エキソサイト、非活性部位
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2016/09/01 10:10:34」(JST)
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An exosite is a secondary binding site, remote from the active site, on an enzyme or other protein.[1]
This is similar to allosteric sites, but differs in the fact that, in order for an enzyme to be active, its exosite typically must be occupied.[2] Exosites have recently become a topic of increased interest in biomedical research as potential drug targets.[3][4]
References
- ^ IngentaConnect Manipulation of thrombin exosite I, by ligand-directed covalent m
- ^ Congress of the International Society on Thrombosis and Haemostasis Archived November 26, 2004, at the Wayback Machine.
- ^ Muller, Jens. "An Exosite-Specific ssDNA Aptamer Inhibits the Anticoagulant Functions of Activated Protein C and Enhances Inhibition by Protein C Inhibitor". Cell.com. Retrieved 11 May 2013.
- ^ Serine Endopeptidases: Advances in Research and Application: 2011 Edition. ScholarlyAdditions. Retrieved 11 May 2013.
External links
- http://bloodjournal.hematologylibrary.org/cgi/reprint/84/6/1843.pdf
UpToDate Contents
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English Journal
- Functional characterization of selective exosite-binding inhibitors of matrix metalloproteinase-13 (MMP-13) - experimental validation in human breast and colon cancer.
- Kothapalli R1, Sivaraman Siveen K2, Tan TZ3, Paul Thiery J3,4,5, Kumar AP2,3,6,7, Sethi G2, Swaminathan K8.
- Bioscience, biotechnology, and biochemistry.Biosci Biotechnol Biochem.2016 Jun 29:1-10. [Epub ahead of print]
- Considering the pathological significance of MMP-13 in breast and colon cancers, exosite-based inhibition of the C-terminal hemopexin (Hpx) domain could serve as an alternative strategy to develop selective inhibitors for MMP-13.Two of six lead compounds, compound 5 (2,3-dihydro-1,4-benzodioxine-5-c
- PMID 27362887
- Polyphosphate is a novel cofactor for regulation of complement by the serpin, C1-inhibitor.
- Wijeyewickrema LC1, Lameignere E2, Hor L1, Duncan RC1, Shiba T3, Travers RJ4, Kapopara PR2, Lei V2, Smith SA4, Kim H5, Morrissey JH4, Pike RN1, Conway EM6.
- Blood.Blood.2016 Jun 23. pii: blood-2016-02-699561. [Epub ahead of print]
- The complement system plays a key role in innate immunity, inflammation and coagulation. The system is delicately balanced by negative regulatory mechanisms that modulate the host response to pathogen invasion and injury. The serpin, C1 inhibitor (C1-INH), is the only known plasma inhibitor of C1s,
- PMID 27338096
- Reprogramming Caspase-7 Specificity by Regio-Specific Mutations and Selection Provides Alternate Solutions for Substrate Recognition.
- Hill ME1, MacPherson DJ1, Wu P1, Julien O, Wells JA, Hardy JA1.
- ACS chemical biology.ACS Chem Biol.2016 Jun 17;11(6):1603-12. doi: 10.1021/acschembio.5b00971. Epub 2016 Mar 31.
- The ability to routinely engineer protease specificity can allow us to better understand and modulate their biology for expanded therapeutic and industrial applications. Here, we report a new approach based on a caged green fluorescent protein (CA-GFP) reporter that allows for flow-cytometry-based s
- PMID 27032039
Japanese Journal
- Exosite-interactive regions in the A1 and A2 domains of factor VIII facilitate thrombin-catalyzed cleavage of heavy chain
- 日本血栓止血学会誌 = The Journal of Japanese Society on Thrombosis and Hemostasis 15(4), 366-369, 2004-08-01
- NAID 130000067736
- The fourth epidermal growth factor-like domain of thrombomodulin interacts with the basic exosite of protein C
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