Results 21 to 30 of about 312,553 (300)

Deciphering post‐translational modification codes [PDF]

open access: yesFEBS Letters, 2013
Post‐translational modifications (PTMs) occur on nearly all proteins. Many domains within proteins are modified on multiple amino acid sidechains by diverse enzymes to create a myriad of possible protein species. How these combinations of PTMs lead to distinct biological outcomes is only beginning to be understood.
Lothrop, Adam P.   +2 more
openaire   +2 more sources

Post‐translation modification of proteins in tears [PDF]

open access: yesELECTROPHORESIS, 2010
AbstractThis is the first 2‐DE study using sequential dyes to analyse phospho‐, glyco‐ and total tear protein profiles (Pro‐Q Diamond for phosphoprotein, Pro‐Q Emerald for glycoprotein and Sypro Ruby for total protein). This method minimised the gel–gel variations, allowing better comparisons among the three profiles and generated a whole map of PTM ...
You, Jingjing   +10 more
openaire   +5 more sources

Post-Translational Modifications in the Nuclear Region of Young, Aged, and Cataract Human Lenses

open access: yes, 2007
The urea-soluble proteins from the nucleus of two young, two aged, and two early-stage nuclear cataract lenses were subjected to tryptic digestion and analysis by 2D LC−MS/MS. Several novel post-translational modifications were identified.
Peter G. Hains (4270291)   +1 more
core   +5 more sources

Analysis of a macrophage carbamylated proteome reveals a function in post-translational modification crosstalk

open access: yesCell Communication and Signaling, 2023
Background Lysine carbamylation is a biomarker of rheumatoid arthritis and kidney diseases. However, its cellular function is understudied due to the lack of tools for systematic analysis of this post-translational modification (PTM).
Youngki You   +9 more
doaj   +1 more source

A convolutional neural network based tool for predicting protein AMPylation sites from binary profile representation

open access: yesScientific Reports, 2022
AMPylation is an emerging post-translational modification that occurs on the hydroxyl group of threonine, serine, or tyrosine via a phosphodiester bond. AMPylators catalyze this process as covalent attachment of adenosine monophosphate to the amino acid ...
Sayed Mehedi Azim   +4 more
doaj   +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   +3 more sources

Post-Translational Modification of Lamins: Mechanisms and Functions

open access: yesFrontiers in Cell and Developmental Biology, 2022
Lamins are the ancient type V intermediate filament proteins contributing to diverse biological functions, such as the maintenance of nuclear morphology, stabilization of chromatin architecture, regulation of cell cycle progression, regulation of spatial-
Mingyue Zheng   +2 more
doaj   +1 more source

Post-translational protein modifications in schizophrenia [PDF]

open access: yesnpj Schizophrenia, 2020
AbstractResearch investigating the pathophysiology of schizophrenia has not yet precisely defined the molecular phenotype of this disorder. Many studies have investigated cellular dysfunction by examining expression levels of molecular targets in postmortem patient brain; however, inconsistencies between transcript and protein measures in schizophrenia
Toni M. Mueller   +1 more
openaire   +2 more sources

Asparagine hydroxylation is a reversible post-translational modification [PDF]

open access: yes, 2020
Amino acid hydroxylation is a common post-translational modification, which generally regulates protein interactions or adds a functional group that can be further modified.
Peet, Daniel J.   +4 more
core   +1 more source

Biosynthesis and functions of sulfur modifications in tRNA

open access: yesFrontiers in Genetics, 2014
Sulfur is an essential element for a variety of cellular constituents in all living organisms. In tRNA molecules, there are many sulfur-containing nucleosides, such as the derivatives of 2‑thiouridine (s2U), 4-thiouridine (s4U), 2-thiocytidine (s2C), and
Naoki eShigi
doaj   +1 more source

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