Click Chemistry in Proteomic Investigations
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TLDR
This Primer discusses how one of the most versatile bioorthogonal reactions, "click chemistry", has been exploited to overcome limitations of biological approaches to enable the selective marking and functional investigation of critical protein-small-molecule interactions and PTMs in native biological environments.About:
This article is published in Cell.The article was published on 2020-02-20 and is currently open access. It has received 165 citations till now. The article focuses on the topics: Click chemistry.read more
Citations
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A Pragmatic Guide to Enrichment Strategies for Mass Spectrometry-based Glycoproteomics.
TL;DR: Common enrichment strategies used in modern mass spectrometry (MS)-based glycoproteomic experiments, including lectins and other affinity chromatographies, hydrophilic interaction chromatography (HILIC) and its derivatives, porous graphitic carbon (PGC), reversible and irreversible chemical coupling strategies, and chemical biology tools that often leverage bioorthogonal handles are reviewed.
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Arylfluorosulfate-Based Electrophiles for Covalent Protein Labeling: A New Addition to the Arsenal.
TL;DR: The recent but intense introduction of arylfluorosulfates into the arsenal of available warheads for selective covalent modification of proteins is reviewed to highlight the untapped potential of this functional group for use in chemical biology and drug discovery.
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High-Throughput Screening Platforms in the Discovery of Novel Drugs for Neurodegenerative Diseases
TL;DR: A review of the increasing role of HTS in contemporary drug discovery processes, in particular for NDDs, and evaluate the criteria underlying its successful application is presented in this paper.
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Expedited mapping of the ligandable proteome using fully functionalized enantiomeric probe pairs.
Yujia Wang,Melissa M. Dix,Giulia Bianco,Jarrett R. Remsberg,Hsinyu Lee,Marian Kalocsay,Steven P. Gygi,Stefano Forli,Gregory D. Vite,R. Michael Lawrence,Christopher G. Parker,Benjamin F. Cravatt +11 more
TL;DR: This work identifies numerous stereoselective protein–fragment interactions in cells and shows that these interactions occur at functional sites on proteins from diverse classes, indicating that incorporating chirality into fully functionalized fragment libraries provides a robust and streamlined method to discover ligandable proteins in cells.
References
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A stepwise huisgen cycloaddition process: copper(I)-catalyzed regioselective "ligation" of azides and terminal alkynes.
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Click Chemistry: Diverse Chemical Function from a Few Good Reactions.
TL;DR: In this paper, a set of powerful, highly reliable, and selective reactions for the rapid synthesis of useful new compounds and combinatorial libraries through heteroatom links (C-X-C), an approach called click chemistry is defined, enabled, and constrained by a handful of nearly perfect "springloaded" reactions.
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Peptidotriazoles on solid phase: [1,2,3]-triazoles by regiospecific copper(i)-catalyzed 1,3-dipolar cycloadditions of terminal alkynes to azides.
TL;DR: A novel regiospecific copper(I)-catalyzed 1,3-dipolar cycloaddition of terminal alkynes to azides on solid-phase is reported, and the X-ray structure of 2-azido-2-methylpropanoic acid has been solved, to yield structural information on the 1, 3-dipoles entering the reaction.
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Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics.
Shao En Ong,Blagoy Blagoev,Irina Kratchmarova,Dan B. Kristensen,Hanno Steen,Akhilesh Pandey,Matthias Mann +6 more
TL;DR: SILAC is a simple, inexpensive, and accurate procedure that can be used as a quantitative proteomic approach in any cell culture system and is applied to the relative quantitation of changes in protein expression during the process of muscle cell differentiation.
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Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
TL;DR: An approach for the accurate quantification and concurrent sequence identification of the individual proteins within complex mixtures based on isotope-coded affinity tags and tandem mass spectrometry is described.