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(1)H, (15)N, (13)C resonance assignment of human osteopontin
Osteopontin (OPN) is a 33.7 kDa intrinsically disordered protein and a member of the SIBLING family of proteins. OPN is bearing a signal peptide for secretion into the extracellular space, where it exerts its main physiological function, the control of calcium biomineralization. It is often involved...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Netherlands
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4568010/ https://www.ncbi.nlm.nih.gov/pubmed/25616494 http://dx.doi.org/10.1007/s12104-014-9594-7 |
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author | Platzer, Gerald Żerko, Szymon Saxena, Saurabh Koźmiński, Wiktor Konrat, Robert |
author_facet | Platzer, Gerald Żerko, Szymon Saxena, Saurabh Koźmiński, Wiktor Konrat, Robert |
author_sort | Platzer, Gerald |
collection | PubMed |
description | Osteopontin (OPN) is a 33.7 kDa intrinsically disordered protein and a member of the SIBLING family of proteins. OPN is bearing a signal peptide for secretion into the extracellular space, where it exerts its main physiological function, the control of calcium biomineralization. It is often involved in tumorigenic processes influencing proliferation, migration and survival, as well as the adhesive properties of cancer cells via CD44 and integrin signaling pathways. Here we report the nearly complete NMR chemical shift assignment of recombinant human osteopontin. |
format | Online Article Text |
id | pubmed-4568010 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Springer Netherlands |
record_format | MEDLINE/PubMed |
spelling | pubmed-45680102015-09-15 (1)H, (15)N, (13)C resonance assignment of human osteopontin Platzer, Gerald Żerko, Szymon Saxena, Saurabh Koźmiński, Wiktor Konrat, Robert Biomol NMR Assign Article Osteopontin (OPN) is a 33.7 kDa intrinsically disordered protein and a member of the SIBLING family of proteins. OPN is bearing a signal peptide for secretion into the extracellular space, where it exerts its main physiological function, the control of calcium biomineralization. It is often involved in tumorigenic processes influencing proliferation, migration and survival, as well as the adhesive properties of cancer cells via CD44 and integrin signaling pathways. Here we report the nearly complete NMR chemical shift assignment of recombinant human osteopontin. Springer Netherlands 2015-01-24 2015 /pmc/articles/PMC4568010/ /pubmed/25616494 http://dx.doi.org/10.1007/s12104-014-9594-7 Text en © The Author(s) 2015 https://creativecommons.org/licenses/by/4.0/ Open AccessThis article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited. |
spellingShingle | Article Platzer, Gerald Żerko, Szymon Saxena, Saurabh Koźmiński, Wiktor Konrat, Robert (1)H, (15)N, (13)C resonance assignment of human osteopontin |
title | (1)H, (15)N, (13)C resonance assignment of human osteopontin |
title_full | (1)H, (15)N, (13)C resonance assignment of human osteopontin |
title_fullStr | (1)H, (15)N, (13)C resonance assignment of human osteopontin |
title_full_unstemmed | (1)H, (15)N, (13)C resonance assignment of human osteopontin |
title_short | (1)H, (15)N, (13)C resonance assignment of human osteopontin |
title_sort | (1)h, (15)n, (13)c resonance assignment of human osteopontin |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4568010/ https://www.ncbi.nlm.nih.gov/pubmed/25616494 http://dx.doi.org/10.1007/s12104-014-9594-7 |
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