scholarly journals Comparative Analysis of Mass-Spectrometry-Based Proteomic Methods for Protein Target Discovery Using a One-Pot Approach

2019 ◽  
Vol 31 (2) ◽  
pp. 217-226 ◽  
Author(s):  
Aurora Cabrera ◽  
Nancy Wiebelhaus ◽  
Baiyi Quan ◽  
Renze Ma ◽  
He Meng ◽  
...  
Molbank ◽  
10.3390/m1140 ◽  
2020 ◽  
Vol 2020 (2) ◽  
pp. M1140
Author(s):  
Jack Bennett ◽  
Paul Murphy

(2S,3R,6R)-2-[(R)-1-Hydroxyallyl]-4,4-dimethoxy-6-methyltetrahydro-2H-pyran-3-ol was isolated in 18% after treating the glucose derived (5R,6S,7R)-5,6,7-tris[(triethylsilyl)oxy]nona-1,8-dien-4-one with (1S)-(+)-10-camphorsulfonic acid (CSA). The one-pot formation of the title compound involved triethylsilyl (TES) removal, alkene isomerization, intramolecular conjugate addition and ketal formation. The compound was characterized by 1H and 13C NMR spectroscopy, ESI mass spectrometry and IR spectroscopy. NMR spectroscopy was used to establish the product structure, including the conformation of its tetrahydropyran ring.


2019 ◽  
Vol 567 ◽  
pp. 90-95 ◽  
Author(s):  
Lauana Fogaça de Almeida ◽  
Leonardo Nazário de Moraes ◽  
Lucilene Delazari dos Santos ◽  
Guilherme Targino Valente

2012 ◽  
Vol 58 (2) ◽  
pp. 353-365 ◽  
Author(s):  
Ana Konvalinka ◽  
James W Scholey ◽  
Eleftherios P Diamandis

Abstract BACKGROUND Technological advances have resulted in a renaissance of proteomic studies directed at finding markers of disease progression, diagnosis, or responsiveness to therapy. Renal diseases are ideally suited for such research, given that urine is an easily accessible biofluid and its protein content is derived mainly from the kidney. Current renal prognostic markers have limited value, and renal biopsy remains the sole method for establishing a diagnosis. Mass spectrometry instruments, which can detect thousands of proteins at nanomolar (or even femtomolar) concentrations, may be expected to allow the discovery of improved markers of progression, diagnosis, or treatment responsiveness. CONTENT In this review we describe the strengths and limitations of proteomic methods and the drawbacks of existing biomarkers, and provide an overview of opportunities in the field. We also highlight several proteomic studies of biomarkers of renal diseases selected from the plethora of studies performed. SUMMARY It is clear that the field of proteomics has not yet fulfilled its promise. However, ongoing efforts to standardize sample collection and preparation, improve study designs, perform multicenter validations, and create joint industry–regulatory bodies offer promise for the recognition of novel molecules that could change clinical nephrology forever.


2010 ◽  
Vol 21 (22) ◽  
pp. 3963-3972 ◽  
Author(s):  
Neus Teixidó-Travesa ◽  
Judit Villén ◽  
Cristina Lacasa ◽  
Maria Teresa Bertran ◽  
Marco Archinti ◽  
...  

The γ-tubulin complex is a multi-subunit protein complex that nucleates microtubule polymerization. γ-Tubulin complexes are present in all eukaryotes, but size and subunit composition vary. In Drosophila, Xenopus, and humans large γ-tubulin ring complexes (γTuRCs) have been described, which have a characteristic open ring-shaped structure and are composed of a similar set of subunits, named γ-tubulin, GCPs 2-6, and GCP-WD in humans. Despite the identification of these proteins, γTuRC function and regulation remain poorly understood. Here we establish a new method for the purification of native human γTuRC. Using mass spectrometry of whole protein mixtures we compared the composition of γTuRCs from nonsynchronized and mitotic human cells. Based on our analysis we can define core subunits as well as more transient interactors such as the augmin complex, which associates specifically with mitotic γTuRCs. We also identified GCP8/MOZART2 as a novel core subunit that is present in both interphase and mitotic γTuRCs. GCP8 depletion does not affect γTuRC assembly but interferes with γTuRC recruitment and microtubule nucleation at interphase centrosomes without disrupting general centrosome structure. GCP8-depleted cells do not display any obvious mitotic defects, suggesting that GCP8 specifically affects the organization of the interphase microtubule network.


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