The DOI matches its Crossref record; 52 of the 52 references it cites were found in a registry or an index.
Human leukocyte and porcine pancreatic elastase: x-ray crystal structures, mechanism, substrate specificity, and mechanism-based inhibitors
Abstract
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTHuman leukocyte and porcine pancreatic elastase: x-ray crystal structures, mechanism, substrate specificity, and mechanism-based inhibitorsWolfram Bode, Edgar Meyer, Jr., and James C. PowersCite this: Biochemistry 1989, 28, 5, 1951–1963Publication Date (Print):March 7, 1989Publication History Published online1 May 2002Published inissue 7 March 1989https://pubs.acs.org/doi/10.1021/bi00431a001https://doi.org/10.1021/bi00431a001research-articleACS PublicationsRequest reuse permissionsArticle Views1200Altmetric-Citations302LEARN 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 Get e-Alerts
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Citations
Cites
On the size of the active site in proteases. I. Papain
Schechter, I., & Berger, A. (1967) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(67)80055-x · Cited by 5,204
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HUMAN PLASMA PROTEINASE INHIBITORS
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Structural basis of the activation and action of trypsin
Huber, R., & Bode, W. (1978) · Accounts of Chemical Research · doi:10.1021/ar50123a006 · Cited by 677
Self-citationStructure of crystalline α-chymotrypsin
Birktoft, J. J., & Blow, D. M. (1972) · Journal of Molecular Biology · doi:10.1016/0022-2836(72)90210-0 · Cited by 671
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Self-citationMarquart, M., Walter, J., Deisenhofer, J., Bode, W., & Huber, R. (1983) · Acta Crystallographica Section B Structural Science · doi:10.1107/s010876818300275x · Cited by 575
Self-citationHuman leukocyte granule elastase: rapid isolation and characterization
Baugh, R. J., & Travis, J. (1976) · Biochemistry · doi:10.1021/bi00649a017 · Cited by 539
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Cited by
Irreversible Inhibitors of Serine, Cysteine, and Threonine Proteases
Powers, J. C., Asgian, J. L., Ekici, Ö. D., & James, K. E. (2002) · Chemical Reviews · doi:10.1021/cr010182v · Cited by 1,090
Self-citationThe structural aspects of limited proteolysis of native proteins
Hubbard, S. J. (1998) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(97)00175-1 · Cited by 406
Structure of a Legume Lectin with an Ordered N-Linked Carbohydrate in Complex with Lactose
Shaanan, B., Lis, H., & Sharon, N. (1991) · Science · doi:10.1126/science.1948067 · Cited by 261
López-Boado, Y. S., Espinola, M., Bahr, S., & Belaaouaj, A. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.1.509 · Cited by 92
Metadata
- Authors
- Bode, W., Meyer, E., & Powers, J. C.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1989-03-07
- Volume
- 28
- Issue
- 5
- Pages
- 1951-1963
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W1995609060
- Cited by
- 397
- References
- 52
- FWCI
- 11.65
- Type
- journal article
- Language
- en
- Open access
- closed
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- Bode, W., Meyer, E., & Powers, J. C. (1989). Human leukocyte and porcine pancreatic elastase: x-ray crystal structures, mechanism, substrate specificity, and mechanism-based inhibitors. Biochemistry. https://doi.org/10.1021/bi00431a001
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