Results 191 to 200 of about 13,776 (215)

An Acetylation Switch Regulates SUMO-Dependent Protein Interaction Networks

open access: bronze, 2012
Rebecca Ullmann   +3 more
openalex   +1 more source

The SUMO E3 Ligase-Like Proteins PIAL1 and PIAL2 Interact with MOM1 and Form a Novel Complex Required for Transcriptional Silencing

open access: bronze, 2016
Yongfeng Han   +11 more
openalex   +1 more source

Generation of specific inhibitors of SUMO-1– and SUMO-2/3–mediated protein-protein interactions using Affimer (Adhiron) technology

open access: green, 2017
David J. Hughes   +14 more
openalex   +1 more source

Cloning and soluble expression of mature α-luffin from Luffa cylindrica inE. coli using SUMO fusion protein

open access: bronze, 2018
Shaghayegh Namvar   +5 more
openalex   +1 more source

SUMO: a (Oxidative) Stressed Protein

NeuroMolecular Medicine, 2013
Redox species are produced during the physiological cellular metabolism of a normal tissue. In turn, their presence is also attributed to pathological conditions including neurodegenerative diseases. Many are the molecular changes that occur during the unbalance of the redox homeostasis.
Feligioni, M, NISTICO', ROBERT GIOVANNI
openaire   +5 more sources

SUMO as a Solubility Tag and In Vivo Cleavage of SUMO Fusion Proteins with Ulp1 [PDF]

open access: possible, 2014
Expression of proteins in E. coli is often plagued by insolubility of the protein of interest. A solution to this problem is the expression of proteins as fusions to solubility tags such as the SUMO protein. SUMO fusion proteins can be cleaved to remove the SUMO moiety using SUMO-specific proteases such as Ulp1. Here, we describe the use of vectors for
Albert J. Courey   +2 more
openaire   +2 more sources

SUMO fusions and SUMO-specific protease for efficient expression and purification of proteins [PDF]

open access: possibleJournal of Structural and Functional Genomics, 2004
SUMO (small ubiquitin-related modifier) modulates protein structure and function by covalently binding to the lysine side chains of the target proteins. Yeast cells contain two SUMO proteases, Ulp1 and Ulp2, that cleave sumoylated proteins in the cell.
Michael R. Mattern   +5 more
openaire   +2 more sources

Protein Modification by SUMO

Annual Review of Biochemistry, 2004
▪ Abstract  Small ubiquitin-related modifier (SUMO) family proteins function by becoming covalently attached to other proteins as post-translational modifications. SUMO modifies many proteins that participate in diverse cellular processes, including transcriptional regulation, nuclear transport, maintenance of genome integrity, and signal transduction.
openaire   +3 more sources

SUMO proteins: Guardians of immune system

Journal of Autoimmunity, 2017
Small ubiquitin-like modifier (SUMO) proteins belong to the ubiquitin-like family and act to change the function of target proteins through post-translational modifications. Through their interactions with innate immune pathways, SUMOs promote an efficient immune response to pathogenic challenge avoiding, at the same time, an excess of immune response ...
ADORISIO, SABRINA   +8 more
openaire   +4 more sources

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