Literature DB >> 21500332

A FlAsH-tetracysteine assay for quantifying the association and orientation of transmembrane α-helices.

Christopher J Pace1, Qiongying Huang, Fang Wang, Kanwal S Palla, Amelia A Fuller, Jianmin Gao.   

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Year:  2011        PMID: 21500332     DOI: 10.1002/cbic.201000736

Source DB:  PubMed          Journal:  Chembiochem        ISSN: 1439-4227            Impact factor:   3.164


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  6 in total

1.  Rotamer-Restricted Fluorogenicity of the Bis-Arsenical ReAsH.

Authors:  Allison S Walker; Paul R Rablen; Alanna Schepartz
Journal:  J Am Chem Soc       Date:  2016-05-10       Impact factor: 15.419

Review 2.  Advances in chemical labeling of proteins in living cells.

Authors:  Qi Yan; Marcel P Bruchez
Journal:  Cell Tissue Res       Date:  2015-03-07       Impact factor: 5.249

3.  Surveying protein structure and function using bis-arsenical small molecules.

Authors:  Rebecca A Scheck; Alanna Schepartz
Journal:  Acc Chem Res       Date:  2011-07-18       Impact factor: 22.384

4.  High-resolution helix orientation in actin-bound myosin determined with a bifunctional spin label.

Authors:  Benjamin P Binder; Sinziana Cornea; Andrew R Thompson; Rebecca J Moen; David D Thomas
Journal:  Proc Natl Acad Sci U S A       Date:  2015-06-08       Impact factor: 11.205

5.  The transmembrane domains of the bacterial cell division proteins FtsB and FtsL form a stable high-order oligomer.

Authors:  Ambalika S Khadria; Alessandro Senes
Journal:  Biochemistry       Date:  2013-10-18       Impact factor: 3.162

6.  Interactions of AsCy3 with cysteine-rich peptides.

Authors:  Seth C Alexander; Alanna Schepartz
Journal:  Org Lett       Date:  2014-07-07       Impact factor: 6.005

  6 in total

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