ArticleMolecular & cellular proteomics : MCP2009
Identification of heparin-binding sites in proteins by selective labeling.
Article in Molecular & cellular proteomics : MCP, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
45 citing papers in PubMed, 78 citations in OpenAlex.
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- Chemical Modification of Glycosaminoglycan Polysaccharides.Molecules (Basel, Switzerland) · 2021Review
- Pleiotrophin interacts with glycosaminoglycans in a highly flexible and adaptable manner.FEBS letters · 2021Article
- Growth Factors VEGF-AInternational journal of molecular sciences · 2021Article
- A Systems View of the Heparan Sulfate Interactome.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2021Review
- Incorporation of FGF-2 into Pharmaceutical Grade Fucoidan/Chitosan Polyelectrolyte Multilayers.Marine drugs · 2020Article
- HS2ST1-dependent signaling pathways determine breast cancer cell viability, matrix interactions, and invasive behavior.Cancer science · 2020Article
- Construction and evaluation of an antibody phage display library targeting heparan sulfate.Glycoconjugate journal · 2020Article
- Mass Spectrometry-Based Protein Footprinting for Higher-Order Structure Analysis: Fundamentals and Applications.Chemical reviews · 2020Review
- The Challenge of Modulating Heparan Sulfate Turnover by Multitarget Heparin Derivatives.Molecules (Basel, Switzerland) · 2020Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heparan sulfate proteoglycans are key regulators of complex molecular networks due to the interaction of their sugar chains with a large number of partner proteins, which in humans number more than 200 (Ori, A., Wilkinson, M. C., and Fernig, D. G. (2008) The heparanome and regulation of cell function: structures, functions and challenges. Front. Biosci. 13, 4309-4338). We developed a method to selectively label residues involved in heparin binding that matches the requirements for medium/high throughput applications called the "Protect and Label" strategy. This is based on the protection against chemical modification given by heparin/heparan sulfate to the residues located in the heparin-binding site. Thus, analysis of fibroblast growth factor-2 bound to heparin and incubated with N-hydroxysuccinimide acetate showed that lysines involved in the sugar binding are protected against chemical modification. Moreover following release from heparin, the protected lysine side chains may be specifically labeled with N-hydroxysuccinimide biotin. After protein digestion, the biotinylated peptides were readily isolated and identified by MALDI-Q-TOF mass spectrometry. The analysis of labeled peptides obtained from three well characterized heparin-binding proteins with very different heparin-binding sites, fibroblast growth factor-2, platelet factor-4, and pleiotrophin demonstrates the success of this new approach, which thus provides a rapid and reliable procedure to identify heparin-binding sites.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.