The Serpin MNEI Inhibits Elastase-like and Chymotrypsin-like Serine Proteases through Efficient Reactions at Two Active Sites-Reference-Cited by-同舟云学术

The Serpin MNEI Inhibits Elastase-like and Chymotrypsin-like Serine Proteases through Efficient Reactions at Two Active Sites

Published:2001-11-30 Issue:51 Volume:40 Page:15762-15770
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Cooley Jessica¹,Takayama Thomas K.¹,Shapiro Steven D.¹,Schechter Norman M.¹,Remold-O'Donnell Eileen¹

Affiliation:

1. Center for Blood Research, 800 Huntington Avenue, Boston, Massachusetts 02115, Departments of Biochemistry and Urology, University of Washington, Seattle, Washington 98195, Department of Pulmonary and Critical Care Medicine, Brigham and Women's Hospital, Boston, Massachusetts 02115, Department of Dermatology, University of Pennsylvania, Philadelphia, Pennsylvania 19104, and Department of Pediatrics, Harvard Medical School, Boston, Massachusetts 02115

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi0113925

Reference76 articles.

1. Elastase inhibitor. Characterization of the human elastase inhibitor molecule associated with monocytes, macrophages, and neutrophils.

2. Carbohydrate structures of glycoproteins and glycolipids as differentiation antigens, tumour-associated antigens and components of receptor systems

3. Human α1-proteinase inhibitor

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