The DOI matches its Crossref record; 137 of the 137 references it cites were found in a registry or an index.
Structure and Mechanism of the Pepsin-Like Family of Aspartic Peptidases
Abstract
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTStructure and Mechanism of the Pepsin-Like Family of Aspartic PeptidasesBen M. DunnView Author Information Department of Biochemistry & Molecular Biology, University of Florida College of Medicine, Gainesville, Florida 32610-0245 Cite this: Chem. Rev. 2002, 102, 12, 4431–4458Publication Date (Web):November 9, 2002Publication History Received15 May 2002Published online9 November 2002Published inissue 1 December 2002https://pubs.acs.org/doi/10.1021/cr010167qhttps://doi.org/10.1021/cr010167qresearch-articleACS PublicationsCopyright © 2002 American Chemical SocietyRequest reuse permissionsArticle Views3921Altmetric-Citations282LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose SUBJECTS:Chemical structure,Inhibitors,Monomers,Noncovalent interactions,Peptides and proteins Get e-Alerts
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Membrane-anchored aspartyl protease with Alzheimer's disease β-secretase activity
Yan, R., Bienkowski, M. J., Shuck, M. E., Miao, H., Tory, M. C., Pauley, A. M., Brashler, J. R., Stratman, N. C., Mathews, W. R., Buhl, A. E., et al. (1999) · Nature · doi:10.1038/990107 · Cited by 1,438
The Handbook of proteolytic enzymes
Barrett, A. J., Rawlings, N. D., & Woessner, J. F. (1998) · Cited by 1,119
Identification of a Novel Aspartic Protease (Asp 2) as β-Secretase
Hussain, I., Powell, D., Howlett, D. R., Tew, D. G., Meek, T. D., Chapman, C., Gloger, I. S., Murphy, K. E., Southan, C. D., Ryan, D. M., et al. (1999) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.1999.0811 · Cited by 1,080
HEMOGLOBIN METABOLISM IN THE MALARIA PARASITE PLASMODIUM FALCIPARUM
Francis, S. E., Sullivan, D. J., & Goldberg, A. D. E. (1997) · Annual Review of Microbiology · doi:10.1146/annurev.micro.51.1.97 · Cited by 782
Human aspartic protease memapsin 2 cleaves the β-secretase site of β-amyloid precursor protein
Lin, X., Koelsch, G., Wu, S., Downs, D., Dashti, A., & Tang, J. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.4.1456 · Cited by 776
Structure of the Protease Domain of Memapsin 2 (β-Secretase) Complexed with Inhibitor
Hong, L., Koelsch, G., Lin, X., Wu, S., Terzyan, S., Ghosh, A. K., Zhang, X. C., & Tang, J. (2000) · Science · doi:10.1126/science.290.5489.150 · Cited by 711
Cited by
Chemistry and Biology Of Multicomponent Reactions
Dömling, A., Wang, W., & Wang, K. (2012) · Chemical Reviews · doi:10.1021/cr100233r · Cited by 2,547
Structure and function of plant aspartic proteinases
Simões, I., & Faro, C. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04136.x · Cited by 298
Purification of cynarases from artichoke (Cynara scolymus L.): enzymatic properties of cynarase A
Sidrach, L., García-Cánovas, F., Tudela, J., & Neptuno Rodríguez-López, J. (2005) · Phytochemistry · doi:10.1016/j.phytochem.2004.10.005 · Cited by 74
Digestion of food proteins: the role of pepsin
Yang, M., Yang, Z., Everett, D. W., Gilbert, E. P., Singh, H., & Ye, A. (2025) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2025.2453096 · Cited by 65
“…broad specificity for hydrolyzing bonds adjacent to aromatic and hydrophobic amino acids, such as phenylalanine, tyrosine, tryptophan, and leucine (Dunn 2002; Inouye and Fruton 1967), with an optimum pH of approximately 2.0 (Kondjoyan, Daudin, and Santé-Lhoutellier 2015; Pletschke, Naudé, and…”
InfluentialRaposo, S., & Domingos, A. (2008) · Process Biochemistry · doi:10.1016/j.procbio.2007.11.003 · Cited by 64
Metadata
- Authors
- Dunn, B. M.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2002-11-09
- Volume
- 102
- Issue
- 12
- Pages
- 4431-4458
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W1992636402
- Cited by
- 372
- References
- 137
- FWCI
- 0.22
- Type
- journal article
- Language
- en
- Open access
- closed
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