scholarly journals TRUE Gene Silencing: Screening of a Heptamer-type Small Guide RNA Library for Potential Cancer Therapeutic Agents

10.3791/53879 ◽  
2016 ◽  
Author(s):  
Arisa Haino ◽  
Tatsuya Ishikawa ◽  
Mineaki Seki ◽  
Masayuki Nashimoto
Keyword(s):  
Gene Silencing ◽  
Therapeutic Agents ◽  
Guide Rna ◽  
Potential Cancer

TRUE Gene Silencing: Unique Gene Silencing by the tRNA Maturase tRNase ZL under the Direction of Small-guide RNA

2007 ◽  
Vol 49 (1) ◽  
pp. 54-64
Author(s):  
Aiko Nakashima ◽  
Masayuki Nashimoto ◽  
Masato Tamura
Keyword(s):  
Gene Silencing ◽  
Guide Rna ◽  
Unique Gene

scholarly journals Human Argonaute2 and Argonaute3 are catalytically activated by different lengths of guide RNA

2020 ◽  
Author(s):  
Mi Seul Park ◽  
GeunYoung Sim ◽  
Audrey C. Kehling ◽  
Kotaro Nakanishi
Keyword(s):  
Gene Silencing ◽  
Fold Increase ◽  
Specific Gene ◽  
Small Interfering Rnas ◽  
Guide Rna ◽  
Guide Rnas ◽  
Argonaute Proteins ◽  
Complementary Rnas ◽  
Standing Question

AbstractRNA interfering is a eukaryote-specific gene silencing by 20∼23 nucleotide (nt) microRNAs and small interfering RNAs that recruit Argonaute proteins to complementary RNAs for degradation. In humans, Argonaute2 (AGO2) has been known as the only slicer while Argonaute3 (AGO3) barely cleaves RNAs. Therefore, the intrinsic slicing activity of AGO3 remains controversial and a long-standing question. Here, we report 14-nt 3′ end-shortened variants of let-7a, miR-27a, and specific miR-17-92 families that make AGO3 an extremely competent slicer by an ∼ 82-fold increase in target cleavage. These RNAs, named cleavage-inducing tiny guide RNAs (cityRNAs), conversely lower the activity of AGO2, demonstrating that AGO2 and AGO3 have different optimum guide lengths for target cleavage. Our study sheds light on the role of tiny guide RNAs.

Synthesis of pheophorbide-a conjugates with anticancer drugs as potential cancer diagnostic and therapeutic agents

2011 ◽  
Vol 19 (18) ◽  
pp. 5383-5391 ◽  
Author(s):  
Hyun You ◽  
Hyo-Eun Yoon ◽  
Jung-Hoon Yoon ◽  
Hyojin Ko ◽  
Yong-Chul Kim
Keyword(s):  
Anticancer Drugs ◽  
Therapeutic Agents ◽  
Pheophorbide A ◽  
Cancer Diagnostic ◽  
Potential Cancer

Autophagy Regulators as Potential Cancer Therapeutic agents: A Review

2015 ◽  
Vol 15 (8) ◽  
pp. 720-744 ◽  
Author(s):  
Shan Li ◽  
Lingfei Wang ◽  
Yongzhou Hu ◽  
Rong Sheng
Keyword(s):  
Therapeutic Agents ◽  
Potential Cancer

scholarly journals Human Argonaute2 and Argonaute3 are catalytically activated by different lengths of guide RNA

2020 ◽  
Vol 117 (46) ◽  
pp. 28576-28578
Author(s):  
Mi Seul Park ◽  
GeunYoung Sim ◽  
Audrey C. Kehling ◽  
Kotaro Nakanishi
Keyword(s):  
Gene Silencing ◽  
Specific Gene ◽  
Small Interfering Rnas ◽  
Guide Rna ◽  
Guide Rnas ◽  
Argonaute Proteins ◽  
Rna Interfering ◽  
Complementary Rnas ◽  
Standing Question

RNA interfering is a eukaryote-specific gene silencing by 20∼23-nucleotide (nt) microRNAs and small interfering RNAs that recruit Argonaute proteins to complementary RNAs for degradation. In humans, Argonaute2 (AGO2) has been known as the only slicer while Argonaute3 (AGO3) barely cleaves RNAs. Therefore, the intrinsic slicing activity of AGO3 remains controversial and a long-standing question. Here, we report 14-nt 3′ end-shortened variants of let-7a, miR-27a, and specific miR-17–92 families that make AGO3 an extremely competent slicer, increasing target cleavage up to ∼82-fold in some instances. These RNAs, named cleavage-inducing tiny guide RNAs (cityRNAs), conversely lower the activity of AGO2, demonstrating that AGO2 and AGO3 have different optimum guide lengths for target cleavage. Our study sheds light on the role of tiny guide RNAs.

TRUE Gene Silencing : Unique Gene Silencing by the tRNA Maturase tRNase ZL under the Direction of Small-guide RNA

2007 ◽  
Vol 49 (1) ◽  
pp. 54-64
Author(s):  
Aiko Nakashima ◽  
Masayuki Nashimoto ◽  
Masato Tamura
Keyword(s):  
Gene Silencing ◽  
Guide Rna ◽  
Unique Gene

scholarly journals Gene silencing by the tRNA maturase tRNase ZL under the direction of small-guide RNA

Gene Therapy ◽  
2006 ◽  
Vol 14 (1) ◽  
pp. 78-85 ◽  
Author(s):  
A Nakashima ◽  
H Takaku ◽  
H S Shibata ◽  
Y Negishi ◽  
M Takagi ◽  
...  
Keyword(s):  
Gene Silencing ◽  
Guide Rna

scholarly journals Structure-Based Development of Small Molecule PFKFB3 Inhibitors: A Framework for Potential Cancer Therapeutic Agents Targeting the Warburg Effect

PLoS ONE ◽  
2011 ◽  
Vol 6 (9) ◽  
pp. e24179 ◽  
Author(s):  
Minsuh Seo ◽  
Jeong-Do Kim ◽  
David Neau ◽  
Inder Sehgal ◽  
Yong-Hwan Lee
Keyword(s):  
Small Molecule ◽  
Warburg Effect ◽  
Therapeutic Agents ◽  
Potential Cancer ◽  
The Warburg Effect

scholarly journals Advances in Histone Demethylase KDM3A as a Cancer Therapeutic Target

Cancers ◽  
2020 ◽  
Vol 12 (5) ◽  
pp. 1098 ◽  
Author(s):  
Jung Yoo ◽  
Yu Hyun Jeon ◽  
Ha Young Cho ◽  
Sang Wu Lee ◽  
Go Woon Kim ◽  
...  
Keyword(s):  
Therapeutic Target ◽  
Structural Information ◽  
Therapeutic Agents ◽  
Histone Demethylase ◽  
Histone Demethylases ◽  
Selective Inhibitors ◽  
Lxxll Motif ◽  
Demethylase Activity ◽  
Potential Cancer ◽  
Insight Into

Lysine-specific histone demethylase 3 (KDM3) subfamily proteins are H3K9me2/me1 histone demethylases that promote gene expression. The KDM3 subfamily primarily consists of four proteins (KDM3A−D). All four proteins contain the catalytic Jumonji C domain (JmjC) at their C-termini, but whether KDM3C has demethylase activity is under debate. In addition, KDM3 proteins contain a zinc-finger domain for DNA binding and an LXXLL motif for interacting with nuclear receptors. Of the KDM3 proteins, KDM3A is especially deregulated or overexpressed in multiple cancers, making it a potential cancer therapeutic target. However, no KDM3A-selective inhibitors have been identified to date because of the lack of structural information. Uncovering the distinct physiological and pathological functions of KDM3A and their structure will give insight into the development of novel selective inhibitors. In this review, we focus on recent studies highlighting the oncogenic functions of KDM3A in cancer. We also discuss existing KDM3A-related inhibitors and review their potential as therapeutic agents for overcoming cancer.

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