Results 31 to 40 of about 13,776 (215)

How Does SUMO Participate in Spindle Organization?

open access: yesCells, 2019
The ubiquitin-like protein SUMO is a regulator involved in most cellular mechanisms. Recent studies have discovered new modes of function for this protein.
Ariane Abrieu, Dimitris Liakopoulos
doaj   +1 more source

Simplifying recombinant protein production: Combining Golden Gate cloning with a standardized protein purification scheme [PDF]

open access: yesarXiv, 2023
Recombinant protein production is pivotal in molecular biology, enabling profound insights into cellular processes through biophysical, biochemical, and structural analyses of the purified samples. The demand for substantial biomolecule quantities often presents challenges, particularly for eukaryotic proteins.
arxiv  

Super Resolution Microscopy of SUMO Proteins in Neurons [PDF]

open access: yesFrontiers in Cellular Neuroscience, 2019
The ubiquitously expressed SUMO proteins regulate a plethora of cellular pathways and processes. While they have a predominantly nuclear localization, extranuclear roles of SUMO isoforms at the synapse have also been described, making SUMOylation one of the major post-translational regulators of nerve functions.
Colnaghi L   +7 more
openaire   +5 more sources

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

SUMO Modification of Hepatitis B Virus Core Mediates Nuclear Entry, Promyelocytic Leukemia Nuclear Body Association, and Efficient Formation of Covalently Closed Circular DNA

open access: yesMicrobiology Spectrum, 2023
Persistence of hepatitis B virus (HBV) infection is due to a nuclear covalently closed circular DNA (cccDNA), generated from the virion-borne relaxed circular DNA (rcDNA) genome in a process likely involving numerous cell factors from the host DNA damage
Samuel Hofmann   +14 more
doaj   +1 more source

Bad Weather, Social Network, and Internal Migration; Case of Japanese Sumo Wrestlers 1946-1985 [PDF]

open access: yesarXiv, 2022
Post-World War II , there was massive internal migration from rural to urban areas in Japan. The location of Sumo stables was concentrated in Tokyo. Hence, supply of Sumo wrestlers from rural areas to Tokyo was considered as migration. Using a panel dataset covering forty years, specifically 1946-1985, this study investigates how weather conditions and
arxiv  

SUMO Modification: Wrestling with Protein Conformation [PDF]

open access: yesCurrent Biology, 2005
SUMO modification of human thymine-DNA glycosylase facilitates the processing of base excision repair substrates by an unusual mechanism: while leaving the catalytic center unaffected, it induces product release by eliciting a conformational change in the enzyme.
openaire   +3 more sources

A Chain of Events: Regulating Target Proteins by SUMO Polymers [PDF]

open access: yesTrends in Biochemical Sciences, 2021
Small ubiquitin-like modifiers (SUMOs) regulate virtually all nuclear processes. The fate of the target protein is determined by the architecture of the attached SUMO protein, which can be of polymeric nature. Here, we highlight the multifunctional aspects of dynamic signal transduction by SUMO polymers.
Jansen, N.S., Vertegaal, A.C.O.
openaire   +4 more sources

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

Tomosyn interacts with the SUMO E3 ligase PIASγ. [PDF]

open access: yesPLoS ONE, 2014
Protein modification by Small Ubiquitin-like MOdifier (SUMO) entities is involved in a number of neuronal functions, including synaptogenesis and synaptic plasticity. Tomosyn-1 (syntaxin-binding protein 5; STXPB5) binds to t-SNARE (Soluble NSF Attachment
Cornelia J Geerts   +4 more
doaj   +1 more source

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