Results 101 to 110 of about 83,359 (255)

Protein neddylation in lung tumorigenesis: Target validation and targeted therapy

open access: yesFundamental Research
Much akin to ubiquitylation, neddylation is catalyzed by a cascade of three enzymes: E1 NEDD8-activating enzyme, E2 NEDD8-conjugating enzyme (UBE2M or UBE2F), and E3 NEDD8 ligases.
Yawen Zheng   +3 more
doaj   +1 more source

Table_1_How to Inactivate Human Ubiquitin E3 Ligases by Mutation.DOCX

open access: yes, 2020
E3 ubiquitin ligases are the ultimate enzymes involved in the transfer of ubiquitin to substrate proteins, a process that determines the fate of the modified protein.
Ugo Mayor (404331)   +3 more
core   +1 more source

Exploring the biological and chemical complexity of the ligases. [PDF]

open access: yes, 2014
Using a novel method to map and cluster chemical reactions, we have re-examined the chemistry of the ligases [Enzyme Commission (EC) Class 6] and their associated protein families in detail.
Thornton, Janet M   +3 more
core   +1 more source

Structural and biochemical insights into the thermostable esterase Ta0887 from Thermoplasma acidophilum

open access: yesFEBS Open Bio, EarlyView.
In this study, a novel esterase from the thermoacidophilic archaeon Thermoplasma acidophilum was biochemically and structurally characterized. Our results demonstrate that Ta0887 is a highly thermostable esterase that preferentially hydrolyzes p‐nitrophenyl hexanoate and possesses an α‐helical cap domain that likely contributes to its substrate ...
Alejandro Delgado‐Rey   +4 more
wiley   +1 more source

Threonine 348 regulates the subcellular localization of PTEN

open access: yesFEBS Open Bio, EarlyView.
Thr348 in the C2 domain is a key contributor to PTEN subcellular localization. The PTEN350 fragment and PTENA4 accumulated in the nucleus, whereas PTENK13R,A4 predominantly localized to the plasma membrane. In contrast, substitution of Thr348 with Asp (T348D) disrupted these characteristic localization patterns, resulting in predominant cytoplasmic ...
Takashi Kato, Suzu Tanaka, Miyu Ohashi
wiley   +1 more source

Role of E3 ligases on skeletal muscle plasticity.

open access: yes, 2012
Neste estudo analisamos o envolvimento de E3 ligases sob três aspectos da plasticidade muscular esquelética: a perda de massa decorrente do desuso, a manutenção de fibras tipo I e II e a regeneração do tecido muscular.
Igor Luchini Baptista   +1 more
core   +1 more source

A minimal cellulosome‐like system in Cellulosilyticum lentocellum

open access: yesFEBS Open Bio, EarlyView.
Cellulose‐degrading bacteria typically use cellulosomes, large multi‐enzyme complexes on a scaffold protein. In Cellulosilyticum lentocellum, we characterise a far smaller arrangement, a single scaffold bound to one cellulase through a single cohesin‐dockerin interaction.
John Allan   +2 more
wiley   +1 more source

The ubiquitin symphony: E3 ligases as key conductors in the orchestra of growth and stress responses in fruits and vegetables

open access: yesHorticultural Plant Journal
Fruits and vegetables undergo various regulatory mechanisms during growth, development, postharvest process and stress responses, all of which are crucial to their quality.
Durray Shahwar   +5 more
doaj   +1 more source

E3 ubiquitin ligases: key regulators of hormone signaling in plants [PDF]

open access: yes, 2018
Ubiquitin-mediated control of protein stability is central to most aspects of plant hormone signaling. Attachment of ubiquitin to target proteins occurs via an enzymatic cascade with the final step being catalyzed by a family of enzymes known as E3 ...
Kelley, Dior
core  

The C‐terminal domain of yeast Arginyltransferase1 is essential for its catalytic activity

open access: yesFEBS Open Bio, EarlyView.
Arginyltransferase 1 (Ate1), a eukaryotic enzyme, catalyses arginylation, transferring arginine from tRNA‐Arg to the amino terminus of the target protein. Overexpression of Ate1 in yeast is lethal and is dependent on arginylation. This study elucidates how mutations in the cofactor‐binding and active site of Ate1 and truncation of its structural ...
Vikas Kumar Yadav   +4 more
wiley   +1 more source

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