Results 41 to 50 of about 445,929 (364)

iProteinDB: An Integrative Database of Drosophila Post-translational Modifications

open access: yesG3: Genes, Genomes, Genetics, 2019
Post-translational modification (PTM) serves as a regulatory mechanism for protein function, influencing their stability, interactions, activity and localization, and is critical in many signaling pathways.
Yanhui Hu   +10 more
doaj   +1 more source

Citrullination Post-Translational Modification: State of the Art of Brain Tumor Investigations and Future Perspectives

open access: yesDiagnostics, 2023
The present review aims to describe the state of the art of research studies investigating the citrullination post-translational modification in adult and pediatric brain tumors.
Diana Valeria Rossetti   +4 more
doaj   +1 more source

Nucleosome sliding can influence the spreading of histone modifications [PDF]

open access: yes, 2021
Nucleosomes are the fundamental building blocks of chromatin that not only help in the folding of chromatin but also in carrying epigenetic information. It is known that nucleosome sliding is responsible for dynamically organizing chromatin structure and the resulting gene regulation.
arxiv   +1 more source

Interplay between R513 methylation and S516 phosphorylation of the cardiac voltage-gated sodium channel [PDF]

open access: yes, 2014
Arginine methylation is a novel post-translational modification within the voltage-gated ion channel superfamily, including the cardiac sodium channel, Naᵥ1.5.
Beltran-Alvarez, Pedro   +5 more
core   +1 more source

Post-translational modifications of transporters

open access: yesPharmacology & Therapeutics, 2018
Drug transporter proteins are critical to the distribution of a wide range of endogenous compounds and xenobiotics such as hormones, bile acids, peptides, lipids, sugars, and drugs. There are two classes of drug transporters- the solute carrier (SLC) transporters and ATP-binding cassette (ABC) transporters -which predominantly differ in the energy ...
Lindsay C. Czuba   +2 more
openaire   +4 more sources

Post-Translational Modifications of TRP Channels [PDF]

open access: yesCells, 2014
Transient receptor potential (TRP) channels constitute an ancient family of cation channels that have been found in many eukaryotic organisms from yeast to human. TRP channels exert a multitude of physiological functions ranging from Ca2+ homeostasis in the kidney to pain reception and vision. These channels are activated by a wide range of stimuli and
Olaf Voolstra, Armin Huber
openaire   +4 more sources

Post-translational modifications of the polycystin proteins [PDF]

open access: yesCellular Signalling, 2020
Autosomal dominant polycystic kidney disease (ADPKD) is the most common inherited cause of kidney failure and affects up to 12 million people worldwide. Germline mutations in two genes, PKD1 or PKD2, account for almost all patients with ADPKD.
Streets, A., Ong, A.
openaire   +2 more sources

Citrullination – small change with a great consequence [PDF]

open access: yes, 2013
Citrullination is one of the possible post-translational modifications of proteins. It is based on a conversion of L-arginine residue (L-Arg) to L-citrulline residue (L-Cit). The reaction is catalyzed by peptidylarginine deiminases (PAD). The change of L-
Gogól Mariusz
core   +1 more source

Near atmospheric carbon dioxide activates plant ubiquitin cross-linking

open access: yesBBA Advances, 2023
Background Identifying CO2-binding proteins is vital for our knowledge of CO2-regulated molecular processes. The carbamate post-translational modification is a reversible CO2-mediated adduct that can form on neutral N-terminal α-amino or lysine ε-amino ...
Harry G Gannon, Martin J Cann
doaj  

Role of glutathionylation in infection and inflammation [PDF]

open access: yes, 2019
Glutathionylation, that is, the formation of mixed disulfides between protein cysteines and glutathione (GSH) cysteines, is a reversible post-translational modification catalyzed by dierent cellular oxidoreductases, by which the redox state of the cell
Baldelli, S.   +5 more
core   +1 more source

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