scholarly journals P088 TGFB bound to GARP promotes acetylation-mediated FOXP3 protein stabilisation

Author(s):  
P Lehmkuhl ◽  
B Zapp ◽  
H Schulze-Koops ◽  
A Skapenko
Foods ◽  
2021 ◽  
Vol 10 (3) ◽  
pp. 608
Author(s):  
Inma Arenas ◽  
Miguel Ribeiro ◽  
Luís Filipe-Ribeiro ◽  
Rafael Vilamarim ◽  
Elisa Costa ◽  
...  

In this work, the effect of pre-fermentative skin maceration (PFSM) on the chemical composition of the macromolecular fraction, polysaccharides and proteins, phenolic compounds, chromatic characteristics, and protein stability of Albariño monovarietal white wines was studied. PFSM increased the extraction of phenolic compounds and polysaccharides and reduced the extraction of pathogenesis-related proteins (PRPs). PFSM wine showed significantly higher protein instability. Sodium and calcium bentonites were used for protein stabilisation of wines obtained with PFSM (+PFSM) and without PFSM (−PFSM), and their efficiencies compared to fungal chitosan (FCH) and k-carrageenan. k-Carrageenan reduced the content of PRPs and the protein instability in both wines, and it was more efficient than sodium and calcium bentonites. FCH was unable to heat stabilise both wines, and PRPs levels remained unaltered. On the other hand, FCH decreased the levels of wine polysaccharides by 60%. Sodium and calcium bentonite also decreased the levels of wine polysaccharides although to a lower extent (16% to 59%). k-Carrageenan did not affect the wine polysaccharide levels. Overall, k-carrageenan is suitable for white wine protein stabilisation, having a more desirable impact on the wine macromolecular fraction than the other fining agents, reducing the levels of the wine PRPs without impacting polysaccharide composition.


2002 ◽  
Vol 2 ◽  
pp. 1209-1215 ◽  
Author(s):  
Javier Sancho ◽  
Marta Bueno ◽  
Luis A. Campos ◽  
Juan Fernandez-Recio ◽  
Maria Pilar Iran ◽  
...  

Proteins perform many useful molecular tasks, and their biotechnological use continues to increase. As protein activity requires a stable native conformation, protein stabilisation is a major scientific and practical issue. Towards that end, many successful protein stabilisation strategies have been devised in recent years. In most cases, model proteins with a two-state folding equilibrium have been used to study and demonstrate protein stabilisation. Many proteins, however, display more complex folding equilibria where stable intermediates accumulate. Stabilising these proteins requires specifically stabilising the native state relative to the intermediates, as these are expected to lack activity. Here we discuss how to investigate the ‘relevant’ stability of proteins with equilibrium intermediates and propose a way to dissect the contribution of side chain interactions to the overall stability into the ‘relevant’ and ‘nonrelevant’ terms. Examples of this analysis performed on apoflavodoxin and in a single-chain mini antibody are presented.


ChemBioChem ◽  
2015 ◽  
Vol 16 (10) ◽  
pp. 1454-1459 ◽  
Author(s):  
Hyoung Eun Bae ◽  
Kamil Gotfryd ◽  
Jennifer Thomas ◽  
Hazrat Hussain ◽  
Muhammad Ehsan ◽  
...  

2015 ◽  
Vol 23 ◽  
pp. A57
Author(s):  
K.A. Staines ◽  
M. Prideaux ◽  
P. Hohenstein ◽  
D.J. Buttle ◽  
A.A. Pitsillides ◽  
...  

2017 ◽  
Vol 19 (13) ◽  
pp. 8667-8670 ◽  
Author(s):  
A. Sanchez-Fernandez ◽  
K. J. Edler ◽  
T. Arnold ◽  
D. Alba Venero ◽  
A. J. Jackson

Deep eutectic solvents as media for protein stabilisation: conformation in the absence and presence of water.


2009 ◽  
Vol 44 (2) ◽  
pp. 330-336 ◽  
Author(s):  
Johannes de Bruijn ◽  
Cristina Loyola ◽  
Adan Flores ◽  
Felicitas Hevia ◽  
Pedro Melín ◽  
...  

2021 ◽  
Author(s):  
Julianty Frost ◽  
Sonia Rocha ◽  
Alessio Ciulli

The vonHippel Lindau (VHL) protein is a tumour suppressor protein frequently mutated in the VHL disease, which functions as substrate recognition subunit of a Cul2 E3 ubiquitin ligase (CRL2VHL). CRL2VHL plays an important role in oxygen sensing, by binding and targeting Hypoxia Inducible Factor-alpha subunits (HIF-alpha) for ubiquitination and degradation. VHL is also commonly hijacked by heterobifunctional degrader molecules known as proteolysis-targeting chimeras (PROTACs). In previous work we reported the structure-based design and functional characterisation of VHL inhibitors (VH032 and VH298) that induce the HIF response in cells. Here, we use unbiased quantitative mass spectrometry to identify the proteomic changes elicited by the VHL inhibitor and compare this to hypoxia or broad-spectrum prolyl-hydroxylase domain (PHD) enzyme inhibitor IOX2. Our results demonstrate the VHL inhibitor selectively activates the HIF response that vastly overlaps with hypoxia- and IOX2-induced proteomic changes. Interestingly, VHL inhibitors were found to selectively upregulate a single protein, which is VHL itself. Our analysis revealed that this occurs via protein stabilisation of VHL isoforms and not via changes in transcript levels. Increased VHL levels upon VH298 treatment resulted in turn to reduced levels of HIF-1 protein. Our results demonstrate the high specificity of VHL inhibitors and suggest that use of these inhibitors would not produce overtly side effects due to prolonged HIF stabilisation. They also exemplify the concept that small-molecule binding induced protein stabilisation can increase protein levels inside cells.


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