Results 31 to 40 of about 28,234 (247)

Protein partners of deubiquitinating enzymes [PDF]

open access: yesBiochemical Journal, 2008
Protein modification by ubiquitin and ubiquitin-like molecules is a critical regulatory process. Like most regulated protein modifications, ubiquitination is reversible. Deubiquitination, the reversal of ubiquitination, is quickly being recognized as an important regulatory strategy.
Karen H, Ventii, Keith D, Wilkinson
openaire   +2 more sources

Endocytosis: Why not wait to deubiquitinate? [PDF]

open access: yesCurrent Biology, 2000
Deubiquitination by the Fat facets protein - a regulator of photoreceptor differentiation during Drosophila eye development - has been found to activate endocytosis, while ubiquitination inhibits endocytosis. Surprisingly, this is the opposite effect that ubiquitination has on endocytosis of many plasma membrane proteins.
Carthew, Richard W., Xu, Chunyan
openaire   +2 more sources

DNA requirement in FANCD2 deubiquitination by USP1-UAF1-RAD51AP1 in the Fanconi anemia DNA damage response

open access: yesNature Communications, 2019
In the Fanconi anemia pathway, deubiquitination of FANCD2 is a fundamental regulatory step. Here, the authors have developed a set of biochemical tools to reconstitute FANCD2 deubiquitination by recombinant USP1-UAF1-RAD51AP1 and reveal critical ...
Fengshan Liang   +9 more
doaj   +1 more source

Deubiquitinating Enzymes and Bone Remodeling [PDF]

open access: yesStem Cells International, 2018
Bone remodeling, which is essential for bone homeostasis, is controlled by multiple factors and mechanisms. In the past few years, studies have emphasized the role of the ubiquitin-dependent proteolysis system in regulating bone remodeling. Deubiquitinases, which are grouped into five families, remove ubiquitin from target proteins and are involved in ...
Yu-chen Guo, Shi-wen Zhang, Quan Yuan
openaire   +3 more sources

USP7: Novel Drug Target in Cancer Therapy

open access: yesFrontiers in Pharmacology, 2019
Ubiquitin specific protease 7 (USP7) is one of the deubiquitinating enzymes (DUB) that erases ubiquitin and protects substrate protein from degradation.
Zhiru Wang   +15 more
doaj   +1 more source

The roles of protein ubiquitination in tumorigenesis and targeted drug discovery in lung cancer

open access: yesFrontiers in Endocrinology, 2023
The malignant lung cancer has a high morbidity rate and very poor 5-year survival rate. About 80% - 90% of protein degradation in human cells is occurred through the ubiquitination enzyme pathway.
Zhen Ye   +4 more
doaj   +1 more source

Deciphering histone 2A deubiquitination [PDF]

open access: yesGenome Biology, 2008
Three recent papers have identified distinct enzymes that can remove ubiquitin from mammalian histone 2A (H2A). Functions in transcriptional activation, DNA repair and control of the cell cycle have been proposed for these enzymes.
Michael J, Clague   +2 more
openaire   +2 more sources

A plague of deubiquitination [PDF]

open access: yesThe Journal of Experimental Medicine, 2005
Plague bacteria inject infected host cells with a ubiquitin-chopping enzyme, according to Zhou and colleagues in a study on [page 1327][1]. The group shows that the virulence factor YopJ operates as a deubiquitinase to shut down multiple signaling pathways that would otherwise help trigger ...
openaire   +1 more source

Epigenetics disruptions enabled by porphyrin-derived metal-organic frameworks disarm resistances to sonocatalytic ROS anti-tumor actions

open access: yesFundamental Research
Post-transcriptional epigenetic modifications provide numerous implications for tumor progression, metastasis and recurrence, which also pose resistances to reactive oxygen species (ROS)-based anti-tumor.
Yan Zhang   +12 more
doaj   +1 more source

Components of the ubiquitin-proteasome pathway compete for surfaces on Rad23 family proteins [PDF]

open access: yes
Background: The delivery of ubiquitinated proteins to the proteasome for degradation is a key step in the regulation of the ubiquitin-proteasome pathway, yet the mechanisms underlying this step are not understood in detail.
Deshaies, Raymond J.   +6 more
core   +1 more source

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