期刊
BIOPHYSICAL JOURNAL
卷 97, 期 4, 页码 L5-L7出版社
CELL PRESS
DOI: 10.1016/j.bpj.2009.05.046
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资金
- Engineering and Physical Sciences Research Council
- Biotechnology and Biological Sciences Research Council
- Medical Research Council
- Wellcome Trust, UK
- Fundacao para a Ciencia e a Tecnologia, Portugal
- Biotechnology and Biological Sciences Research Council [BB/D000467/1] Funding Source: researchfish
We present a general method called dynamic single-molecule colocalization for quantitating the associations of single cell surface molecules labeled with distinct autofluorescent proteins. The chief advantages of the new quantitative approach are that, in addition to stable interactions, it is capable of measuring nonconstitutive associations, such as those induced by the cyloskeleton, and it is applicable to situations where the number of molecules is small.
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