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Alan Finkelstein, Ph.D.

Affiliations: 
Physiology & Biophysics, and Neuroscience Albert Einstein College of Medicine, New York, New York, United States 
Area:
Ion-Conducting Channels Incorporated into Planar Lipid Bilayer Membranes
Website:
http://galvani.aecom.yu.edu/home.html
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"Alan Finkelstein"
Bio:

Alan Finkelstein received his Ph.D. from The Rockefeller University and was subsequently invited to join the faculty of the Albert Einstein College of Medicine, where he has remained. He has a long-term interest in transport across membranes, and a more recent fascination with protein translocation. His research has included the permeability properties of planar lipid bilayer membranes, the fusion of lipid vesicles with these membranes, and the properties of channels reconstituted in them. These properties include: water, nonelectrolyte and ion flow through the channels, single-file transport, and voltage gating. In work on diphtheria and the channel-forming colicins, his laboratory has discovered and studied protein translocation associated with their voltage gating. Work on the anthrax toxin has been concerned with how the channel-forming component of the toxin acts to unfold its other protein components and serves as conduit for their translocation.

Mean distance: 13.15 (cluster 32)
 
SNBCP
Cross-listing: Chemistry Tree

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R. John Collier collaborator Albert Einstein (Chemistry Tree)
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Publications

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Kienker PK, Wu Z, Finkelstein A. (2015) Topography of the TH5 Segment in the Diphtheria Toxin T-Domain Channel. The Journal of Membrane Biology
Schiffmiller A, Anderson D, Finkelstein A. (2015) Ion selectivity of the anthrax toxin channel and its effect on protein translocation. The Journal of General Physiology. 146: 183-92
Thomson R, Finkelstein A. (2015) Human trypanolytic factor APOL1 forms pH-gated cation-selective channels in planar lipid bilayers: relevance to trypanosome lysis. Proceedings of the National Academy of Sciences of the United States of America. 112: 2894-9
Kienker PK, Wu Z, Finkelstein A. (2015) Mapping the membrane topography of the TH6-TH7 segment of the diphtheria toxin T-domain channel. The Journal of General Physiology. 145: 107-25
Schiffmiller A, Finkelstein A. (2015) Ion conductance of the stem of the anthrax toxin channel during lethal factor translocation. Journal of Molecular Biology. 427: 1211-23
Vargas-Uribe M, Rodnin MV, Kienker P, et al. (2014) Crucial Role of H322 in the Folding of Diphtheria Toxin T-Domain into the Open-Channel State Biophysical Journal. 106: 717a
Vargas-Uribe M, Rodnin MV, Kienker P, et al. (2013) Crucial role of H322 in folding of the diphtheria toxin T-domain into the open-channel state. Biochemistry. 52: 3457-63
Kienker P, Wu Z, Finkelstein A. (2013) Mapping the Membrane Topography of Segments TH6-TH7 and TH8-TH9 in the Diphtheria Toxin T-Domain Channel Biophysical Journal. 104: 240a
Udho E, Jakes KS, Finkelstein A. (2012) TonB-dependent transporter FhuA in planar lipid bilayers: partial exit of its plug from the barrel. Biochemistry. 51: 6753-9
Kienker P, Wu Z, Finkelstein A. (2012) Evidence for a TH6-TH7 Transmembrane Hairpin in the Diphtheria Toxin T-Domain Open Channel State Biophysical Journal. 102: 657a
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