scholarly journals Tripping the Light Fantastic: Blue-Light Photoreceptors as Examples of Environmentally Modulated Protein−Protein Interactions

Biochemistry ◽  
2011 ◽  
Vol 50 (1) ◽  
pp. 4-16 ◽  
Author(s):  
Brian D. Zoltowski ◽  
Kevin H. Gardner
Keyword(s):  
Blue Light ◽  
Protein Interactions ◽  
Protein Protein Interactions

scholarly journals Optogenetic control of mRNA localization and translation in live cells

2020 ◽  
Author(s):  
Sangkyu Lee ◽  
Won Heo ◽  
Na Kim
Keyword(s):  
Protein Synthesis ◽  
Blue Light ◽  
Protein Interactions ◽  
Mrna Localization ◽  
Spatiotemporal Dynamics ◽  
Live Cells ◽  
Protein Protein Interactions ◽  
Protein Clusters ◽  
Specific Mrnas ◽  
Specific Mrna

Abstract Numerous efforts have been made toward the goal of visualizing the spatiotemporal dynamics of single mRNA molecules, yet our capacity for precisely controlling their functions lags behind. Here, we present an optogenetic approach for manipulating the localization and translation of specific mRNAs in live cells. Our technique combines blue light-responsive protein-protein interactions with mRNA visualization modules to robustly and reversibly generate protein clusters that can trap specific mRNA molecules. This sequestration reduces the binding chance of mRNAs with ribosomes, thereby dramatically attenuating protein synthesis

scholarly journals Optical Control of Protein–Protein Interactions via Blue Light-Induced Domain Swapping

Biochemistry ◽  
2014 ◽  
Vol 53 (30) ◽  
pp. 5008-5016 ◽  
Author(s):  
Jakeb M. Reis ◽  
Darcy C. Burns ◽  
G. Andrew Woolley
Keyword(s):  
Blue Light ◽  
Protein Interactions ◽  
Domain Swapping ◽  
Optical Control ◽  
Protein Protein Interactions

scholarly journals Blue light photosensors: Examples of environmentally‐regulated protein/protein interactions

2009 ◽  
Vol 23 (S1) ◽  
Author(s):  
Kevin H. Gardner ◽  
Abigail I. Nash ◽  
Wen‐huang Ko ◽  
Fernando Correa ◽  
Qiong Wu
Keyword(s):  
Blue Light ◽  
Protein Interactions ◽  
Protein Protein Interactions

scholarly journals Optogenetic control of mRNA localization and translation in live cells

2020 ◽  
Author(s):  
Na Yeon Kim ◽  
Sangkyu Lee ◽  
Won Do Heo
Keyword(s):  
Protein Synthesis ◽  
Blue Light ◽  
Protein Interactions ◽  
Mrna Localization ◽  
Spatiotemporal Dynamics ◽  
Live Cells ◽  
Protein Protein Interactions ◽  
Protein Clusters ◽  
Specific Mrnas ◽  
Specific Mrna

Abstract Numerous efforts have been made toward the goal of visualizing the spatiotemporal dynamics of single mRNA molecules, yet our capacity for precisely controlling their functions lags behind. Here, we present an optogenetic approach for manipulating the localization and translation of specific mRNAs in live cells. Our technique combines blue light-responsive protein-protein interactions with mRNA visualization modules to robustly and reversibly generate protein clusters that can trap specific mRNA molecules. This sequestration reduces the binding chance of mRNAs with ribosomes, thereby dramatically attenuating protein synthesis

Protein-protein interactions of the p53 family with the Bcl-2 family in hepatocellular carcinoma

2011 ◽  
Vol 49 (08) ◽  
Author(s):  
LC König ◽  
M Meinhard ◽  
C Sandig ◽  
MH Bender ◽  
A Lovas ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Protein Interactions ◽  
Protein Protein Interactions ◽  
P53 Family

Partial Purification of a Specific Plasminogen Activator from Porcine Parotid Glands

1974 ◽  
Vol 31 (03) ◽  
pp. 403-414 ◽  
Author(s):  
Terence Cartwright
Keyword(s):  
Nucleic Acid ◽  
Salivary Glands ◽  
Plasminogen Activator ◽  
Protein Interactions ◽  
Partial Purification ◽  
Protein Protein Interactions ◽  
Parotid Glands ◽  
Two Stage ◽  
Preliminary Characterization ◽  
Specific Inhibitors

SummaryA method is described for the extraction with buffers of near physiological pH of a plasminogen activator from porcine salivary glands. Substantial purification of the activator was achieved although this was to some extent complicated by concomitant extraction of nucleic acid from the glands. Preliminary characterization experiments using specific inhibitors suggested that the activator functioned by a similar mechanism to that proposed for urokinase, but with some important kinetic differences in two-stage assay systems. The lack of reactivity of the pig gland enzyme in these systems might be related to the tendency to protein-protein interactions observed with this material.

Target-Templated de novo Design of Macrocyclic D-/L-Peptides: Inhibitors of the PD-1/PD-L1 Interaction

2020 ◽  
Author(s):  
Salvador Guardiola ◽  
Monica Varese ◽  
Xavier Roig ◽  
Jesús Garcia ◽  
Ernest Giralt
Keyword(s):  
Protein Interactions ◽  
Cyclic Peptides ◽  
General Framework ◽  
Large Scale ◽  
De Novo ◽  
Inhibitory Effect ◽  
Original Text ◽  
Protein Protein Interactions ◽  
Retraction Notice ◽  
Pharmaceutical Properties

<p>NOTE: This preprint has been retracted by consensus from all authors. See the retraction notice in place above; the original text can be found under "Version 1", accessible from the version selector above.</p><p><br></p><p>------------------------------------------------------------------------</p><p><br></p><p>Peptides, together with antibodies, are among the most potent biochemical tools to modulate challenging protein-protein interactions. However, current structure-based methods are largely limited to natural peptides and are not suitable for designing target-specific binders with improved pharmaceutical properties, such as macrocyclic peptides. Here we report a general framework that leverages the computational power of Rosetta for large-scale backbone sampling and energy scoring, followed by side-chain composition, to design heterochiral cyclic peptides that bind to a protein surface of interest. To showcase the applicability of our approach, we identified two peptides (PD-<i>i</i>3 and PD-<i>i</i>6) that target PD-1, a key immune checkpoint, and work as protein ligand decoys. A comprehensive biophysical evaluation confirmed their binding mechanism to PD-1 and their inhibitory effect on the PD-1/PD-L1 interaction. Finally, elucidation of their solution structures by NMR served as validation of our <i>de novo </i>design approach. We anticipate that our results will provide a general framework for designing target-specific drug-like peptides.<i></i></p>

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