Results 41 to 50 of about 54,326 (298)

RanBP2-Mediated SUMOylation Promotes Human DNA Polymerase Lambda Nuclear Localization and DNA Repair [PDF]

open access: yes, 2020
Cellular DNA is under constant attack by a wide variety of agents, both endogenous and exogenous. To counteract DNA damage, human cells have a large collection of DNA repair factors. Among them, DNA polymerase lambda (Polλ) stands out for its versatility,
Cortés Ledesma, Felipe   +4 more
core   +1 more source

SUMO protein modification

open access: yesBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2004
SUMO (small ubiquitin-related modifier) family proteins are not only structurally but also mechanistically related to ubiquitin in that they are posttranslationally attached to other proteins. As ubiquitin, SUMO is covalently linked to its substrates via amide (isopeptide) bonds formed between its C-terminal glycine residue and the epsilon-amino group ...
openaire   +2 more sources

SUMOylation regulates LKB1 localization and its oncogenic activity in liver cancer [PDF]

open access: yes, 2019
BACKGROUND: Even though liver kinase B1 (LKB1) is usually described as a tumor suppressor in a wide variety of tissues, it has been shown that LKB1 aberrant expression is associated with bad prognosis in Hepatocellular Carcinoma (HCC).
Díaz Moreno, Irene   +4 more
core   +1 more source

USE OF SUMO-EXPRESSION SYSTEM AND SUMO-PROTEASE FOR PRODUCTION OF ACTIVE INTERFERON α-2b [PDF]

open access: yesBiotechnologia Acta
Recombinant proteins production in prokaryotic expression systems is often complicated by need of native, N-terminal formylmethionine free molecule extraction, refolding, and processing.
I-M.M. KLYMKOVYCH, M.M. SKRYNNYK
doaj   +1 more source

Functional reconstitution of a tunable E3-dependent sumoylation pathway in Escherichia coli. [PDF]

open access: yesPLoS ONE, 2012
SUMO (small ubiquitin-related modifier) is a reversible post-translational protein modifier that alters the localization, activity, or stability of proteins to which it is attached.
Sean P O'Brien, Matthew P DeLisa
doaj   +1 more source

An influenza virus-triggered SUMO switch orchestrates co-opted endogenous retroviruses to stimulate host antiviral immunity [PDF]

open access: yes, 2019
Dynamic small ubiquitin-like modifier (SUMO) linkages to diverse cellular protein groups are critical to orchestrate resolution of stresses such as genome damage, hypoxia, or proteotoxicity.
Domingues, Patricia   +6 more
core   +4 more sources

SUMO: of branched proteins and nuclear bodies [PDF]

open access: yesOncogene, 2001
SUMO belongs to a growing number of ubiquitin-like proteins that covalently modify their target proteins. Although some evidence supports a role of SUMO modification in regulating protein stability, most studied examples support a model by which SUMO alters the interaction properties of its targets, often affecting their subcellular localization ...
Seeler, Jacob-Sebastian, Dejean, Anne
openaire   +2 more sources

A Photo-Crosslinking Approach to Identify Class II SUMO-1 Binders

open access: yesFrontiers in Chemistry, 2022
The small ubiquitin-like modifier (SUMO) is involved in various cellular processes and mediates known non-covalent protein-protein interactions by three distinct binding surfaces, whose interactions are termed class I to class III.
Kira Brüninghoff   +4 more
doaj   +1 more source

The role of Schizosaccharomyces pombe SUMO ligases in genome stability [PDF]

open access: yes, 2007
SUMOylation is a post-translational modification that affects a large number of proteins, many of which are nuclear. While the role of SUMOylation is beginning to be elucidated, it is clear that understanding the mechanisms that regulate the process is ...
A. Skilton   +44 more
core   +2 more sources

SUMOylation inhibits FOXM1 activity and delays mitotic transition [PDF]

open access: yes, 2014
The forkhead box transcription factor FOXM1 is an essential effector of G2/M-phase transition, mitosis and the DNA damage response. As such, it is frequently deregulated during tumorigenesis. Here we report that FOXM1 is dynamically modified by SUMO1 but
Brosens, Jan J.   +13 more
core   +1 more source

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