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MAHONE AT ASSOCIATES

KARNACK-USA

Company Name:
Corporate Name:
MAHONE AT ASSOCIATES
Company Title:  
Company Description:  
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Company Address: Rt. 1 Box 799 / 185 Baldwin Rd,KARNACK,TX,USA 
ZIP Code:
Postal Code:
75661 
Telephone Number: 9036793782 (+1-903-679-3782) 
Fax Number:  
Website:
cuatmymall. com 
Email:
 
USA SIC Code(Standard Industrial Classification Code):
8999 
USA SIC Description:
Services NEC 
Number of Employees:
 
Sales Amount:
 
Credit History:
Credit Report:
 
Contact Person:
 
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Company News:
  • Gasdermin D permeabilization of mitochondrial inner and outer membranes . . .
    Here, we show that the N-terminal pore-forming GSDMD fragment (GSDMD-NT) rapidly damaged both inner and outer mitochondrial membranes (OMMs) leading to reduced mitochondrial numbers, mitophagy, ROS, loss of transmembrane potential, attenuated oxidative phosphorylation (OXPHOS), and release of mitochondrial proteins and DNA from the matrix and
  • Issue: Immunity - Cell Press
    Miao, Jiang, Chang et al provide insight into the events connecting GSDMD cleavage and pyroptosis, revealing a critical role for mitochondrial damage in this form of cell death Mechanistically, the N-terminal GSDMD fragment (GSDMD-NT; brown sticks) rapidly forms pores in the mitochondrial inner and outer membranes in a manner dependent on the
  • Gasdermin D 触发心磷脂驱动的线粒体损伤和细胞焦亡,Trends . . .
    研究表明,gasdermin D N 末端 (GSDMD-NT) 通过在线粒体内外膜 (OMM) 上形成孔,从而在细胞焦亡中引发线粒体损伤。 作者强调了线粒体心磷脂在 GSDMD-NT 作用中的关键作用,并显着增进了我们对这种炎症细胞死亡机制的理解。
  • Immunity封面文章揭示焦亡细胞线粒体损伤新机制 - 腾讯网
    该研究揭示了一种新型由Gasdermin成孔蛋白介导的线粒体细胞死亡通路,为病原体感染及肿瘤等相关疾病的预防 治疗提供了新的思路与靶点。 封面图来源:123RF 参考资料: [1] 研究揭示焦亡细胞线粒体损伤新机制 Retrieved- November 16, 2023 from http: www cas ac cn syky 202311 t20231116_4985901 shtml 原始论文: [1] Miao et al , Gasdermin D permeabilization of mitochondrial inner and outer membranes accelerates and enhances pyroptosis Immunity (2023)
  • GSDMD-mediated mitochondrial dysfunction in marginal cells: A . . . - PNAS
    Herein, we demonstrated that pyroptosis—a recently identified inflammatory type of regulated cell death dependent on gasdermin D (GSDMD)—was activated in the cochleae of cisplatin-treated mice, causing CIHL Meanwhile, treatment with the GSDMD inhibitor necrosulfonamide alleviated CIHL in these mice
  • Gasdermin D对线粒体内膜和外膜的渗透作用可加速和加强焦 . . .
    研究人员发现N端的成孔Gasdermin D(GSDMD)片段(GSDMD-NT)会迅速损伤线粒体内膜和外膜(OMM),导致线粒体数量减少、线粒体自噬、ROS、跨膜电位丧失、氧化磷酸化(OXPHOS)减弱以及线粒体蛋白和DNA从基质和膜间隙中释放出来。
  • Gasdermin D permeabilization of mitochondrial inner and outer membranes . . .
    Here, we show that the N-terminal pore-forming GSDMD fragment (GSDMD-NT) rapidly damaged both inner and outer mitochondrial membranes (OMMs) leading to reduced mitochondrial numbers, mitophagy, ROS, loss of transmembrane potential, attenuated oxidative phosphorylation (OXPHOS), and release of mitochondrial proteins and DNA from the matrix and in
  • Gasdermin D triggers cardiolipin-driven mitochondrial damage and . . .
    In a remarkable recent study, Miao et al reveal that gasdermin D N-terminal (GSDMD-NT) instigates mitochondrial damage in pyroptosis by forming pores in inner and outer mitochondrial membranes (OMMs) The authors highlight the key role of mitochondrial cardiolipin in the action of GSDMD-NT, and sig …
  • Gasdermin D permeabilization of mitochondrial inner and outer membranes . . .
    Here, we show that the N-terminal pore-forming GSDMD fragment (GSDMD-NT) rapidly damaged both inner and outer mitochondrial membranes (OMMs) leading to reduced mitochondrial numbers, mitophagy, ROS, loss of transmembrane potential, attenuated oxidative phosphorylation (OXPHOS), and release of mitochondrial proteins and DNA from the matrix and in
  • Gasdermin D permeabilization of mitochondrial inner and outer membranes . . .
    Here, we show that the N-terminal pore-forming GSDMD fragment (GSDMD-NT) rapidly damaged both inner and outer mitochondrial membranes leading to reduced mitochondrial numbers, mitophagy, ROS, loss of transmembrane potential, attenuated oxidative phosphorylation and release of mitochondrial proteins and DNA from the matrix and intermembrane space




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