Mass spectrometry for monitoring protease reactions

More than 560 genes are annotated as proteases in the human genome. About half of the genes are not or are only marginally characterized. Over the past decade, mass spectrometry has become the basis for proteomics, especially for protein identification, performed in a high-throughput manner. This de...

Descripción completa

Detalles Bibliográficos
Autores principales: Schlüter, H., Hildebrand, D., Gallin, C., Schulz, A., Thiemann, J., Trusch, M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer-Verlag 2008
Materias:
Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7080141/
https://www.ncbi.nlm.nih.gov/pubmed/18584157
http://dx.doi.org/10.1007/s00216-008-2213-7
_version_ 1783507968434634752
author Schlüter, H.
Hildebrand, D.
Gallin, C.
Schulz, A.
Thiemann, J.
Trusch, M.
author_facet Schlüter, H.
Hildebrand, D.
Gallin, C.
Schulz, A.
Thiemann, J.
Trusch, M.
author_sort Schlüter, H.
collection PubMed
description More than 560 genes are annotated as proteases in the human genome. About half of the genes are not or are only marginally characterized. Over the past decade, mass spectrometry has become the basis for proteomics, especially for protein identification, performed in a high-throughput manner. This development was also very fruitful for exploring the complex systems associated with protease functions, as briefly reviewed here. Mass spectrometry is an ideal tool for monitoring protease reactions, as will be highlighted in this review.
format Online
Article
Text
id pubmed-7080141
institution National Center for Biotechnology Information
language English
publishDate 2008
publisher Springer-Verlag
record_format MEDLINE/PubMed
spelling pubmed-70801412020-03-23 Mass spectrometry for monitoring protease reactions Schlüter, H. Hildebrand, D. Gallin, C. Schulz, A. Thiemann, J. Trusch, M. Anal Bioanal Chem Review More than 560 genes are annotated as proteases in the human genome. About half of the genes are not or are only marginally characterized. Over the past decade, mass spectrometry has become the basis for proteomics, especially for protein identification, performed in a high-throughput manner. This development was also very fruitful for exploring the complex systems associated with protease functions, as briefly reviewed here. Mass spectrometry is an ideal tool for monitoring protease reactions, as will be highlighted in this review. Springer-Verlag 2008-06-27 2008 /pmc/articles/PMC7080141/ /pubmed/18584157 http://dx.doi.org/10.1007/s00216-008-2213-7 Text en © Springer-Verlag 2008 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.
spellingShingle Review
Schlüter, H.
Hildebrand, D.
Gallin, C.
Schulz, A.
Thiemann, J.
Trusch, M.
Mass spectrometry for monitoring protease reactions
title Mass spectrometry for monitoring protease reactions
title_full Mass spectrometry for monitoring protease reactions
title_fullStr Mass spectrometry for monitoring protease reactions
title_full_unstemmed Mass spectrometry for monitoring protease reactions
title_short Mass spectrometry for monitoring protease reactions
title_sort mass spectrometry for monitoring protease reactions
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7080141/
https://www.ncbi.nlm.nih.gov/pubmed/18584157
http://dx.doi.org/10.1007/s00216-008-2213-7
work_keys_str_mv AT schluterh massspectrometryformonitoringproteasereactions
AT hildebrandd massspectrometryformonitoringproteasereactions
AT gallinc massspectrometryformonitoringproteasereactions
AT schulza massspectrometryformonitoringproteasereactions
AT thiemannj massspectrometryformonitoringproteasereactions
AT truschm massspectrometryformonitoringproteasereactions

Ejemplares similares