Structure and Function of C1-Inhibitor
Immunology and Allergy Clinics of North America, ISSN: 0889-8561, Vol: 26, Issue: 4, Page: 615-632
2006
- 63Citations
- 53Captures
Metric Options: Counts1 Year3 YearSelecting the 1-year or 3-year option will change the metrics count to percentiles, illustrating how an article or review compares to other articles or reviews within the selected time period in the same journal. Selecting the 1-year option compares the metrics against other articles/reviews that were also published in the same calendar year. Selecting the 3-year option compares the metrics against other articles/reviews that were also published in the same calendar year plus the two years prior.
Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations63
- Citation Indexes63
- 63
- CrossRef52
- Captures53
- Readers53
- 50
Review Description
C1-INH belongs to the family of serpins. Structural studies have yielded a clear understanding of the biochemical principle underlying the functional activities of these proteins. Although the crystal structure of C1-INH has yet to be revealed, homology modeling has provided a three-dimensional model of the serpin part of C1-INH. This model has helped us understand the biochemical consequences of mutations of the C1-INH gene as they occur in patients who have HAE. The structure of the N-terminal domain of C1-INH remains unknown; however, this part of the molecule is unlikely to be important in the inhibitory activity of C1-INH toward its target proteases. Mutations in this part have not been described in patients who have HAE, except for a deletion containing two cysteine residues involved in the stabilization of the serpin domain. Recent studies suggest some anti-inflammatory functions for this N-terminal part, possibly explaining the effects of C1-INH in diseases other than HAE. © 2006 Elsevier Inc. All rights reserved.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0889856106000774; http://dx.doi.org/10.1016/j.iac.2006.08.004; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=33751044151&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/17085281; https://linkinghub.elsevier.com/retrieve/pii/S0889856106000774; https://dx.doi.org/10.1016/j.iac.2006.08.004
Elsevier BV
Provide Feedback
Have ideas for a new metric? Would you like to see something else here?Let us know