Dong Ken C相关文献与解析，生知库 | 链接生命科学的每一步

The deubiquitinase Rpn11 functions as an allosteric ubiquitin sensor to promote substrate engagement by the 26S proteasome

去泛素化酶Rpn11作为一种变构泛素传感器，促进26S蛋白酶体与底物结合。

期刊:Cell Reports

影响因子:6.9

doi:10.1016/j.celrep.2025.115736

Htet, Zaw Min; Dong, Ken C; Martin, Andreas

Identification of novel ubiquitin receptors on the 26S proteasome by photo-crosslinking mass spectrometry

利用光交联质谱法鉴定26S蛋白酶体上的新型泛素受体

期刊:

影响因子:

doi:10.64898/2025.12.19.695558

MacRae, Nicole S; Dong, Ken C; Harimoto, Hiromitsu; Martin, Andreas

信号转导

发表日期：2025

文献求助收藏

Structural landscape of AAA+ ATPase motor states in the substrate-degrading human 26S proteasome reveals conformation-specific binding of TXNL1

底物降解型人类26S蛋白酶体中AAA+ ATPase马达状态的结构图谱揭示了TXNL1的构象特异性结合

期刊:

影响因子:

doi:10.1101/2024.11.08.622731

Arkinson, Connor; Gee, Christine L; Zhang, Zeyuan; Dong, Ken C; Martin, Andreas

发表日期：2024

文献求助收藏

The Ufd1 cofactor determines the linkage specificity of polyubiquitin chain engagement by the AAA+ ATPase Cdc48

Ufd1 辅因子决定了 AAA+ ATPase Cdc48 与多聚泛素链结合的连接特异性

期刊:Molecular Cell

影响因子:16.6

doi:10.1016/j.molcel.2023.01.016

Williams, Cameron; Dong, Ken C; Arkinson, Connor; Martin, Andreas

发表日期：2023

文献求助收藏

The 26S Proteasome Utilizes a Kinetic Gateway to Prioritize Substrate Degradation.

26S蛋白酶体利用动力学通道来优先降解底物

期刊:Cell

影响因子:42.5

doi:10.1016/j.cell.2019.02.031

Bard Jared A M, Bashore Charlene, Dong Ken C, Martin Andreas

免疫/内分泌

发表日期：2019

文献求助收藏

The Cdc48 unfoldase prepares well-folded protein substrates for degradation by the 26S proteasome

Cdc48解折叠酶使折叠良好的蛋白质底物准备好被26S蛋白酶体降解。

期刊:Communications Biology

影响因子:5.1

doi:10.1038/s42003-019-0283-z

Olszewski, Michal M; Williams, Cameron; Dong, Ken C; Martin, Andreas

发表日期：2019

文献求助收藏

Structure and Function of the 26S Proteasome

26S蛋白酶体的结构和功能

期刊:Annual Review of Biochemistry

影响因子:20.5

doi:10.1146/annurev-biochem-062917-011931

Bard, Jared A M; Goodall, Ellen A; Greene, Eric R; Jonsson, Erik; Dong, Ken C; Martin, Andreas

发表日期：2018

文献求助收藏

Mechanisms and regulation of substrate degradation by the 26S proteasome

26S蛋白酶体底物降解的机制和调控

Structural landscape of the degrading 26S proteasome reveals conformation-specific binding of TXNL1

降解的 26S 蛋白酶体的结构图谱揭示了 TXNL1 的构象特异性结合

NUB1 traps unfolded FAT10 for ubiquitin-independent degradation by the 26S proteasome.

NUB1 捕获未折叠的 FAT10，使其通过 26S 蛋白酶体进行不依赖泛素的降解

The deubiquitinase Rpn11 functions as an allosteric ubiquitin sensor to promote substrate engagement by the 26S proteasome

去泛素化酶Rpn11作为一种变构泛素传感器，促进26S蛋白酶体与底物结合。

Identification of novel ubiquitin receptors on the 26S proteasome by photo-crosslinking mass spectrometry

利用光交联质谱法鉴定26S蛋白酶体上的新型泛素受体

Structural landscape of AAA+ ATPase motor states in the substrate-degrading human 26S proteasome reveals conformation-specific binding of TXNL1

底物降解型人类26S蛋白酶体中AAA+ ATPase马达状态的结构图谱揭示了TXNL1的构象特异性结合

The Ufd1 cofactor determines the linkage specificity of polyubiquitin chain engagement by the AAA+ ATPase Cdc48

Ufd1 辅因子决定了 AAA+ ATPase Cdc48 与多聚泛素链结合的连接特异性

The 26S Proteasome Utilizes a Kinetic Gateway to Prioritize Substrate Degradation.

26S蛋白酶体利用动力学通道来优先降解底物

The Cdc48 unfoldase prepares well-folded protein substrates for degradation by the 26S proteasome

Cdc48解折叠酶使折叠良好的蛋白质底物准备好被26S蛋白酶体降解。

Structure and Function of the 26S Proteasome

26S蛋白酶体的结构和功能