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Last update 08 May 2025

EE

Last update 08 May 2025

Basic Info

Synonyms

Introduction-

Drugs associated with EE

MTDX-401

Target

Mechanism

EE inhibitors

Active Org.

Montdorex Inc.

Originator Org.

Montdorex Inc.

Active Indication

Nonalcoholic Steatohepatitis

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

MTDX-203

Target

Mechanism

EE inhibitors

Active Org.

Montdorex Inc.

Originator Org.

Montdorex Inc.

Active Indication

Neoplasms

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

MTDX-402

Target

Mechanism

EE inhibitors

Active Org.

Montdorex Inc.

Originator Org.

Montdorex Inc.

Active Indication

Nonalcoholic Steatohepatitis

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with EE

100 Translational Medicine associated with EE

0 Patents (Medical) associated with EE

193

Literatures (Medical) associated with EE

01 Apr 2025·International Journal of Biological Macromolecules

β-Aminobutyric acid activates SA-signalling systemic acquired resistance in peach fruit by suppressing the circadian clock associated protein1

Article

Author: Wang, Kaituo ; Li, Meilin ; Xiang, Fei ; Zheng, Yonghua ; Li, Chunhong ; Zou, Yanyu ; Xia, Yijia ; Zhou, Minghua ; Cao, Shifeng

Circadian clock regulates plant development and physiology by anticipating daily environmental changes. Here we studied the core clock protein involved in β-aminobutyric acid (BABA)-inducible systemic acquired resistance (SAR) resistance to Rhizopus stolonifer in peach fruit. BABA elicitation barely primed the accumulation of jasmonate or ethylene, whose regulation was associated with morning-loop gene expression. Notably, BABA-induced resistance depended on the upregulation of salicylic acid (SA) signalling, accompanied by increased transcription of specific evening-loop genes. Through Y2H screening, pull-down and co-IP analyses, CIRCADIAN CLOCK ASSOCIATED 1 (CCA1), a morning-expressed clock protein repressed by BABA, was identified as an interacting partner of NPR1 in regulating SA-dependent SAR. A CUT&Tag analysis indicated that the association of CCA1 with its target genes, which are enriched in EE or CBS motifs, was involved in SA pathway. Furthermore, EMSA, DLR, Y3H and Co-ip assays suggested that CCA1 did not directly affect the expression of SA-inducible genes but instead hindered the interaction between NPR1 and TGA1. Overexpression of PpCCA1 attenuated the transcription of SA-responsive PR genes, while mutation of PpCCA1 elevated these expressions. Collectively, PpCCA1 functions as a negative regulator of NPR1-dependent SA signalling through antagonistic crosstalk with the NPR1-TGA1 system, but BABA activates SAR by suppressing PpCCA1 in peach fruit.

01 Feb 2025·Journal of Biological Chemistry

Acidic pH of early endosomes governs SARS-CoV-2 transport in host cells

Article

Author: Kondapalli, Kalyan C ; Duhaini, Mariam ; Srour, Ali ; Tripathy, Suvranta K ; Fares, Perla

Endocytosis is a prominent mechanism for SARS-CoV-2 entry into host cells. Upon internalization into early endosomes (EEs), the virus is transported to late endosomes (LEs), where acidic conditions facilitate spike protein processing and viral genome release. Dynein and kinesin motors drive EE transport along microtubules; dynein moves EEs to the perinuclear region, while kinesins direct them towards the plasma membrane, creating a tug-of-war over the direction of transport. Here, we identify that the luminal pH of EEs is a key factor regulating the outcome of this tug-of-war. Among the known endosomal pH regulators, only the sodium-proton exchanger NHE9 has so far been genetically linked to severe COVID-19 risk. NHE9 functions as a proton leak pathway specifically on endosomes. We show that limiting acidification of EEs by increasing the expression of NHE9 leads to decreased infectivity of the SARS-CoV-2 spike-bearing virus in host cells. Our investigation identified the EE membrane lipid phosphatidylinositol-3-phosphate (PI3P) as a link between luminal pH changes and EE transport. Normally, as EEs mature, PI3P depletes. However, in cells with high NHE9 expression, PI3P persists longer on EEs. PI3P plays a pivotal role in the recruitment of motor proteins and the subsequent movement of EEs. Consistently, we observed that NHE9-mediated alkalization of EEs hindered perinuclear movement. Specifically, EE speed and run length were negatively impacted, ultimately leading to EEs falling off microtubules and impairing the delivery of viral cargo to LEs. NHE9 thus offers a unique opportunity as a viable therapeutic target to impede SARS-CoV-2 host cell entry.

01 Feb 2025·Molecular Biology of the Cell

ZYG-12/Hook's dual role as a dynein adaptor for early endosomes and nuclei is regulated by alternative splicing of its cargo binding domain

Article

Author: Cheerambathur, Dhanya K. ; Chan, Fung-Yi ; Moreira, Matilde ; Koehnen, Carlota Boal ; Gassmann, Reto ; Teixeira, Vanessa ; Carvalho, Ana Xavier ; Barbosa, Daniel J. ; Rocha, Helder ; Green, Mattie ; Carvalho, Cátia

The microtubule motor cytoplasmic dynein-1 transports and positions various organelles, but the molecular basis of this functional diversity is not fully understood. Cargo adaptors of the Hook protein family recruit dynein to early endosomes (EE) in fungi and human cells by forming the FTS–Hook–FHIP (FHF) complex. By contrast, the Caenorhabditis elegans Hook homologue ZYG-12 recruits dynein to the nuclear envelope (NE) in the meiotic gonad and mitotic early embryo by forming a Linker of Nucleoskeleton and Cytoskeleton (LINC) complex. Here, we demonstrate that ZYG-12 recruits dynein to EE in epithelia. We identify and functionally characterize the homologues of FTS (UBC-19) and FHIP (FHIP-1) that constitute the C. elegans FHF complex, validate the predicted FHIP-1–RAB-5 binding interface in vivo, and show that ZYG-12 forms FHF via a conserved segment that precedes, and is distinct from, its C-terminal NE targeting domain. Finally, we show that C-terminal ZYG-12 splice isoforms differ in their ability to target to the NE and EE. We conclude that the C. elegans Hook adaptor evolved to recruit dynein to two distinct organelles, and that cargo specificity of ZYG-12 is regulated by alternative splicing.

News (Medical) associated with EE

07 Mar 2024

·www.businesswire.com

Montdorex Announces Acceptance of Its Abstract for Presentation at the AACR Annual Meeting 2024

MONTREAL--( BUSINESS WIRE )--Montdorex Inc. (“Montdorex” or “the Company”), a privately-owned precision medicine company, today announced that Terry Chow, Ph.D., Founder and CEO will present insights on the relevance of inhibiting the endo-exonuclease (EE) enzyme in a poster presentation at the American Association for Cancer Research (AACR) Annual Meeting, to be held in San Diego, CA, April 5-10, 2024. The endo-exonuclease enzyme plays a key role in DNA damage repair mechanisms, but it is also overexpressed in cancer tumors. In a proof-of-concept study, Montdorex showed that tumors with increased EE expression showed the best response to pentamidine, an endo-exonuclease inhibitor. The Company has also identified mono- and di-amidine analogs of pentamidine that are more effective than the parent drug in both in vitro and in vivo studies. “Our lead candidate, MTDX203, showed an increased anti-cancer activity with a higher safety index than pentamidine in preclinical animal studies,” said Terry Chow of Montdorex. “I look forward to presenting our detailed findings to the AACR scientific and investor community at the upcoming annual meeting.” Details of the AACR poster presentation are as follows: Poster Presentation (#5604): Modulating DNA repair through endo-exonuclease inhibition: a new therapeutic paradigm in Oncology [ link to the abstract ] Session Category: Molecular/Cellular Biology and Genetics Session Title: DNA Damage and Repair 2 Session Date and Time: Tuesday, April 9, 2024 1:30 PM – 5:00 PM (PT) Location: Poster Section 14, Poster Board Number 2 About Montdorex Based in Montreal, Canada, Montdorex Inc. is a privately-owned, early-stage precision medicine company, targeting the endo-exonuclease (EE) enzyme involved in cancer tumor growth and inflammatory processes. The company is developing proprietary mono-amidine and di-amidine EE inhibitors to modulate DNA repair in oncology and non cytotoxic di-amidine analogs for anti-inflammatory applications, such as gastrointestinal conditions and liver diseases. For more information, please visit montdorex.com .

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