scholarly journals Protein–Polymer Conjugation via Ligand Affinity and Photoactivation of Glutathione S-Transferase

2014 ◽  
Vol 25 (10) ◽  
pp. 1902-1909 ◽  
Author(s):  
En-Wei Lin ◽  
Natalie Boehnke ◽  
Heather D. Maynard
Keyword(s):  
Glutathione S Transferase ◽  
Ligand Affinity ◽  
Protein Polymer ◽  
Polymer Conjugation

scholarly journals pH-Triggered Reversible Multiple Protein–Polymer Conjugation Based on Molecular Recognition

2015 ◽  
Vol 119 (36) ◽  
pp. 12066-12073 ◽  
Author(s):  
Juan Liu ◽  
Viktoriia Postupalenko ◽  
Jason T. Duskey ◽  
Cornelia G. Palivan ◽  
Wolfgang Meier
Keyword(s):  
Molecular Recognition ◽  
Protein Polymer ◽  
Multiple Protein ◽  
Polymer Conjugation

Monitoring Protein−Polymer Conjugation by a Fluorogenic Cu(I)-Catalyzed Azide−Alkyne 1,3-Dipolar Cycloaddition

2009 ◽  
Vol 20 (6) ◽  
pp. 1129-1138 ◽  
Author(s):  
A. (Ton) J. Dirks ◽  
Jeroen J. L. M. Cornelissen ◽  
Roeland J. M. Nolte
Keyword(s):  
Dipolar Cycloaddition ◽  
Protein Polymer ◽  
Polymer Conjugation

scholarly journals A guide to maximizing the therapeutic potential of protein–polymer conjugates by rational design

2018 ◽  
Vol 47 (24) ◽  
pp. 8998-9014 ◽  
Author(s):  
Jeong Hoon Ko ◽  
Heather D. Maynard
Keyword(s):  
Rational Design ◽  
Therapeutic Potential ◽  
Careful Planning ◽  
Therapeutic Applications ◽  
Polymer Conjugates ◽  
Protein Polymer ◽  
Conjugation Chemistry ◽  
Polymer Conjugation ◽  
Selection Of

Careful planning in the selection of the protein, polymer, conjugation chemistry, and analysis can help maximize the potential of protein–polymer conjugates for therapeutic applications.

Direct introduction of R-SO2F moieties into proteins and protein-polymer conjugation using SuFEx chemistry

Polymer ◽  
2016 ◽  
Vol 99 ◽  
pp. 7-12 ◽  
Author(s):  
Shaohua Li ◽  
Devora Cohen-Karni ◽  
Laura T. Beringer ◽  
Changgong Wu ◽  
Ethan Kallick ◽  
...  
Keyword(s):  
Direct Introduction ◽  
Protein Polymer ◽  
Polymer Conjugation

A supramolecular route for reversible protein-polymer conjugation

2011 ◽  
Vol 2 (2) ◽  
pp. 279-286 ◽  
Author(s):  
Frank Biedermann ◽  
Urs Rauwald ◽  
Jameel M. Zayed ◽  
Oren A. Scherman
Keyword(s):  
Protein Polymer ◽  
Polymer Conjugation

The microtubule associated protein (MAP) tau forms a new class of triple-stranded left-hand helical fibrous protein polymer

1992 ◽  
Vol 50 (1) ◽  
pp. 540-541
Author(s):  
G. C. Ruben ◽  
K. Iqbal ◽  
I. Grundke-Iqbal ◽  
H. Wisniewski ◽  
T. L. Ciardelli ◽  
...  
Keyword(s):  
Axial Ratio ◽  
Normal Structure ◽  
Paired Helical Filaments ◽  
Left Hand ◽  
New Class ◽  
Protein Polymer ◽  
Fibrous Protein ◽  
Protein Map ◽  
Neurotransmitter Transport ◽  
Alzheimer Neurofibrillary Tangles

In neurons, the microtubule associated protein, tau, is found in the axons. Tau stabilizes the microtubules required for neurotransmitter transport to the axonal terminal. Since tau has been found in both Alzheimer neurofibrillary tangles (NFT) and in paired helical filaments (PHF), the study of tau's normal structure had to preceed TEM studies of NFT and PHF. The structure of tau was first studied by ultracentrifugation. This work suggested that it was a rod shaped molecule with an axial ratio of 20:1. More recently, paraciystals of phosphorylated and nonphosphoiylated tau have been reported. Phosphorylated tau was 90-95 nm in length and 3-6 nm in diameter where as nonphosphorylated tau was 69-75 nm in length. A shorter length of 30 nm was reported for undamaged tau indicating that it is an extremely flexible molecule. Tau was also studied in relation to microtubules, and its length was found to be 56.1±14.1 nm.

Glutathione system participation in thoracic aneurysms from patients with Marfan syndrome

VASA ◽  
2017 ◽  
Vol 46 (3) ◽  
pp. 177-186 ◽  
Author(s):  
Alejandra María Zúñiga-Muñoz ◽  
Israel Pérez-Torres ◽  
Verónica Guarner-Lans ◽  
Elías Núñez-Garrido ◽  
Rodrigo Velázquez Espejel ◽  
...  
Keyword(s):  
Aortic Aneurysm ◽  
Marfan Syndrome ◽  
Aortic Aneurysms ◽  
Aortic Dilatation ◽  
Glutathione S Transferase ◽  
Reduced And Oxidized Glutathione ◽  
Total Antioxidant ◽  
Elevated Activity ◽  
Acute Dissection ◽  
Thoracic Aneurysms

Abstract. Background: Aortic dilatation in Marfan syndrome (MFS) is progressive. It is associated with oxidative stress and endothelial dysfunction that contribute to the early acute dissection of the vessel and can result in rupture of the aorta and sudden death. We evaluated the participation of the glutathione (GSH) system, which could be involved in the mechanisms that promote the formation and progression of the aortic aneurysms in MFS patients. Patients and methods: Aortic aneurysm tissue was obtained during chest surgery from eight control subjects and 14 MFS patients. Spectrophotometrical determination of activity of glutathione peroxidase (GPx), glutathione-S-transferase (GST), glutathione reductase (GR), lipid peroxidation (LPO) index, carbonylation, total antioxidant capacity (TAC), and concentration of reduced and oxidized glutathione (GSH and GSSG respectively), was performed in the homogenate from aortic aneurysm tissue. Results: LPO index, carbonylation, TGF-β1, and GR activity were increased in MFS patients (p < 0.04), while TAC, GSH/GSSG ratio, GPx, and GST activity were significantly decreased (p < 0.04). Conclusions: The depletion of GSH, in spite of the elevated activity of GR, not only diminished the activity of GSH-depend GST and GPx, but increased LPO, carbonylation and decreased TAC. These changes could promote the structural and functional alterations in the thoracic aorta of MFS patients.

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