Flexibility of the Thrombin-activatable Fibrinolysis Inhibitor Pro-domain Enables Productive Binding of Protein Substrates-Reference-Cited by-同舟云学术

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Flexibility of the Thrombin-activatable Fibrinolysis Inhibitor Pro-domain Enables Productive Binding of Protein Substrates

Published:2010-12 Issue:49 Volume:285 Page:38243-38250
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Valnickova Zuzana,Sanglas Laura,Arolas Joan L.,Petersen Steen V.,Schar Christine,Otzen Daniel,Aviles Francesc X.,Gomis-Rüth F. Xavier,Enghild Jan J.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference71 articles.

1. MEROPS: the peptidase database

2. Structure and Mechanism of Metallocarboxypeptidases

3. Metallocarboxypeptidases: Emerging Drug Targets in Biomedicine

4. Skidgel, R. A., Erdös, E. G. (2004), pp. 837–840, Academic Press, London.

5. Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma.

Cited by 8 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Structure of Aedes aegypti procarboxypeptidase B1 and its binding with Dengue virus for controlling infection;Life Science Alliance;2021-11-08

2. Structure of Aedes aegypti carboxypeptidase B1 ‐inhibitor complex uncover the disparity between mosquito and non‐mosquito insect carboxypeptidase inhibition mechanism;Protein Science;2021-11-05

3. Thrombin Activatable Fibrinolysis Inhibitor (TAFI): An Updated Narrative Review;International Journal of Molecular Sciences;2021-04-01

4. Structure-function relationships in thrombin-activatable fibrinolysis inhibitor;Journal of Thrombosis and Haemostasis;2016-03-30

5. Metallocarboxypeptidases and their Inhibitors: Recent Developments in Biomedically Relevant Protein and Organic Ligands;Current Medicinal Chemistry;2013-03-01

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