Protein Phosphorylation in Health and Disease

Protein phosphorylation is one of the most abundant reversible post-translational modifications in eukaryotes. It is involved in virtually all cellular processes by regulating protein function, localization and stability and by mediating protein-protein interactions. Furthermore, aberrant protein ph...

Full description

Autores:
Tipo de recurso:
Book
Fecha de publicación:
2016
Institución:
Universidad de Bogotá Jorge Tadeo Lozano
Repositorio:
Expeditio: repositorio UTadeo
Idioma:
eng
OAI Identifier:
oai:expeditiorepositorio.utadeo.edu.co:20.500.12010/14184
Acceso en línea:
https://www.frontiersin.org/research-topics/1984/protein-phosphorylation-in-health-and-disease#nogo
http://hdl.handle.net/20.500.12010/14184
Palabra clave:
Science (General)
Genetics
Evolution
Protein phosphorylation
Systems Biology
Bioinformatics
Network biology
Human Disease
Kinases
Phosphatases
Protein structure
Rights
License
Abierto (Texto Completo)
id UTADEO2_123f64e4845c2dd500f71f74ff751065
oai_identifier_str oai:expeditiorepositorio.utadeo.edu.co:20.500.12010/14184
network_acronym_str UTADEO2
network_name_str Expeditio: repositorio UTadeo
repository_id_str
dc.title.spa.fl_str_mv Protein Phosphorylation in Health and Disease
title Protein Phosphorylation in Health and Disease
spellingShingle Protein Phosphorylation in Health and Disease
Science (General)
Genetics
Evolution
Protein phosphorylation
Systems Biology
Bioinformatics
Network biology
Human Disease
Kinases
Phosphatases
Protein structure
title_short Protein Phosphorylation in Health and Disease
title_full Protein Phosphorylation in Health and Disease
title_fullStr Protein Phosphorylation in Health and Disease
title_full_unstemmed Protein Phosphorylation in Health and Disease
title_sort Protein Phosphorylation in Health and Disease
dc.subject.spa.fl_str_mv Science (General)
Genetics
Evolution
topic Science (General)
Genetics
Evolution
Protein phosphorylation
Systems Biology
Bioinformatics
Network biology
Human Disease
Kinases
Phosphatases
Protein structure
dc.subject.lemb.spa.fl_str_mv Protein phosphorylation
Systems Biology
Bioinformatics
Network biology
dc.subject.keyword.spa.fl_str_mv Human Disease
Kinases
Phosphatases
Protein structure
description Protein phosphorylation is one of the most abundant reversible post-translational modifications in eukaryotes. It is involved in virtually all cellular processes by regulating protein function, localization and stability and by mediating protein-protein interactions. Furthermore, aberrant protein phosphorylation is implicated in the onset and progression of human diseases such as cancer and neurodegenerative disorders. In the last years, tens of thousands of in vivo phosphorylation events have been identified by large-scale quantitative phospho-proteomics experiment suggesting that a large fraction of the proteome might be regulated by phosphorylation. This data explosion is increasingly enabling the development of computational approaches, often combined with experimental validation, aiming at prioritizing phosphosites and assessing their functional relevance. Some computational approaches also address the inference of specificity determinants of protein kinases/phosphatases and the identification of phosphoresidue recognition domains. In this context, several challenging issues are still open regarding phosphorylation, including a better understanding of the interplay between phosphorylation and allosteric regulation, agents and mechanisms disrupting or promoting abnormal phosphorylation in diseases, the identification and modulation of novel phosphorylation inhibitors, and so forth. Furthermore, the determinants of kinase and phosphatase recognition and binding specificity are still unknown in several cases, as well as the impact of disease mutations on phosphorylation-mediated signaling. The articles included in this Research Topic illustrate the very diverse aspects of phosphorylation, ranging from structural changes induced by phosphorylation to the peculiarities of phosphosite evolution. Some also provide a glimpse into the huge complexity of phosphorylation networks and pathways in health and disease, and underscore that a deeper knowledge of such processes is essential to identify disease biomarkers, on one hand, and design more effective therapeutic strategies, on the other.
publishDate 2016
dc.date.created.none.fl_str_mv 2016-01-19
dc.date.accessioned.none.fl_str_mv 2020-10-03T23:46:09Z
dc.date.available.none.fl_str_mv 2020-10-03T23:46:09Z
dc.type.local.spa.fl_str_mv Libro
dc.type.coar.spa.fl_str_mv http://purl.org/coar/resource_type/c_2f33
format http://purl.org/coar/resource_type/c_2f33
dc.identifier.isbn.none.fl_str_mv 978-2-88919-900-6
dc.identifier.issn.none.fl_str_mv 1664-8714
dc.identifier.other.none.fl_str_mv https://www.frontiersin.org/research-topics/1984/protein-phosphorylation-in-health-and-disease#nogo
dc.identifier.uri.none.fl_str_mv http://hdl.handle.net/20.500.12010/14184
dc.identifier.doi.none.fl_str_mv 10.3389/978-2-88919-900-6
identifier_str_mv 978-2-88919-900-6
1664-8714
10.3389/978-2-88919-900-6
url https://www.frontiersin.org/research-topics/1984/protein-phosphorylation-in-health-and-disease#nogo
http://hdl.handle.net/20.500.12010/14184
dc.language.iso.spa.fl_str_mv eng
language eng
dc.rights.coar.fl_str_mv http://purl.org/coar/access_right/c_abf2
dc.rights.local.spa.fl_str_mv Abierto (Texto Completo)
dc.rights.creativecommons.none.fl_str_mv https://creativecommons.org/licenses/by/4.0/
rights_invalid_str_mv Abierto (Texto Completo)
https://creativecommons.org/licenses/by/4.0/
http://purl.org/coar/access_right/c_abf2
dc.format.extent.spa.fl_str_mv 124 páginas
dc.format.mimetype.spa.fl_str_mv application/pdf
dc.publisher.spa.fl_str_mv Frontiers Media SA
institution Universidad de Bogotá Jorge Tadeo Lozano
bitstream.url.fl_str_mv https://expeditiorepositorio.utadeo.edu.co/bitstream/20.500.12010/14184/1/PROTEIN%20PHOSPHORYLATION%20IN.PDF
https://expeditiorepositorio.utadeo.edu.co/bitstream/20.500.12010/14184/2/license.txt
https://expeditiorepositorio.utadeo.edu.co/bitstream/20.500.12010/14184/3/PROTEIN%20PHOSPHORYLATION%20IN.PDF.jpg
bitstream.checksum.fl_str_mv f51d60a9d1c6409ef4ae5b1e6a70e6de
abceeb1c943c50d3343516f9dbfc110f
a1dbe36e1585b98befadaf8ce61d4cf0
bitstream.checksumAlgorithm.fl_str_mv MD5
MD5
MD5
repository.name.fl_str_mv Repositorio Institucional - Universidad Jorge Tadeo Lozano
repository.mail.fl_str_mv expeditio@utadeo.edu.co
_version_ 1818152978049138688
spelling 2020-10-03T23:46:09Z2020-10-03T23:46:09Z2016-01-19978-2-88919-900-61664-8714https://www.frontiersin.org/research-topics/1984/protein-phosphorylation-in-health-and-disease#nogohttp://hdl.handle.net/20.500.12010/1418410.3389/978-2-88919-900-6124 páginasapplication/pdfengFrontiers Media SAScience (General)GeneticsEvolutionProtein phosphorylationSystems BiologyBioinformaticsNetwork biologyHuman DiseaseKinasesPhosphatasesProtein structureProtein Phosphorylation in Health and DiseaseLibrohttp://purl.org/coar/resource_type/c_2f33Abierto (Texto Completo)https://creativecommons.org/licenses/by/4.0/http://purl.org/coar/access_right/c_abf2Protein phosphorylation is one of the most abundant reversible post-translational modifications in eukaryotes. It is involved in virtually all cellular processes by regulating protein function, localization and stability and by mediating protein-protein interactions. Furthermore, aberrant protein phosphorylation is implicated in the onset and progression of human diseases such as cancer and neurodegenerative disorders. In the last years, tens of thousands of in vivo phosphorylation events have been identified by large-scale quantitative phospho-proteomics experiment suggesting that a large fraction of the proteome might be regulated by phosphorylation. This data explosion is increasingly enabling the development of computational approaches, often combined with experimental validation, aiming at prioritizing phosphosites and assessing their functional relevance. Some computational approaches also address the inference of specificity determinants of protein kinases/phosphatases and the identification of phosphoresidue recognition domains. In this context, several challenging issues are still open regarding phosphorylation, including a better understanding of the interplay between phosphorylation and allosteric regulation, agents and mechanisms disrupting or promoting abnormal phosphorylation in diseases, the identification and modulation of novel phosphorylation inhibitors, and so forth. Furthermore, the determinants of kinase and phosphatase recognition and binding specificity are still unknown in several cases, as well as the impact of disease mutations on phosphorylation-mediated signaling. The articles included in this Research Topic illustrate the very diverse aspects of phosphorylation, ranging from structural changes induced by phosphorylation to the peculiarities of phosphosite evolution. Some also provide a glimpse into the huge complexity of phosphorylation networks and pathways in health and disease, and underscore that a deeper knowledge of such processes is essential to identify disease biomarkers, on one hand, and design more effective therapeutic strategies, on the other.Allegra, ViaZanzoni, AndreasORIGINALPROTEIN PHOSPHORYLATION IN.PDFPROTEIN PHOSPHORYLATION IN.PDFVer documentoapplication/pdf14576646https://expeditiorepositorio.utadeo.edu.co/bitstream/20.500.12010/14184/1/PROTEIN%20PHOSPHORYLATION%20IN.PDFf51d60a9d1c6409ef4ae5b1e6a70e6deMD51open accessLICENSElicense.txtlicense.txttext/plain; charset=utf-82938https://expeditiorepositorio.utadeo.edu.co/bitstream/20.500.12010/14184/2/license.txtabceeb1c943c50d3343516f9dbfc110fMD52open accessTHUMBNAILPROTEIN PHOSPHORYLATION IN.PDF.jpgPROTEIN PHOSPHORYLATION IN.PDF.jpgIM Thumbnailimage/jpeg17465https://expeditiorepositorio.utadeo.edu.co/bitstream/20.500.12010/14184/3/PROTEIN%20PHOSPHORYLATION%20IN.PDF.jpga1dbe36e1585b98befadaf8ce61d4cf0MD53open access20.500.12010/14184oai:expeditiorepositorio.utadeo.edu.co:20.500.12010/141842021-02-23 16:28:22.696open accessRepositorio Institucional - Universidad Jorge Tadeo Lozanoexpeditio@utadeo.edu.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