| Chapter title |
Protein Tyrosine Phosphatases
|
|---|---|
| Chapter number | 15 |
| Book title |
Protein Tyrosine Phosphatases
|
| Published in |
Methods in molecular biology, January 2016
|
| DOI | 10.1007/978-1-4939-3746-2_15 |
| Pubmed ID | |
| Book ISBNs |
978-1-4939-3744-8, 978-1-4939-3746-2
|
| Authors |
Stoker, Andrew William, Andrew William Stoker |
| Abstract |
Receptor protein tyrosine phosphatases (RPTPs) form a group of over 20 enzymes in vertebrates, each with unique ectodomains subject to potential extracellular interactions with ligands. It has recently become clear that a remarkably diverse range of ligands exist, including homophilic binders, adhesion molecules, neurotrophin receptors, and proteoglycans. Individual RPTPs can bind several ligands, and vice versa, suggesting that complex cell signaling networks exist. The identification of RPTP ligands and where they are located in tissues remains a challenge for a large number of these enzymes. Here we describe some powerful methods that have proved successful for several research groups, leading to our improved understanding of RPTP-ligand interactions and functional regulation. |
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| Unknown | 1 | 100% |
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| Members of the public | 1 | 100% |
Mendeley readers
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|---|---|---|
| Unknown | 2 | 100% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Ph. D. Student | 1 | 50% |
| Unknown | 1 | 50% |
| Readers by discipline | Count | As % |
|---|---|---|
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| Unknown | 1 | 50% |