the vault complex (9,12). The TEP1 found to locate at the terminal ends of the vault particle, based on the crystal structure of the whole vault particle, isolated from the rat, at 3.5 Å resolution (13). The vault particle consists of a dimer of half-vaults, comprising 39 identical MVP monomers.…”

Section: Introductionmentioning

confidence: 99%

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Expression of Noncoding Vault RNA in Human Malignant Cells and Its Importance in Mitoxantrone Resistance

Gopinath

Wadhwa

Kumar

2010

Molecular Cancer Research

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Several noncoding RNAs do vital cellular functions, including gene regulation and cell differentiation. Previously, we reported that vault RNA (vRNA) has the ability to recognize chemotherapeutic compounds, such as mitoxantrone, based on biophysical and biochemical analyses. In the present study, we show that human glioblastoma-, leukemia-, and osteocarcinoma-derived cell lines overexpress vRNA and exhibit higher resistance toward mitoxantrone. Interestingly, when vRNA expression was suppressed by RNA interference in these cells, the resistance progressively decreased. In agreement with these findings, overexpression of vRNA-1 caused resistance to mitoxantrone. These results suggest a role of vRNA in mitoxantrone resistance in malignant cells and justify further studies on the importance and application of noncoding RNAs in cancer chemotherapeutics. Mol Cancer Res; 8(11); 1536-46. ©2010 AACR.

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“…1B). It was proposed that the interactions between the 42-turn-long cap helix domains of MVP are essential for stabilizing the vault particle (13).…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Expression of Noncoding Vault RNA in Human Malignant Cells and Its Importance in Mitoxantrone Resistance

Gopinath

Wadhwa

Kumar

2010

Molecular Cancer Research

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“…Tϭ1 inner cores of dsRNA viruses are generally known to be critical for genome replication (minus-strand synthesis) and transcription (plusstrand synthesis), since the viral-RNA-dependent RNA polymerase(s) (RdRp) is frequently packaged as an integral component of the capsid. Nanocompartments built entirely of protein subunits with enzymatic activity are found in all domains of life, from the bacterial carboxysome (65) to the eukaryotic vault particle (64). dsRNA, single-stranded RNA (ssRNA) with secondary structure, and dsRNA-containing replication intermediates synthesized during viral infections in plants, animals, and fungi are potent inducers of host cell responses (27,38).…”

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confidence: 99%

The T=1 Capsid Protein of Penicillium chrysogenum Virus Is Formed by a Repeated Helix-Rich Core Indicative of Gene Duplication

Luque

González

Garriga

et al. 2010

J Virol

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Penicillium chrysogenum virus (PcV), a member of the Chrysoviridae family, is a double-stranded RNA (dsRNA) fungal virus with a multipartite genome, with each RNA molecule encapsidated in a separate particle. Chrysoviruses lack an extracellular route and are transmitted during sporogenesis and cell fusion. The PcV capsid, based on a T‫1؍‬ lattice containing 60 subunits of the 982-amino-acid capsid protein, remains structurally undisturbed throughout the viral cycle, participates in genome metabolism, and isolates the virus genome from host defense mechanisms. Using three-dimensional cryoelectron microscopy, we determined the structure of the PcV virion at 8.0 Å resolution. The capsid protein has a high content of rod-like densities characteristic of ␣-helices, forming a repeated ␣-helical core indicative of gene duplication. Whereas the PcV capsid protein has two motifs with the same fold, most dsRNA virus capsid subunits consist of dimers of a single protein with similar folds. The spatial arrangement of the ␣-helical core resembles that found in the capsid protein of the L-A virus, a fungal totivirus with an undivided genome, suggesting a conserved basic fold. The encapsidated genome is organized in concentric shells; whereas the inner dsRNA shells are well defined, the outermost layer is dense due to numerous interactions with the inner capsid surface, specifically, six interacting areas per monomer. The outermost genome layer is arranged in an icosahedral cage, sufficiently well ordered to allow for modeling of an A-form dsRNA. The genome ordering might constitute a framework for dsRNA transcription at the capsid interior and/or have a structural role for capsid stability.Viruses with double-stranded RNA (dsRNA) genomes are found in a broad range of organisms, ranging from bacteria to simple (fungi and protozoa) and complex (animals and plants) eukaryotes.

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“…The encapsulation of drug exhibits a slowed drug release and results in a reduction in effective concentration of the anticancer agents. Furthermore, these vesicles may act as efflux effect by exocytosis which further reduces drug amount in cancer cells (Tanaka et al 2009). …”

Section: Drug Resistance From Cancer Cell Cytoplasmmentioning

confidence: 99%

Advances in investigations on the mechanism of cancer multidrug resistance and the liposomes-based treatment strategy

Zeng

et al. 2014

Journal of Pharmaceutical Investigation

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Multidrug resistance is a major cause that leads to the refractory of cancers after a combination strategy by chemotherapy, radiation and surgical treatment. Among the comprehensive treatment, chemotherapy still plays a crucial role in eliminating malignant cells. The objectives of present review were to elucidate the research advances in the mechanism of cancer multidrug resistance and the liposomes-based treatment strategy. The drug resistance could be related to cancer cells, heterogeneity, microenvironment, and physiological barriers. Drug resistance mechanisms, which involved in adenosine triphosphate (ATP)-binding cassette (ABC) transporters, cytoplasm, nucleus, apoptotic proteins, cancer stem cells, side-population cancer cells, angiogenesis, vasculogenic mimicry channels, extracellular matrix, and blood-brain barrier, were discussed. Latest advances in the nanostructured liposome treatment strategy were summarized, including regulating the overexpression of ABC transporters, and targeting treatments on mitochondria, apoptotic genes, cancer stem cells, cancer side-population cells, new blood vessels, vascular mimicry channels, extracellular matrix, and blood-brain barrier. These translational investigations provide new insights into current cancer therapy, and useful considerations for further developments of the liposomes-based treatment strategy.

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The Structure of Rat Liver Vault at 3.5 Angstrom Resolution

Cited by 135 publications

References 30 publications

Expression of Noncoding Vault RNA in Human Malignant Cells and Its Importance in Mitoxantrone Resistance

Expression of Noncoding Vault RNA in Human Malignant Cells and Its Importance in Mitoxantrone Resistance

The T=1 Capsid Protein of Penicillium chrysogenum Virus Is Formed by a Repeated Helix-Rich Core Indicative of Gene Duplication

Advances in investigations on the mechanism of cancer multidrug resistance and the liposomes-based treatment strategy

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