DocumentCode
3319605
Title
Notice of Retraction
In Silico Investigation of Interaction between Human Neutrophil Elastase and Sea Anemone Heteractis crispa Kunitz Polypeptides
Author
Zelepuga, E. ; Tabakmakher, V. ; Monastyrnaya, M. ; Lukyanov, P. ; Kozlovskaya, E.
Author_Institution
Pacific Inst. of Bioorganic Chem., Far Eastern Branch of Russian Acad. of Sci., Vladivostok, Russia
fYear
2011
fDate
10-12 May 2011
Firstpage
1
Lastpage
4
Abstract
Notice of Retraction
After careful and considered review of the content of this paper by a duly constituted expert committee, this paper has been found to be in violation of IEEE´s Publication Principles.
We hereby retract the content of this paper. Reasonable effort should be made to remove all past references to this paper.
The presenting author of this paper has the option to appeal this decision by contacting TPII@ieee.org.
Serine proteinase neutrophil elastase plays a principle role in inflammatory processes. Therefore, explanation of the selective elastase inhibitors action mechanisms attracts the great interest of the modern biomedicine and bioinformatics. Currently, there are many investigations devoted to search of polypeptide agents effectively suppressing the inflammatory process. Recent studies have shown that some Kunitz type serine proteinase inhibitors may render an anti-inflammatory effect. Here we represent model of complexes of sea anemone Heteractis crispa Kunitz polypeptides (HCPs) with human neutrophil elastase (HNE) and discuss driving forces of the enzyme-inhibitor interaction. Proposed models allow for the first time to clarify the molecular mechanism of these polypeptides anti-inflammatory action.
After careful and considered review of the content of this paper by a duly constituted expert committee, this paper has been found to be in violation of IEEE´s Publication Principles.
We hereby retract the content of this paper. Reasonable effort should be made to remove all past references to this paper.
The presenting author of this paper has the option to appeal this decision by contacting TPII@ieee.org.
Serine proteinase neutrophil elastase plays a principle role in inflammatory processes. Therefore, explanation of the selective elastase inhibitors action mechanisms attracts the great interest of the modern biomedicine and bioinformatics. Currently, there are many investigations devoted to search of polypeptide agents effectively suppressing the inflammatory process. Recent studies have shown that some Kunitz type serine proteinase inhibitors may render an anti-inflammatory effect. Here we represent model of complexes of sea anemone Heteractis crispa Kunitz polypeptides (HCPs) with human neutrophil elastase (HNE) and discuss driving forces of the enzyme-inhibitor interaction. Proposed models allow for the first time to clarify the molecular mechanism of these polypeptides anti-inflammatory action.
Keywords
biomedical materials; enzymes; molecular biophysics; enzyme-inhibitor interaction; human neutrophil elastase; in silico investigation; molecular mechanism; polypeptide anti-inflammatory action; sea anemone Heteractis crispa Kunitz polypeptides; Computational modeling; Inhibitors; Pain; Protein engineering; Proteins; Servers;
fLanguage
English
Publisher
ieee
Conference_Titel
Bioinformatics and Biomedical Engineering, (iCBBE) 2011 5th International Conference on
Conference_Location
Wuhan
ISSN
2151-7614
Print_ISBN
978-1-4244-5088-6
Type
conf
DOI
10.1109/icbbe.2011.5780140
Filename
5780140
Link To Document