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On the Reactivation of the Pre-Existing Normal Fault 被引量:1
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作者 Shuping chen zongpeng chen 《World Journal of Mechanics》 2018年第5期210-217,共8页
The reactivation of pre-existing faults is a common phenomenon in a basin. This paper discusses the relationship between the pre-existing faults and the newly formed Coulomb shear fractures regarding pore fluid pressu... The reactivation of pre-existing faults is a common phenomenon in a basin. This paper discusses the relationship between the pre-existing faults and the newly formed Coulomb shear fractures regarding pore fluid pressures. Based on the Coulomb fracture criterion and Byerlee frictional sliding criterion, an equation relating pore pressure coefficient (&lambda;e), minimum dip angle (αe) of the reactive pre-existing fault and the intersection point depth (z) between the pre-existing fault and a newly formed Coulomb shear fault in an extensional basin, is established in this paper. This equation enhanced the understanding on the reactivation of pre-existing faults and can be used to calculate paleo-pore fluid pressures. The bigger the pore fluid pressure in a pre-existing fault is, the less the minimum dip angle for a reactive pre-existing fault will be. The minimum dip angle is less in shallow area than that in deep area. This will be of significance in petroleum exploration and development. 展开更多
关键词 COULOMB CRITERION Frictional SLIDING CRITERION Pre-Existing FAULT PORE Fluid Pressure REACTIVATION
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A Cullin 5-based complex serves as an essential modulator of ORF9b stability in SARS-CoV-2 replication
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作者 Yuzheng Zhou zongpeng chen +22 位作者 Sijie Liu Sixu Liu Yujie Liao Ashuai Du Zijun Dong Yongxing Zhang Xuan chen Siyi Tao Xin Wu Aroona Razzaq Gang Xu De-an Tan Shanni Li Youwen Deng Jian Peng Shuyan Dai Xu Deng Xianwen Zhang Taijiao Jiang Zheng Zhang Gong cheng Jincun Zhao Zanxian Xia 《Signal Transduction and Targeted Therapy》 SCIE CSCD 2024年第7期3112-3129,共18页
The ORF9b protein,derived from the nucleocapsid’s open-reading frame in both SARS-CoV and SARS-CoV-2,serves as an accessory protein crucial for viral immune evasion by inhibiting the innate immune response.Despite it... The ORF9b protein,derived from the nucleocapsid’s open-reading frame in both SARS-CoV and SARS-CoV-2,serves as an accessory protein crucial for viral immune evasion by inhibiting the innate immune response.Despite its significance,the precise regulatory mechanisms underlying its function remain elusive.In the present study,we unveil that the ORF9b protein of SARS-CoV-2,including emerging mutant strains like Delta and Omicron,can undergo ubiquitination at the K67 site and subsequent degradation via the proteasome pathway,despite certain mutations present among these strains.Moreover,our investigation further uncovers the pivotal role of the translocase of the outer mitochondrial membrane 70(TOM70)as a substrate receptor,bridging ORF9b with heat shock protein 90 alpha(HSP90α)and Cullin 5(CUL5)to form a complex.Within this complex,CUL5 triggers the ubiquitination and degradation of ORF9b,acting as a host antiviral factor,while HSP90αfunctions to stabilize it.Notably,treatment with HSP90 inhibitors such as GA or 17-AAG accelerates the degradation of ORF9b,leading to a pronounced inhibition of SARS-CoV-2 replication.Single-cell sequencing data revealed an up-regulation of HSP90αin lung epithelial cells from COVID-19 patients,suggesting a potential mechanism by which SARS-CoV-2 may exploit HSP90αto evade the host immunity.Our study identifies the CUL5-TOM70-HSP90αcomplex as a critical regulator of ORF9b protein stability,shedding light on the intricate host–virus immune response dynamics and offering promising avenues for drug development against SARS-CoV-2 in clinical settings. 展开更多
关键词 STABILITY MODULATOR offering
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