General Information of the Drug (ID: M6APDG03443)
Name
Geldanamycin-estradiol hybrid
Status
Investigative
TTD Drug ID
D0H6OS
Target Gene(s) and Their Upstream m6A Regulator, Together with the Effect of Target Gene(s) in Drug Response
The target genes involved in drug-target interaction (such as drug-metabolizing enzymes, drug transporters and therapeutic targets) and drug-mediated cell death signaling (including modulating DNA damage and repair capacity, escaping from drug-induced apoptosis, autophagy, cellular metabolic reprogramming, oncogenic bypass signaling, cell microenvironment, cell stemness, etc.) could be regulated by m6A regulator(s) and affected their corresponding drug response. You can browse detailed information on drug-related target gene(s) mediated by m6A regulators.
Erbb2 tyrosine kinase receptor (HER2)
Fat mass and obesity-associated protein (FTO)
In total 1 mechanisms lead to this potential drug response
Response Summary Erbb2 tyrosine kinase receptor (HER2) is a therapeutic target for Geldanamycin-estradiol hybrid. The Fat mass and obesity-associated protein (FTO) has potential in affecting the response of Geldanamycin-estradiol hybrid through regulating the expression of Erbb2 tyrosine kinase receptor (HER2). [1], [2]
Insulin-like growth factor 2 mRNA-binding protein 2 (IGF2BP2)
In total 1 mechanisms lead to this potential drug response
Response Summary Erbb2 tyrosine kinase receptor (HER2) is a therapeutic target for Geldanamycin-estradiol hybrid. The Insulin-like growth factor 2 mRNA-binding protein 2 (IGF2BP2) has potential in affecting the response of Geldanamycin-estradiol hybrid through regulating the expression of Erbb2 tyrosine kinase receptor (HER2). [2], [3]
Heat shock protein 90 alpha (HSP90A)
Fat mass and obesity-associated protein (FTO)
In total 1 mechanisms lead to this potential drug response
Response Summary Heat shock protein 90 alpha (HSP90A) is a therapeutic target for Geldanamycin-estradiol hybrid. The Fat mass and obesity-associated protein (FTO) has potential in affecting the response of Geldanamycin-estradiol hybrid through regulating the expression of Heat shock protein 90 alpha (HSP90A). [4], [5]
Methyltransferase-like 3 (METTL3)
In total 1 mechanisms lead to this potential drug response
Response Summary Heat shock protein 90 alpha (HSP90A) is a therapeutic target for Geldanamycin-estradiol hybrid. The Methyltransferase-like 3 (METTL3) has potential in affecting the response of Geldanamycin-estradiol hybrid through regulating the expression of Heat shock protein 90 alpha (HSP90A). [4], [5]
YTH domain-containing family protein 2 (YTHDF2)
In total 1 mechanisms lead to this potential drug response
Response Summary Heat shock protein 90 alpha (HSP90A) is a therapeutic target for Geldanamycin-estradiol hybrid. The YTH domain-containing family protein 2 (YTHDF2) has potential in affecting the response of Geldanamycin-estradiol hybrid through regulating the expression of Heat shock protein 90 alpha (HSP90A). [5], [6]
References
Ref 1 FTO mediated ERBB2 demethylation promotes tumor progression in esophageal squamous cell carcinoma cells. Clin Exp Metastasis. 2022 Aug;39(4):623-639. doi: 10.1007/s10585-022-10169-4. Epub 2022 May 7.
Ref 2 Tyrosine kinase inhibitors. 15. 4-(Phenylamino)quinazoline and 4-(phenylamino)pyrido[d]pyrimidine acrylamides as irreversible inhibitors of the ATP binding site of the epidermal growth factor receptor. J Med Chem. 1999 May 20;42(10):1803-15. doi: 10.1021/jm9806603.
Ref 3 IGF2BP2 promotes the progression of colorectal cancer through a YAP-dependent mechanism. Cancer Sci. 2021 Oct;112(10):4087-4099. doi: 10.1111/cas.15083. Epub 2021 Aug 3.
Ref 4 m6A RNA Methylation Controls Proliferation of Human Glioma Cells by Influencing Cell Apoptosis. Cytogenet Genome Res. 2019;159(3):119-125. doi: 10.1159/000499062. Epub 2019 Oct 23.
Ref 5 Heat shock protein 90: inhibitors in clinical trials. J Med Chem. 2010 Jan 14;53(1):3-17. doi: 10.1021/jm9004708.
Ref 6 Modification of N6-methyladenosine RNA methylation on heat shock protein expression. PLoS One. 2018 Jun 14;13(6):e0198604. doi: 10.1371/journal.pone.0198604. eCollection 2018.