Conversion of human 5‐lipoxygenase to a 15‐lipoxygenase by a point mutation to mimic phosphorylation at Serine‐663-Reference-Cited by-同舟云学术

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Conversion of human 5‐lipoxygenase to a 15‐lipoxygenase by a point mutation to mimic phosphorylation at Serine‐663

Published:2012-04-18 Issue:8 Volume:26 Page:3222-3229
ISSN:0892-6638
Container-title:The FASEB Journal
language:en
Short-container-title:FASEB j.

Author:

Gilbert Nathaniel C.¹,Rui Zhe¹,Neau David B.²,Waight Maria T.¹,Bartlett Sue G.¹,Boeglin William E.³⁴,Brash Alan R.³⁴,Newcomer Marcia E.¹

Affiliation:

1. Department of Biological Sciences Louisiana State University Baton Rouge Louisiana USA

2. Northeastern Collaborative Access Team Argonne National Laboratory Argonne Illinois USA

3. Department of Pharmacology Vanderbilt University Nashville Tennessee

4. Vanderbilt Institute for Chemical Biology Vanderbilt University Nashville Tennessee

Funder

American Heart Association

National Science Foundation

National Institutes of Health

National Center for Research Resources

National Institute of General Medical Sciences

U.S. Department of Energy

Publisher

Wiley

Subject

Genetics,Molecular Biology,Biochemistry,Biotechnology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1096/fj.12-205286

Reference43 articles.

1. What's all the FLAP about?: 5-lipoxygenase-activating protein inhibitors for inflammatory diseases

2. Requirement of a 5-lipoxygenase-activating protein for leukotriene synthesis

3. 5-Lipoxygenase: mechanisms of regulation

4. Enzyme with dual lipoxygenase activities catalyzes leukotriene A4 synthesis from arachidonic acid.

5. Lipoxins: novel series of biologically active compounds formed from arachidonic acid in human leukocytes.

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