PuSH - Publication Server of Helmholtz Zentrum München: Esterase activity of carbonic anhydrases serves as surrogate for selecting antibodies blocking hydratase activity.

Information

Clues to quality of journals

Open Access Policy of Helmholtz Association 2016

CC Licencences

Publication Metrics

Navigation

Home

Deutsch

Research

Advanced Search

Browse by ...

... HMGU-Authors/Consortia

... Organizational Structure

... Journal

... Publication Type

... Research Data

... Arbeitsgruppen

... Publication Year

Publication overview

Statistics

Statistics (last 5 years)

OA Publications

Publish

Submit Publication

Import publication from...

...EVA

Report missing publication

Highlights

Support & Contact

Contact persons

Help

Data protection

Helmholtz Open Science

JANE Journal Estimator

SHERPA/RoMEO

DOAJ

Export:

Text

Endnote (RIS) BIB

BibTeX

Uda, N.R.* ; Seibert, V.* ; Stenner-Liewen, F.* ; Müller, P.* ; Herzig, P.* ; Gondi, G.* ; Zeidler, R. ; van Dijk, M.* ; Zippelius, A.* ; Renner, C.*

Esterase activity of carbonic anhydrases serves as surrogate for selecting antibodies blocking hydratase activity.

J. Enzyme Inhib. Med. Chem. 30, 955-960 (2015)

DOI

PMC

Open Access Gold as soon as Publ. Version/Full Text is submitted to ZB.

Abstract
Metrics
Extra information

Carbonic anhydrase 9 (CA9) and carbonic anhydrase 12 (CA12) were proposed as potential targets for cancer therapy more than 20 years ago. However, to date, there are only very few antibodies that have been described to specifically target CA9 and CA12 and also block the enzymatic activity of their targets. One of the early stage bottlenecks in identifying CA9- and CA12-inhibiting antibodies has been the lack of a high-throughput screening system that would allow for rapid assessment of inhibition of the targeted carbon dioxide hydratase activity of carbonic anhydrases. In this study, we show that measuring the esterase activity of carbonic anhydrase offers a robust and inexpensive screening method for identifying antibody candidates that block both hydratase and esterase activities of carbonic anhydrase's. To our knowledge, this is the first implementation of a facile surrogate-screening assay to identify potential therapeutic antibodies that block the clinically relevant hydratase activity of carbonic anhydrases.

Impact Factor

Scopus SNIP

Web of Science
Times Cited

Scopus
Cited By

Altmetric

2.332

0.686