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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...

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Autores principales: Platzer, Gerald, Żerko, Szymon, Saxena, Saurabh, Koźmiński, Wiktor, Konrat, Robert
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2015
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.
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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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