Results 101 to 110 of about 81,380 (309)

The ubiquitin E3/E4 ligase, UBE4A, fine-tunes protein ubiquitylation and accumulation at sites of DNA damage facilitating double-strand break repair [PDF]

open access: yes, 2018
Double-strand breaks (DSBs) are critical DNA lesions that robustly activate the elaborate DNA damage response (DDR) network. We identified a critical player in DDR fine-tuning - the E3/E4 ubiquitin ligase, UBE4A.
Baranes Bachar, Keren   +4 more
core   +1 more source

Endocytic Control of Cell‐Autonomous and Non‐Cell‐Autonomous Functions of p53

open access: yesAdvanced Science, EarlyView.
NUMB Ex3‐containing isoforms localize to the plasma membrane, where they recruit p53 through SNX9 and direct it to multivesicular bodies and exosomes. Exported p53 is taken up by neighboring cells and activates nuclear programs, revealing an intercellular, exosome‐based pathway that might help establish a tumor‐suppressive microenvironment.
Roberta Cacciatore   +20 more
wiley   +1 more source

Role of the ubiquitin-selective CDC-48/UFD-1/NPL-4 chaperone in DNA replication [PDF]

open access: yes, 2012
Faithful transmission of genomic information requires tight spatiotemporal regulation of DNA replication factors. Posttranslational modifications, such as ubiquitylation, constitute a fast and effective mechanism to control such complex protein function.
Franz, André
core  

DCAF13 Safeguards Hematopoietic Stem Cells via RRS1‐Regulated Ribosome Biogenesis

open access: yesAdvanced Science, EarlyView.
This study establishes DCAF13 as an essential regulator for hematopoietic stem cell (HSC) function. Its deletion in mice causes lethal pancytopenia and HSC depletion. Mechanistically, DCAF13 interacts with RRS1 and mediates its non‐degradative K27‐linked ubiquitination, thereby stabilizing RRS1 to maintain ribosome biogenesis and protein translation ...
Mengke Li   +25 more
wiley   +1 more source

The role of HECT-type E3 ubiquitin ligases in inflammation

open access: yesFrontiers in Immunology
Homologous to the E6-AP Carboxyl Terminus (HECT)-type E3 ubiquitin ligases are key components of the ubiquitin-proteasome system (UPS) and play an important role in the regulation of inflammatory responses. Inflammation serves as a core defense mechanism
Ziyi Wang   +6 more
doaj   +1 more source

Decoys provide a scalable platform for the identification of plant E3 ubiquitin ligases that regulate circadian function

open access: yeseLife, 2019
The circadian clock relies on regulated degradation of clock proteins to maintain rhythmicity. Despite this, we know few components that mediate protein degradation.
Ann Feke   +6 more
doaj   +1 more source

A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Mat a2 repressor degradation [PDF]

open access: yes, 2001
Substrate discrimination in the ubiquitin–proteasome system is believed to be dictated by specific combinations of ubiquitin–protein ligases (E3s) and ubiquitin-conjugating enzymes (E2s).
Swanson, Rob
core   +2 more sources

Casitas B-lineage lymphoma linker helix mutations found in myeloproliferative neoplasms affect conformation [PDF]

open access: yes, 2016
Background: Casitas B-lineage lymphoma (Cbl or c-Cbl) is a RING ubiquitin ligase that negatively regulates protein tyrosine kinase (PTK) signalling. Phosphorylation of a conserved residue (Tyr371) on the linker helix region (LHR) between the substrate ...
Ahmed, Syed Feroj   +7 more
core   +2 more sources

Targeting Lactate and Lactylation in Cancer Metabolism and Immunotherapy

open access: yesAdvanced Science, EarlyView.
Lactate, once deemed a metabolic waste, emerges as a central regulator of cancer progression. This review elucidates how lactate and its epigenetic derivative, protein lactylation, orchestrate tumor metabolism, immune suppression, and therapeutic resistance.
Jiajing Gong   +5 more
wiley   +1 more source

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