Mass spectrometry for monitoring protease reactions

Standard

Mass spectrometry for monitoring protease reactions. / Schlüter, H; Hildebrand, D; Gallin, C; Schulz, A; Thiemann, J; Trusch, M.

In: ANAL BIOANAL CHEM, Vol. 392, No. 5, 5, 11.2008, p. 783-792.

Research output: SCORING: Contribution to journalSCORING: Review articleResearch

Harvard

Schlüter, H, Hildebrand, D, Gallin, C, Schulz, A, Thiemann, J & Trusch, M 2008, 'Mass spectrometry for monitoring protease reactions', ANAL BIOANAL CHEM, vol. 392, no. 5, 5, pp. 783-792. https://doi.org/10.1007/s00216-008-2213-7

APA

Schlüter, H., Hildebrand, D., Gallin, C., Schulz, A., Thiemann, J., & Trusch, M. (2008). Mass spectrometry for monitoring protease reactions. ANAL BIOANAL CHEM, 392(5), 783-792. [5]. https://doi.org/10.1007/s00216-008-2213-7

Vancouver

Schlüter H, Hildebrand D, Gallin C, Schulz A, Thiemann J, Trusch M. Mass spectrometry for monitoring protease reactions. ANAL BIOANAL CHEM. 2008 Nov;392(5):783-792. 5. https://doi.org/10.1007/s00216-008-2213-7

Bibtex

@article{209f12fc55c7450cb3a42d117ba23aa0,
title = "Mass spectrometry for monitoring protease reactions",
abstract = "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.",
keywords = "Angiotensin II, Animals, Base Sequence, Combinatorial Chemistry Techniques, Genome, Human, Humans, Mass Spectrometry, Peptide Hydrolases, Journal Article, Research Support, Non-U.S. Gov't, Review",
author = "H Schl{\"u}ter and D Hildebrand and C Gallin and A Schulz and J Thiemann and M Trusch",
year = "2008",
month = nov,
doi = "10.1007/s00216-008-2213-7",
language = "English",
volume = "392",
pages = "783--792",
journal = "ANAL BIOANAL CHEM",
issn = "1618-2642",
publisher = "Springer",
number = "5",

}

RIS

TY - JOUR

T1 - Mass spectrometry for monitoring protease reactions

AU - Schlüter, H

AU - Hildebrand, D

AU - Gallin, C

AU - Schulz, A

AU - Thiemann, J

AU - Trusch, M

PY - 2008/11

Y1 - 2008/11

N2 - 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.

AB - 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.

KW - Angiotensin II

KW - Animals

KW - Base Sequence

KW - Combinatorial Chemistry Techniques

KW - Genome, Human

KW - Humans

KW - Mass Spectrometry

KW - Peptide Hydrolases

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

KW - Review

U2 - 10.1007/s00216-008-2213-7

DO - 10.1007/s00216-008-2213-7

M3 - SCORING: Review article

C2 - 18584157

VL - 392

SP - 783

EP - 792

JO - ANAL BIOANAL CHEM

JF - ANAL BIOANAL CHEM

SN - 1618-2642

IS - 5

M1 - 5

ER -