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Cited by 1,203

The DOI matches its Crossref record; 530 of the 530 references it cites were found in a registry or an index.

Phospholipase A2Enzymes: Physical Structure, Biological Function, Disease Implication, Chemical Inhibition, and Therapeutic Intervention

Open access
Dennis, Edward A., Cao, Jian, Hsu, Yuan-Hao, Magrioti, Victoria, Kokotos, George·2011·Chemical Reviews
DOI 10.1021/cr200085w
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Abstract

Phospholipases represent one of the earliest enzyme activities to be identified and studied, and the phospholipase A2 superfamily traces its roots to the identification of lytic actions of snake venom at the end of the 19th century. Both electrostatic and hydrophobic interactions contribute to the interfacial binding of sPLA2 to anionic phospholipid membranes. The interaction between basic residues on the binding surface with anionic vesicles plays an important role in interfacial binding. The major functions will be summarized below and include the ability to kill Gram-positive and Gram-negative bacteria, thereby affecting host defense against bacterial infections. sPLA2 may be involved in the pathogensis of inflammatory bowel disease including Crohn's disease and ulcerative colitis. GIIA sPLA2 protein and mRNA were detected in Paneth cells of the small intestinal mucosa in the intestine in Crohn's disease patients.

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Metadata

Authors
Dennis, E. A., Cao, J., Hsu, Y.-H., Magrioti, V., & Kokotos, G.
Venue
Chemical Reviews
Publisher
American Chemical Society (ACS)
Published
2011-09-12
Volume
111
Issue
10
Pages
6130-6185
ISSN
  • 0009-2665 (ISSN-L)
  • 1520-6890
DOI
10.1021/cr200085w
OpenAlex
W2077755739
Cited by
1,203
References
530
FWCI
4.75
Type
journal article
Language
en
Open access
green

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.