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(2S,3S)-Oxirane-2,3-dicarboxylic acid: A privileged platform for probing human cysteine cathepsins

Paper ID Volume ID Publish Year Pages File Format Full-Text
25468 43575 2007 8 PDF Available
Title
(2S,3S)-Oxirane-2,3-dicarboxylic acid: A privileged platform for probing human cysteine cathepsins
Abstract

The notion that human cysteine cathepsins contribute only to general protein turnover within the lysosomes has changed in the last decade in a substantial manner. A continuously growing number of data accumulated in different fields of life sciences revealed that these enzymes are involved in a variety of pivotal physiological processes. To investigate these particular fraction of proteolytical activity of the human degradome even in a complex cellular environment, chemical probes that covalently label the corresponding proteases proved to be versatile tools. (2S,3S)-Oxirane-2,3-dicarboxylic acid provides an ideal platform for the design of such probing systems. Depending on the complexity of the attached recognition elements, either the activity of the entire group of human cysteine cathepsins or individual members can be detected.

Keywords
Cysteine protease; Degradome; Cathepsin B; Activity-based probing
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(2S,3S)-Oxirane-2,3-dicarboxylic acid: A privileged platform for probing human cysteine cathepsins
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 129, Issue 2, 30 April 2007, Pages 308–315
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
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Full-text PDF Download
Online Support
Any Questions? feel free to contact us