scholarly journals The impact of contrast-enhanced spectral mammogram (CESM) and three-dimensional breast ultrasound (3DUS) on the characterization of the disease extend in cancer patients

2018 ◽  
pp. 20170977 ◽  
Author(s):  
Maha Hussien Helal ◽  
Sahar Mahmoud Mansour ◽  
Lamia Adel Salaleldin ◽  
Basma Mohamed Alkalaawy ◽  
Dorria Saleh Salem ◽  
...  
Amino Acids ◽  
2019 ◽  
Vol 51 (10-12) ◽  
pp. 1409-1431 ◽  
Author(s):  
Luigi Grassi ◽  
Chiara Cabrele

Abstract Peptides and proteins are preponderantly emerging in the drug market, as shown by the increasing number of biopharmaceutics already approved or under development. Biomolecules like recombinant monoclonal antibodies have high therapeutic efficacy and offer a valuable alternative to small-molecule drugs. However, due to their complex three-dimensional structure and the presence of many functional groups, the occurrence of spontaneous conformational and chemical changes is much higher for peptides and proteins than for small molecules. The characterization of biotherapeutics with modern and sophisticated analytical methods has revealed the presence of contaminants that mainly arise from oxidation- and elimination-prone amino-acid side chains. This review focuses on protein chemical modifications that may take place during storage due to (1) oxidation (methionine, cysteine, histidine, tyrosine, tryptophan, and phenylalanine), (2) intra- and inter-residue cyclization (aspartic and glutamic acid, asparagine, glutamine, N-terminal dipeptidyl motifs), and (3) β-elimination (serine, threonine, cysteine, cystine) reactions. It also includes some examples of the impact of such modifications on protein structure and function.


2014 ◽  
Vol 20 (3) ◽  
pp. 177-187 ◽  
Author(s):  
Ioannis Papantoniou ◽  
Maarten Sonnaert ◽  
Liesbet Geris ◽  
Frank P. Luyten ◽  
Jan Schrooten ◽  
...  

2011 ◽  
Vol 29 (3) ◽  
pp. E62-E66 ◽  
Author(s):  
Maria Riccarda Del Bene ◽  
Francesco Cappelli ◽  
Luigi Rega ◽  
Francesco Venditti ◽  
Giuseppe Barletta

Author(s):  
Aikaterini Kefala ◽  
Dina Kotsifaki ◽  
Mary Providaki ◽  
Maria Amprazi ◽  
Michael Kokkinidis

Earlier studies have found that the occurrence of inverse sequence identity in proteins is not indicative of three-dimensional similarity, but rather leads to different folds or unfolded proteins. Short helices, however, frequently keep their conformations when their sequences are inverted. To explore the impact of sequence inversion on long helices, revRM6, with the inverse amino-acid sequence relative to RM6, a highly stable variant of the ColE1 Rop protein, was engineered. RM6 is a highly regular four-α-helical bundle that serves as a model system for protein-folding studies. Here, the crystallization and preliminary crystallographic characterization of revRM6 are reported. The protein was overexpressed inEscherichia coli, purified to homogeneity and crystallized. The crystals belonged to space groupP41212, with unit-cell parametersa=b= 44.98,c= 159.74 Å, and diffracted to a resolution of 3.45 Å.


2021 ◽  
Vol 5 (3) ◽  
pp. 204
Author(s):  
Jia, MD Wanru ◽  
Zhang, MD Jingwen, ◽  
Dong, MD Yijie ◽  
Zhu, MD Ying ◽  
Jia, MD Xiaohong ◽  
...  

Molecules ◽  
2020 ◽  
Vol 25 (14) ◽  
pp. 3144
Author(s):  
Dmitry Tikhonov ◽  
Liudmila Kulikova ◽  
Arthur Kopylov ◽  
Kristina Malsagova ◽  
Alexander Stepanov ◽  
...  

New advances in protein post-translational modifications (PTMs) have revealed a complex layer of regulatory mechanisms through which PTMs control cell signaling and metabolic pathways, contributing to the diverse metabolic phenotypes found in cancer. Using conformational templates and the three-dimensional (3D) environment investigation of proteins in patients with colorectal cancer, it was demonstrated that most PTMs (phosphorylation, acetylation, and ubiquitination) are localized in the supersecondary structures (helical pairs). We showed that such helical pairs are represented on the outer surface of protein molecules and characterized by a largely accessible area for the surrounding solvent. Most promising and meaningful modifications were observed on the surface of vitamin D-binding protein (VDBP), complement C4-A (CO4A), X-ray repair cross-complementing protein 6 (XRCC6), Plasma protease C1 inhibitor (IC1), and albumin (ALBU), which are related to colorectal cancer developing. Based on the presented data, we propose the impact of the observed modifications in immune response, inflammatory reaction, regulation of cell migration, and promotion of tumor growth. Here, we suggest a computational approach in which high-throughput analysis for identification and characterization of PTM signature, associated with cancer metabolic reprograming, can be improved to prognostic value and bring a new strategy to the targeted therapy.


2016 ◽  
Vol 848 ◽  
pp. 722-725
Author(s):  
Kai Wang ◽  
Min Huang ◽  
Yue Huang ◽  
Zhong Hua Zhou ◽  
Shirley Shen

Anti-fogging functional coatings have a broad application prospective in the fields of construction and transportation vehicles. In this study, superior water absorbing and anti-fogging coatings were prepared by a cure reaction using epoxy resins as water absorbent resins, hydroxyethyl ethylenediamine as a curing agent, γ-ammonia propyl triethoxy silane as a coupling agent, organic silicon sol as filler. The impact of additional polyethylene glycol (PEG) on the properties of water absorbing and antifogging coating has also been studied. The anti-fogging experiments were conducted in a 40 °C water steam bath, and the result shows that the sample with additional 4.0 % PEG has an anti-fogging time of 315 seconds (s), which is better than that without PEG (the anti-fogging time being 240s). Infrared spectroscopy and scanning electron microscope structure characterization indicate that the sample with additional PEG has an obvious three-dimensional network structure with hydroxyl groups, which leads to a great saturated water quantity and a superior anti-fogging performance.


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