Target discovery of ebselen with a biotinylated probe

2018 ◽  
Vol 54 (68) ◽  
pp. 9506-9509 ◽  
Author(s):  
Zhenzhen Chen ◽  
Zhongyao Jiang ◽  
Nan Chen ◽  
Qian Shi ◽  
Lili Tong ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Protein Profiling ◽  
Robust Identification ◽  
Target Discovery

An activity-based protein profiling (ABPP) method for ebselen-binding proteins based on biotin-ebselen allowed for the robust identification of 462 targeted proteins, implicating multifunctional regulation of ebselen.

Target Discovery in Ralstonia solanacearum through an Activity-Based Protein Profiling Technique Based on Bioactive Oxadiazole Sulfones

2020 ◽  
Vol 68 (8) ◽  
pp. 2340-2346 ◽  
Author(s):  
Biao Chen ◽  
Qing-Su Long ◽  
Jiao Meng ◽  
Xiang Zhou ◽  
Zhi-Bing Wu ◽  
...  
Keyword(s):  
Ralstonia Solanacearum ◽  
Protein Profiling ◽  
Target Discovery

scholarly journals A Glycal-Based Photoaffinity Probe That Enriches Sialic Acid Binding Proteins

2019 ◽  
Author(s):  
Peter Thuy-Boun ◽  
Dennis Wolan
Keyword(s):  
Sialic Acid ◽  
Binding Proteins ◽  
Binding Protein ◽  
Factor H ◽  
Protein Profiling ◽  
Complement Factor ◽  
Acid Binding Protein ◽  
Sialic Acid Binding ◽  
Kinetic Inhibition ◽  
Protein Complement

<p>To identify sialic acid binding proteins from complex proteomes, three photocrosslinking affinity-based probes were constructed using Neu5Ac (<b>5 </b>and <b>6</b>) and Neu5Ac2en (<b>7</b>) scaffolds. Kinetic inhibition assays and Western blotting revealed the Neu5Ac2en-based <b>7 </b>to be an effective probe for the labeling of a purified gut microbial sialidase (BDI_2946) and a purified human sialic acid binding protein (hCD33). Additionally, LC-MS/MS affinity-based protein profiling verified the ability of <b>7</b>to enrich a low-abundance sialic acid binding protein (complement factor H) from human serum thus validating the utility of this probe in a complex context.</p>

scholarly journals A Glycal-Based Photoaffinity Probe That Enriches Sialic Acid Binding Proteins

2019 ◽  
Author(s):  
Peter Thuy-Boun ◽  
Dennis Wolan
Keyword(s):  
Sialic Acid ◽  
Binding Proteins ◽  
Binding Protein ◽  
Factor H ◽  
Protein Profiling ◽  
Complement Factor ◽  
Acid Binding Protein ◽  
Sialic Acid Binding ◽  
Kinetic Inhibition ◽  
Protein Complement

<p>To identify sialic acid binding proteins from complex proteomes, three photocrosslinking affinity-based probes were constructed using Neu5Ac (<b>5 </b>and <b>6</b>) and Neu5Ac2en (<b>7</b>) scaffolds. Kinetic inhibition assays and Western blotting revealed the Neu5Ac2en-based <b>7 </b>to be an effective probe for the labeling of a purified gut microbial sialidase (BDI_2946) and a purified human sialic acid binding protein (hCD33). Additionally, LC-MS/MS affinity-based protein profiling verified the ability of <b>7</b>to enrich a low-abundance sialic acid binding protein (complement factor H) from human serum thus validating the utility of this probe in a complex context.</p>

High resolution spot scan imaging of frozen, hydrated actin bundles with 400kV electrons

1992 ◽  
Vol 50 (1) ◽  
pp. 512-513
Author(s):  
J. Jakana ◽  
M.F. Schmid ◽  
P. Matsudaira ◽  
W. Chiu
Keyword(s):  
High Resolution ◽  
Binding Proteins ◽  
Actin Binding ◽  
Eukaryotic Cells ◽  
Dimensional Structure ◽  
Structural Basis ◽  
Actin Bundle ◽  
Actin Bundles ◽  
3 Dimensional ◽  
Macromolecular Assembly

Actin is a protein found in all eukaryotic cells. In its polymerized form, the cells use it for motility, cytokinesis and for cytoskeletal support. An example of this latter class is the actin bundle in the acrosomal process from the Limulus sperm. The different functions actin performs seem to arise from its interaction with the actin binding proteins. A 3-dimensional structure of this macromolecular assembly is essential to provide a structural basis for understanding this interaction in relationship to its development and functions.

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