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Deubiquitinases: From mechanisms to their inhibition by small molecules
Deubiquitinases (DUBs) are specialized proteases that remove ubiquitin from substrates or
cleave within ubiquitin chains to regulate ubiquitylation and therefore play important roles in …
cleave within ubiquitin chains to regulate ubiquitylation and therefore play important roles in …
Deubiquitinating enzymes (DUBs): Regulation, homeostasis, and oxidative stress response
NA Snyder, GM Silva - Journal of Biological Chemistry, 2021 - jbc.org
Ubiquitin signaling is a conserved, widespread, and dynamic process in which protein
substrates are rapidly modified by ubiquitin to impact protein activity, localization, or stability …
substrates are rapidly modified by ubiquitin to impact protein activity, localization, or stability …
Nsp3 of coronaviruses: Structures and functions of a large multi-domain protein
J Lei, Y Kusov, R Hilgenfeld - Antiviral research, 2018 - Elsevier
The multi-domain non-structural protein 3 (Nsp3) is the largest protein encoded by the
coronavirus (CoV) genome, with an average molecular mass of about 200 kD. Nsp3 is an …
coronavirus (CoV) genome, with an average molecular mass of about 200 kD. Nsp3 is an …
Deubiquitylating enzymes and drug discovery: emerging opportunities
JA Harrigan, X Jacq, NM Martin… - Nature reviews Drug …, 2018 - nature.com
More than a decade after a Nobel Prize was awarded for the discovery of the ubiquitin–
proteasome system and clinical approval of proteasome and ubiquitin E3 ligase inhibitors …
proteasome system and clinical approval of proteasome and ubiquitin E3 ligase inhibitors …
Mechanisms of deubiquitinase specificity and regulation
Protein ubiquitination is one of the most powerful posttranslational modifications of proteins,
as it regulates a plethora of cellular processes in distinct manners. Simple …
as it regulates a plethora of cellular processes in distinct manners. Simple …
Molecular basis of USP7 inhibition by selective small-molecule inhibitors
AP Turnbull, S Ioannidis, WW Krajewski… - Nature, 2017 - nature.com
Ubiquitination controls the stability of most cellular proteins, and its deregulation contributes
to human diseases including cancer. Deubiquitinases remove ubiquitin from proteins, and …
to human diseases including cancer. Deubiquitinases remove ubiquitin from proteins, and …
USP14-regulated allostery of the human proteasome by time-resolved cryo-EM
S Zhang, S Zou, D Yin, L Zhao, D Finley, Z Wu, Y Mao - Nature, 2022 - nature.com
Proteasomal degradation of ubiquitylated proteins is tightly regulated at multiple levels,–. A
primary regulatory checkpoint is the removal of ubiquitin chains from substrates by the …
primary regulatory checkpoint is the removal of ubiquitin chains from substrates by the …
High-throughput screening identifies established drugs as SARS-CoV-2 PLpro inhibitors
A new coronavirus (SARS-CoV-2) has been identified as the etiologic agent for the COVID-
19 outbreak. Currently, effective treatment options remain very limited for this disease; …
19 outbreak. Currently, effective treatment options remain very limited for this disease; …
Targeting ubiquitin specific proteases (USPs) in cancer immunotherapy: from basic research to preclinical application
H Gao, J Yin, C Ji, X Yu, J Xue, X Guan… - Journal of Experimental …, 2023 - Springer
Tumors have evolved in various mechanisms to evade the immune system, hindering the
antitumor immune response and facilitating tumor progression. Immunotherapy has become …
antitumor immune response and facilitating tumor progression. Immunotherapy has become …
Assessing the performance of the MM/PBSA and MM/GBSA methods. 6. Capability to predict protein–protein binding free energies and re-rank binding poses …
Understanding protein–protein interactions (PPIs) is quite important to elucidate crucial
biological processes and even design compounds that interfere with PPIs with …
biological processes and even design compounds that interfere with PPIs with …