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Arash Zarrine-Afsar - Publications

Affiliations: 
University of Toronto, Toronto, ON, Canada 
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6 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2015 Czar MF, Zosel F, König I, Nettels D, Wunderlich B, Schuler B, Zarrine-Afsar A, Jockusch RA. Gas-Phase FRET Efficiency Measurements To Probe the Conformation of Mass-Selected Proteins. Analytical Chemistry. 87: 7559-65. PMID 26110465 DOI: 10.1021/Acs.Analchem.5B01591  0.599
2013 Rosenzweig R, Moradi S, Zarrine-Afsar A, Glover JR, Kay LE. Unraveling the mechanism of protein disaggregation through a ClpB-DnaK interaction. Science (New York, N.Y.). 339: 1080-3. PMID 23393091 DOI: 10.1126/Science.1233066  0.335
2009 Zhang F, Zarrine-Afsar A, Al-Abdul-Wahid MS, Prosser RS, Davidson AR, Woolley GA. Structure-based approach to the photocontrol of protein folding. Journal of the American Chemical Society. 131: 2283-9. PMID 19170498 DOI: 10.1021/Ja807938V  0.393
2005 Maxwell KL, Wildes D, Zarrine-Afsar A, De Los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallée-Bélisle A, Main ER, Bemporad F, Qiu L, Teilum K, et al. Protein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Science : a Publication of the Protein Society. 14: 602-16. PMID 15689503 DOI: 10.1110/Ps.041205405  0.331
2005 Zarrine-Afsar A, Davidson AR. The analysis of protein folding kinetic data produced in protein engineering experiments. Methods (San Diego, Calif.). 34: 41-50. PMID 15283914 DOI: 10.1016/j.ymeth.2004.03.013  0.381
2003 Zarrine-Afsar A, Krylov SN. Use of capillary electrophoresis and endogenous fluorescent substrate to monitor intracellular activation of protein kinase A. Analytical Chemistry. 75: 3720-4. PMID 14572035 DOI: 10.1021/ac034463+  0.362
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