Linked Life Data

12663938

Source:http://linkedlifedata.com/resource/pubmed/id/12663938

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2003-3-28
pubmed:abstractText
Most antimitotic compounds have highly specific interactions with tubulin, the major protein component of microtubules. It is, therefore, often desirable to characterize interactions of these agents with tubulin. In particular, quantitative comparisons between new and old ("standard") agents, between different classes of agent, and between structural analogs (e.g., for a structure activity relationship study) are important. Because antimitotic drugs have a variety of effects on tubulin and bind at multiple distinct sites on the protein, the tubulin assembly reaction is probably the only universally applicable reaction that can be analyzed. In my laboratory, we use the assembly of purified tubulin induced by higher concentrations of monosodium glutamate as our basic assay system. This report presents a detailed description of our current routine assay, including the effects of a variety of reaction components on the reaction. In addition, the variety of effects that reaction components can have on the quantitative results obtained with drugs, using the colchicine site drug combretastatin A-4 as a model compound, is described.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1085-9195
pubmed:author
pubmed:issnType
Print
pubmed:volume
38
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-22
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Evaluation of antimitotic agents by quantitative comparisons of their effects on the polymerization of purified tubulin.
pubmed:affiliation
Screening Technologies Branch, Developmental Therapeutics Program, Division of Cancer Treatment and Dignosis, National Cancer Instittue at Frederick, National Institutes of Health, MD 21702, USA. hamele@mail.nih.gov
pubmed:publicationType
Journal Article, Comparative Study, Review, Evaluation Studies