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Examining the mechanism of action of a kinesin inhibitor using stable isotope labeled inhibitors for cross-linking (SILIC).(Report)

A method, Stable Isotope Labeled Inhibitors for Cross-linking (SILIC) is developed based on research involving photo-cross-linking and the use of mixtures of stable isotopes, for mapping a small molecule inhibitor's binding site in its target protein. The proposed method in combination with mutagene... Full description

Journal Title: Journal of the American Chemical Society August 17, 2011, Vol.133(32), p.12386-12389
Main Author: Wacker, Sarah A.
Other Authors: Kashyap, Sudhir , Xiang Li , Kapoor, Tarun M.
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 0002-7863
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title: Examining the mechanism of action of a kinesin inhibitor using stable isotope labeled inhibitors for cross-linking (SILIC).(Report)
format: Article
creator:
  • Wacker, Sarah A.
  • Kashyap, Sudhir
  • Xiang Li
  • Kapoor, Tarun M.
subjects:
  • Antineoplastic Agents -- Structure
  • Antineoplastic Agents -- Chemical Properties
  • Binding Sites (Biochemistry) -- Research
  • Cell Division -- Research
  • Mass Spectrometry -- Usage
  • Molecular Motors (Biochemistry) -- Structure
  • Molecular Motors (Biochemistry) -- Research
  • Structure-activity Relationships (Pharmacology) -- Research
ispartof: Journal of the American Chemical Society, August 17, 2011, Vol.133(32), p.12386-12389
description: A method, Stable Isotope Labeled Inhibitors for Cross-linking (SILIC) is developed based on research involving photo-cross-linking and the use of mixtures of stable isotopes, for mapping a small molecule inhibitor's binding site in its target protein. The proposed method in combination with mutagenesis studies applied to an ATP-competitive inhibitor of kinesin-5, a widely conserved motor protein required for cell division and an anticancer drug target indicated that the inhibitor binds at an allosteric site in the motor protein.
language: English
source:
identifier: ISSN: 0002-7863
fulltext: no_fulltext
issn:
  • 0002-7863
  • 00027863
url: Link


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titleExamining the mechanism of action of a kinesin inhibitor using stable isotope labeled inhibitors for cross-linking (SILIC).(Report)
creatorWacker, Sarah A. ; Kashyap, Sudhir ; Xiang Li ; Kapoor, Tarun M.
ispartofJournal of the American Chemical Society, August 17, 2011, Vol.133(32), p.12386-12389
identifierISSN: 0002-7863
subjectAntineoplastic Agents -- Structure ; Antineoplastic Agents -- Chemical Properties ; Binding Sites (Biochemistry) -- Research ; Cell Division -- Research ; Mass Spectrometry -- Usage ; Molecular Motors (Biochemistry) -- Structure ; Molecular Motors (Biochemistry) -- Research ; Structure-activity Relationships (Pharmacology) -- Research
descriptionA method, Stable Isotope Labeled Inhibitors for Cross-linking (SILIC) is developed based on research involving photo-cross-linking and the use of mixtures of stable isotopes, for mapping a small molecule inhibitor's binding site in its target protein. The proposed method in combination with mutagenesis studies applied to an ATP-competitive inhibitor of kinesin-5, a widely conserved motor protein required for cell division and an anticancer drug target indicated that the inhibitor binds at an allosteric site in the motor protein.
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titleExamining the mechanism of action of a kinesin inhibitor using stable isotope labeled inhibitors for cross-linking (SILIC).(Report)
descriptionA method, Stable Isotope Labeled Inhibitors for Cross-linking (SILIC) is developed based on research involving photo-cross-linking and the use of mixtures of stable isotopes, for mapping a small molecule inhibitor's binding site in its target protein. The proposed method in combination with mutagenesis studies applied to an ATP-competitive inhibitor of kinesin-5, a widely conserved motor protein required for cell division and an anticancer drug target indicated that the inhibitor binds at an allosteric site in the motor protein.
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abstractA method, Stable Isotope Labeled Inhibitors for Cross-linking (SILIC) is developed based on research involving photo-cross-linking and the use of mixtures of stable isotopes, for mapping a small molecule inhibitor's binding site in its target protein. The proposed method in combination with mutagenesis studies applied to an ATP-competitive inhibitor of kinesin-5, a widely conserved motor protein required for cell division and an anticancer drug target indicated that the inhibitor binds at an allosteric site in the motor protein.
pubAmerican Chemical Society
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date2011-08-17