Chidamide inhibits cell glycolysis in acute myeloid leukemia by decreasing N6-methyladenosine-related GNAS-AS1
Background Acute myeloid leukemia (AML) is a hematopoietic malignancy. Chidamide has shown anti-cancer effect in different malignancies. The function of Chidamide in glycolysis in AML cells remains unclear. Methods AML cells were treated with 1000 nM Chidamide for 48 h. The levels of long non-coding...
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| description | Background
Acute myeloid leukemia (AML) is a hematopoietic malignancy. Chidamide has shown anti-cancer effect in different malignancies. The function of Chidamide in glycolysis in AML cells remains unclear.
Methods
AML cells were treated with 1000 nM Chidamide for 48 h. The levels of long non-coding RNA-GNAS-AS1, miR-34a-5p, glycolysis-related proteins, and Ras homolog gene family (RhoA)/Rho-associated protein kinase (ROCK) signaling-related proteins were detected by qRT-PCR or western blot. Cell viability and apoptosis were measured by CCK-8 and flow cytometry. Glycolysis levels were measured by assay kits. GNAS-AS1 N6-methyladenosine (m6A) modification level was detected by methylated RNA immunoprecipitation sequencing. The combined targets of miR-34a-5p were validated using a dual-luciferase reporter assay. BALB/C nude mice were selected for subcutaneous tumor validation. Chidamide at a dosage of 25 mg/kg was used in the animal study.
Results
GNAS-AS1 promoted glycolysis in AML cells by upregulating the expression of glycolysis-related proteins and increasing glucose consumption, lactate production, ATP generation, and the extracellular acidification rate. Chidamide treatment suppressed WT1-associated protein (WTAP)-mediated RNA m6A modification of GNAS-AS1. Chidamide downregulated GNAS-AS1 to inhibit glycolysis in AML cells. GNAS-AS1 targeted miR-34a-5p to promote insulin-like growth factor 2 mRNA-binding protein (IGF2BP2) expression. IGF2BP2 inhibition reversed the promoting effect of miR-34a-5p knockdown on glycolysis and RhoA/ROCK pathway in Chidamide-treated cells. GNAS-AS1 overexpression abolished the inhibitory effect of Chidamide on AML tumorigenesis in vivo by modulating the RhoA/ROCK pathway.
Conclusion
Chidamide inhibited glycolysis in AML by repressing WTAP-mediated GNAS-AS1 m6A modification and then regulating the miR-34a-5p/IGF2BP2 axis.
Graphical abstract |
| doi_str_mv | 10.1007/s40199-023-00482-y |
| format | Article |
| fullrecord | <record><control><sourceid>gale_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_11087453</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A771647144</galeid><sourcerecordid>A771647144</sourcerecordid><originalsourceid>FETCH-LOGICAL-c573t-f0e6df80f6471f9845964ac16636620e8f0a0168c8b123613aa538edce07c34d3</originalsourceid><addsrcrecordid>eNp9kk9v1DAQxSMEoqXwBTigSEiIS8r4T2zvCa1WUJCqciicLa8z2bg4dokTpHx7HLa0uwghH2zN_OZZ8_SK4iWBcwIg3yUOZLWqgLIKgCtazY-KUwqgKkoZeXzwPimepXQDwBQX9GlxwuSKCinoaRE2nWtM7xosXejc1o2ptOh9ufOzjX5OLuVGaew0YtnP6KNrSo_Td-ydKbdz2aAd0CQXduWVqHocu9mbBkPMJawG9GbEpry4Wl9X62vyvHjSGp_wxd19Vnz7-OHr5lN1-eXi82Z9WdlasrFqAUXTKmgFl6RdKV6vBDeWCMGEoICqBQNEKKu2hDJBmDE1U9hYBGkZb9hZ8X6veztt-6UexsF4fTu43gyzjsbp405wnd7Fn5oQUJLXLCu8vVMY4o8J06h7lxZnTMA4JU2VEgIIk3VGX_-F3sRpCHk_zaBmNa-lkg_UznjULrQxf2wXUb2Wkiybcp6p839Q-TTZcBsDti7XjwbeHAx0aPzYpein0cWQjkG6B-0QUxqwvXeDgF7ypPd50jlP-nee9JyHXh36eD_yJ0AZYHsg5VbY4fCw-39kfwEAbNSG</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>3053545787</pqid></control><display><type>article</type><title>Chidamide inhibits cell glycolysis in acute myeloid leukemia by decreasing N6-methyladenosine-related GNAS-AS1</title><source>MEDLINE</source><source>Springer journals</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>Free Full-Text Journals in Chemistry</source><creator>Hu, Changmei ; Fu, Xiao ; Li, Shujun ; Chen, Cong ; Zhao, Xielan ; Peng, Jie</creator><creatorcontrib>Hu, Changmei ; Fu, Xiao ; Li, Shujun ; Chen, Cong ; Zhao, Xielan ; Peng, Jie</creatorcontrib><description>Background
Acute myeloid leukemia (AML) is a hematopoietic malignancy. Chidamide has shown anti-cancer effect in different malignancies. The function of Chidamide in glycolysis in AML cells remains unclear.
Methods
AML cells were treated with 1000 nM Chidamide for 48 h. The levels of long non-coding RNA-GNAS-AS1, miR-34a-5p, glycolysis-related proteins, and Ras homolog gene family (RhoA)/Rho-associated protein kinase (ROCK) signaling-related proteins were detected by qRT-PCR or western blot. Cell viability and apoptosis were measured by CCK-8 and flow cytometry. Glycolysis levels were measured by assay kits. GNAS-AS1 N6-methyladenosine (m6A) modification level was detected by methylated RNA immunoprecipitation sequencing. The combined targets of miR-34a-5p were validated using a dual-luciferase reporter assay. BALB/C nude mice were selected for subcutaneous tumor validation. Chidamide at a dosage of 25 mg/kg was used in the animal study.
Results
GNAS-AS1 promoted glycolysis in AML cells by upregulating the expression of glycolysis-related proteins and increasing glucose consumption, lactate production, ATP generation, and the extracellular acidification rate. Chidamide treatment suppressed WT1-associated protein (WTAP)-mediated RNA m6A modification of GNAS-AS1. Chidamide downregulated GNAS-AS1 to inhibit glycolysis in AML cells. GNAS-AS1 targeted miR-34a-5p to promote insulin-like growth factor 2 mRNA-binding protein (IGF2BP2) expression. IGF2BP2 inhibition reversed the promoting effect of miR-34a-5p knockdown on glycolysis and RhoA/ROCK pathway in Chidamide-treated cells. GNAS-AS1 overexpression abolished the inhibitory effect of Chidamide on AML tumorigenesis in vivo by modulating the RhoA/ROCK pathway.
Conclusion
Chidamide inhibited glycolysis in AML by repressing WTAP-mediated GNAS-AS1 m6A modification and then regulating the miR-34a-5p/IGF2BP2 axis.
Graphical abstract</description><identifier>ISSN: 2008-2231</identifier><identifier>ISSN: 1560-8115</identifier><identifier>EISSN: 2008-2231</identifier><identifier>DOI: 10.1007/s40199-023-00482-y</identifier><identifier>PMID: 37926762</identifier><language>eng</language><publisher>Cham: Springer International Publishing</publisher><subject>Adenosine - analogs & derivatives ; Adenosine - pharmacology ; Aminopyridines - pharmacology ; Animals ; Antineoplastic Agents - pharmacology ; Apoptosis ; Apoptosis - drug effects ; Benzamides - pharmacology ; Biomedical and Life Sciences ; Biomedicine ; Cancer ; Care and treatment ; Cell Line, Tumor ; Cell Survival - drug effects ; Glucose metabolism ; Glycolysis - drug effects ; Humans ; Kinases ; Lactates ; Leukemia ; Leukemia, Myeloid, Acute - drug therapy ; Leukemia, Myeloid, Acute - genetics ; Leukemia, Myeloid, Acute - metabolism ; Medicinal Chemistry ; Methyltransferases ; Mice ; Mice, Inbred BALB C ; Mice, Nude ; MicroRNAs - genetics ; Pharmaceutical Sciences/Technology ; Pharmacology/Toxicology ; Protein binding ; Protein kinases ; Proteins ; Research Article ; RNA ; Xenograft Model Antitumor Assays</subject><ispartof>Daru, 2023-11, Vol.32 (1), p.11-24</ispartof><rights>The Author(s), under exclusive licence to Tehran University of Medical Sciences 2023. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.</rights><rights>2023. The Author(s), under exclusive licence to Tehran University of Medical Sciences.</rights><rights>COPYRIGHT 2023 BioMed Central Ltd.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c573t-f0e6df80f6471f9845964ac16636620e8f0a0168c8b123613aa538edce07c34d3</citedby><cites>FETCH-LOGICAL-c573t-f0e6df80f6471f9845964ac16636620e8f0a0168c8b123613aa538edce07c34d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC11087453/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC11087453/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,41488,42557,51319,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/37926762$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hu, Changmei</creatorcontrib><creatorcontrib>Fu, Xiao</creatorcontrib><creatorcontrib>Li, Shujun</creatorcontrib><creatorcontrib>Chen, Cong</creatorcontrib><creatorcontrib>Zhao, Xielan</creatorcontrib><creatorcontrib>Peng, Jie</creatorcontrib><title>Chidamide inhibits cell glycolysis in acute myeloid leukemia by decreasing N6-methyladenosine-related GNAS-AS1</title><title>Daru</title><addtitle>DARU J Pharm Sci</addtitle><addtitle>Daru</addtitle><description>Background
Acute myeloid leukemia (AML) is a hematopoietic malignancy. Chidamide has shown anti-cancer effect in different malignancies. The function of Chidamide in glycolysis in AML cells remains unclear.
Methods
AML cells were treated with 1000 nM Chidamide for 48 h. The levels of long non-coding RNA-GNAS-AS1, miR-34a-5p, glycolysis-related proteins, and Ras homolog gene family (RhoA)/Rho-associated protein kinase (ROCK) signaling-related proteins were detected by qRT-PCR or western blot. Cell viability and apoptosis were measured by CCK-8 and flow cytometry. Glycolysis levels were measured by assay kits. GNAS-AS1 N6-methyladenosine (m6A) modification level was detected by methylated RNA immunoprecipitation sequencing. The combined targets of miR-34a-5p were validated using a dual-luciferase reporter assay. BALB/C nude mice were selected for subcutaneous tumor validation. Chidamide at a dosage of 25 mg/kg was used in the animal study.
Results
GNAS-AS1 promoted glycolysis in AML cells by upregulating the expression of glycolysis-related proteins and increasing glucose consumption, lactate production, ATP generation, and the extracellular acidification rate. Chidamide treatment suppressed WT1-associated protein (WTAP)-mediated RNA m6A modification of GNAS-AS1. Chidamide downregulated GNAS-AS1 to inhibit glycolysis in AML cells. GNAS-AS1 targeted miR-34a-5p to promote insulin-like growth factor 2 mRNA-binding protein (IGF2BP2) expression. IGF2BP2 inhibition reversed the promoting effect of miR-34a-5p knockdown on glycolysis and RhoA/ROCK pathway in Chidamide-treated cells. GNAS-AS1 overexpression abolished the inhibitory effect of Chidamide on AML tumorigenesis in vivo by modulating the RhoA/ROCK pathway.
Conclusion
Chidamide inhibited glycolysis in AML by repressing WTAP-mediated GNAS-AS1 m6A modification and then regulating the miR-34a-5p/IGF2BP2 axis.
Graphical abstract</description><subject>Adenosine - analogs & derivatives</subject><subject>Adenosine - pharmacology</subject><subject>Aminopyridines - pharmacology</subject><subject>Animals</subject><subject>Antineoplastic Agents - pharmacology</subject><subject>Apoptosis</subject><subject>Apoptosis - drug effects</subject><subject>Benzamides - pharmacology</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Cancer</subject><subject>Care and treatment</subject><subject>Cell Line, Tumor</subject><subject>Cell Survival - drug effects</subject><subject>Glucose metabolism</subject><subject>Glycolysis - drug effects</subject><subject>Humans</subject><subject>Kinases</subject><subject>Lactates</subject><subject>Leukemia</subject><subject>Leukemia, Myeloid, Acute - drug therapy</subject><subject>Leukemia, Myeloid, Acute - genetics</subject><subject>Leukemia, Myeloid, Acute - metabolism</subject><subject>Medicinal Chemistry</subject><subject>Methyltransferases</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>Mice, Nude</subject><subject>MicroRNAs - genetics</subject><subject>Pharmaceutical Sciences/Technology</subject><subject>Pharmacology/Toxicology</subject><subject>Protein binding</subject><subject>Protein kinases</subject><subject>Proteins</subject><subject>Research Article</subject><subject>RNA</subject><subject>Xenograft Model Antitumor Assays</subject><issn>2008-2231</issn><issn>1560-8115</issn><issn>2008-2231</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kk9v1DAQxSMEoqXwBTigSEiIS8r4T2zvCa1WUJCqciicLa8z2bg4dokTpHx7HLa0uwghH2zN_OZZ8_SK4iWBcwIg3yUOZLWqgLIKgCtazY-KUwqgKkoZeXzwPimepXQDwBQX9GlxwuSKCinoaRE2nWtM7xosXejc1o2ptOh9ufOzjX5OLuVGaew0YtnP6KNrSo_Td-ydKbdz2aAd0CQXduWVqHocu9mbBkPMJawG9GbEpry4Wl9X62vyvHjSGp_wxd19Vnz7-OHr5lN1-eXi82Z9WdlasrFqAUXTKmgFl6RdKV6vBDeWCMGEoICqBQNEKKu2hDJBmDE1U9hYBGkZb9hZ8X6veztt-6UexsF4fTu43gyzjsbp405wnd7Fn5oQUJLXLCu8vVMY4o8J06h7lxZnTMA4JU2VEgIIk3VGX_-F3sRpCHk_zaBmNa-lkg_UznjULrQxf2wXUb2Wkiybcp6p839Q-TTZcBsDti7XjwbeHAx0aPzYpein0cWQjkG6B-0QUxqwvXeDgF7ypPd50jlP-nee9JyHXh36eD_yJ0AZYHsg5VbY4fCw-39kfwEAbNSG</recordid><startdate>20231106</startdate><enddate>20231106</enddate><creator>Hu, Changmei</creator><creator>Fu, Xiao</creator><creator>Li, Shujun</creator><creator>Chen, Cong</creator><creator>Zhao, Xielan</creator><creator>Peng, Jie</creator><general>Springer International Publishing</general><general>BioMed Central Ltd</general><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>K9.</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20231106</creationdate><title>Chidamide inhibits cell glycolysis in acute myeloid leukemia by decreasing N6-methyladenosine-related GNAS-AS1</title><author>Hu, Changmei ; Fu, Xiao ; Li, Shujun ; Chen, Cong ; Zhao, Xielan ; Peng, Jie</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c573t-f0e6df80f6471f9845964ac16636620e8f0a0168c8b123613aa538edce07c34d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Adenosine - analogs & derivatives</topic><topic>Adenosine - pharmacology</topic><topic>Aminopyridines - pharmacology</topic><topic>Animals</topic><topic>Antineoplastic Agents - pharmacology</topic><topic>Apoptosis</topic><topic>Apoptosis - drug effects</topic><topic>Benzamides - pharmacology</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Cancer</topic><topic>Care and treatment</topic><topic>Cell Line, Tumor</topic><topic>Cell Survival - drug effects</topic><topic>Glucose metabolism</topic><topic>Glycolysis - drug effects</topic><topic>Humans</topic><topic>Kinases</topic><topic>Lactates</topic><topic>Leukemia</topic><topic>Leukemia, Myeloid, Acute - drug therapy</topic><topic>Leukemia, Myeloid, Acute - genetics</topic><topic>Leukemia, Myeloid, Acute - metabolism</topic><topic>Medicinal Chemistry</topic><topic>Methyltransferases</topic><topic>Mice</topic><topic>Mice, Inbred BALB C</topic><topic>Mice, Nude</topic><topic>MicroRNAs - genetics</topic><topic>Pharmaceutical Sciences/Technology</topic><topic>Pharmacology/Toxicology</topic><topic>Protein binding</topic><topic>Protein kinases</topic><topic>Proteins</topic><topic>Research Article</topic><topic>RNA</topic><topic>Xenograft Model Antitumor Assays</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hu, Changmei</creatorcontrib><creatorcontrib>Fu, Xiao</creatorcontrib><creatorcontrib>Li, Shujun</creatorcontrib><creatorcontrib>Chen, Cong</creatorcontrib><creatorcontrib>Zhao, Xielan</creatorcontrib><creatorcontrib>Peng, Jie</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Daru</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hu, Changmei</au><au>Fu, Xiao</au><au>Li, Shujun</au><au>Chen, Cong</au><au>Zhao, Xielan</au><au>Peng, Jie</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Chidamide inhibits cell glycolysis in acute myeloid leukemia by decreasing N6-methyladenosine-related GNAS-AS1</atitle><jtitle>Daru</jtitle><stitle>DARU J Pharm Sci</stitle><addtitle>Daru</addtitle><date>2023-11-06</date><risdate>2023</risdate><volume>32</volume><issue>1</issue><spage>11</spage><epage>24</epage><pages>11-24</pages><issn>2008-2231</issn><issn>1560-8115</issn><eissn>2008-2231</eissn><abstract>Background
Acute myeloid leukemia (AML) is a hematopoietic malignancy. Chidamide has shown anti-cancer effect in different malignancies. The function of Chidamide in glycolysis in AML cells remains unclear.
Methods
AML cells were treated with 1000 nM Chidamide for 48 h. The levels of long non-coding RNA-GNAS-AS1, miR-34a-5p, glycolysis-related proteins, and Ras homolog gene family (RhoA)/Rho-associated protein kinase (ROCK) signaling-related proteins were detected by qRT-PCR or western blot. Cell viability and apoptosis were measured by CCK-8 and flow cytometry. Glycolysis levels were measured by assay kits. GNAS-AS1 N6-methyladenosine (m6A) modification level was detected by methylated RNA immunoprecipitation sequencing. The combined targets of miR-34a-5p were validated using a dual-luciferase reporter assay. BALB/C nude mice were selected for subcutaneous tumor validation. Chidamide at a dosage of 25 mg/kg was used in the animal study.
Results
GNAS-AS1 promoted glycolysis in AML cells by upregulating the expression of glycolysis-related proteins and increasing glucose consumption, lactate production, ATP generation, and the extracellular acidification rate. Chidamide treatment suppressed WT1-associated protein (WTAP)-mediated RNA m6A modification of GNAS-AS1. Chidamide downregulated GNAS-AS1 to inhibit glycolysis in AML cells. GNAS-AS1 targeted miR-34a-5p to promote insulin-like growth factor 2 mRNA-binding protein (IGF2BP2) expression. IGF2BP2 inhibition reversed the promoting effect of miR-34a-5p knockdown on glycolysis and RhoA/ROCK pathway in Chidamide-treated cells. GNAS-AS1 overexpression abolished the inhibitory effect of Chidamide on AML tumorigenesis in vivo by modulating the RhoA/ROCK pathway.
Conclusion
Chidamide inhibited glycolysis in AML by repressing WTAP-mediated GNAS-AS1 m6A modification and then regulating the miR-34a-5p/IGF2BP2 axis.
Graphical abstract</abstract><cop>Cham</cop><pub>Springer International Publishing</pub><pmid>37926762</pmid><doi>10.1007/s40199-023-00482-y</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adenosine - analogs & derivatives Adenosine - pharmacology Aminopyridines - pharmacology Animals Antineoplastic Agents - pharmacology Apoptosis Apoptosis - drug effects Benzamides - pharmacology Biomedical and Life Sciences Biomedicine Cancer Care and treatment Cell Line, Tumor Cell Survival - drug effects Glucose metabolism Glycolysis - drug effects Humans Kinases Lactates Leukemia Leukemia, Myeloid, Acute - drug therapy Leukemia, Myeloid, Acute - genetics Leukemia, Myeloid, Acute - metabolism Medicinal Chemistry Methyltransferases Mice Mice, Inbred BALB C Mice, Nude MicroRNAs - genetics Pharmaceutical Sciences/Technology Pharmacology/Toxicology Protein binding Protein kinases Proteins Research Article RNA Xenograft Model Antitumor Assays |
| title | Chidamide inhibits cell glycolysis in acute myeloid leukemia by decreasing N6-methyladenosine-related GNAS-AS1 |
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