Structure–activity relationship, kinetic mechanism, and selectivity for a new class of ubiquitin C-terminal hydrolase-L1 (UCH-L1) inhibitors-Reference-Cited by-同舟云学术

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Structure–activity relationship, kinetic mechanism, and selectivity for a new class of ubiquitin C-terminal hydrolase-L1 (UCH-L1) inhibitors

Published:2007-07 Issue:13 Volume:17 Page:3729-3732
ISSN:0960-894X
Container-title:Bioorganic & Medicinal Chemistry Letters
language:en
Short-container-title:Bioorganic & Medicinal Chemistry Letters

Author:

Mermerian Ara H.,Case April,Stein Ross L.,Cuny Gregory D.

Publisher

Elsevier BV

Subject

Organic Chemistry,Clinical Biochemistry,Drug Discovery,Pharmaceutical Science,Molecular Biology,Molecular Medicine,Biochemistry

Reference16 articles.

1. Ubiquitination and deubiquitination: Targeting of proteins for degradation by the proteasome

2. Deubiquitinating Enzymes as Cellular Regulators

3. Deubiquitinating enzymes—the importance of driving in reverse along the ubiquitin–proteasome pathway

4. Mechanism and function of deubiquitinating enzymes

5. Kinetic studies of isopeptidase T: modulation of peptidase activity by ubiquitin

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