Research Topics
| Alan FinkelsteinSummaryAffiliation: Albert Einstein College of Medicine Country: USA Publications
| Collaborators
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Detail Information
Publications
The number of subunits comprising the channel formed by the T domain of diphtheria toxinM Gordon
Department of Neuroscience, Albert Einstein College of Medicine, Bronx, NY 10461, USA
J Gen Physiol 118:471-80. 2001..The observed single channels were blocked at either negative or positive voltages, but never both. Therefore, we conclude that the T domain channel is monomeric...
The diphtheria toxin channel-forming T-domain translocates its own NH2-terminal region and the catalytic domain across planar phospholipid bilayersA Finkelstein
Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, NY 10461, USA
Int J Med Microbiol 290:435-40. 2000..g., toxin receptor) or of any other cellular components...- TonB-dependent transporter FhuA in planar lipid bilayers: partial exit of its plug from the barrelEshwar Udho
Deptartment of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, NY 10461, USA
Biochemistry 51:6753-9. 2012..Negative staining electron microscopy showed that FhuA in a detergent solution formed vesicles, thus explaining why an osmotic gradient promoted the insertion of FhuA into membranes... - Proton-coupled protein transport through the anthrax toxin channelAlan Finkelstein
Departments of Physiology and Biophysics and Neuroscience, Albert Einstein College of Medicine, Bronx, NY 10461, USA
Philos Trans R Soc Lond B Biol Sci 364:209-15. 2009..This paper discusses how the (PA63)7 channel both participates in the unfolding of LF and OF and functions in their translocation as a proton-protein symporter... - A kinetic analysis of protein transport through the anthrax toxin channelDaniel Basilio
Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, NY 10461, USA
J Gen Physiol 137:521-31. 2011..The cumulative distribution of first-passage times of the rod past the end of the channel displays S-shaped kinetics with a voltage dependence in agreement with experimental data... - Trapping a translocating protein within the anthrax toxin channel: implications for the secondary structure of permeating proteinsDaniel Basilio
Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, NY 10461, USA
J Gen Physiol 137:343-56. 2011..e., the channel unfolds the secondary structure of the protein. We also show that the channel not only can translocate LF(N) in the normal direction but also can, at least partially, translocate LF(N) in the opposite direction... - The colicin Ia receptor, Cir, is also the translocator for colicin IaKaren S Jakes
Department of Physiology and Biophysics, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA
Mol Microbiol 75:567-78. 2010..We show that purified T domain competes with Ia and protects E. coli from being killed by it. Thus, in addition to binding to colicin Ia's receptor-binding domain, Cir also binds weakly to its translocation domain... - Protein translocation by bacterial toxin channels: a comparison of diphtheria toxin and colicin IaZhengyan Wu
Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, New York 10461, USA
Biophys J 91:3249-56. 2006..This difference cannot be attributed to specific recognition of the A chain by diphtheria toxin's translocation pathway because the translocation pathway also accommodates folded myoglobin... - Identification of channel-lining amino acid residues in the hydrophobic segment of colicin IaPaul K Kienker
Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, NY 10461, USA
J Gen Physiol 132:693-707. 2008.... - Evidence for a proton-protein symport mechanism in the anthrax toxin channelDaniel Basilio
Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, NY 10461, USA
J Gen Physiol 133:307-14. 2009..We also find that a site that disfavors the entry of negatively charged residues into the (PA(63))(7) channel resides at or near its Phi-clamp, the ring of seven phenylalanines near the channel's entrance... - Reconstitution of bacterial outer membrane TonB-dependent transporters in planar lipid bilayer membranesEshwar Udho
Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, NY 10461, USA
Proc Natl Acad Sci U S A 106:21990-5. 2009..We hypothesize that 4 M urea reversibly unfolds the FhuA and Cir plugs, thereby opening an ion-conducting pathway through these channels, and that this mimics to some extent the in vivo action of TonB on these plugs... - Sizing the protein translocation pathway of colicin Ia channelsPaul K Kienker
Department of Physiology and Biophysics, Albert Einstein College of Medicine, 1300 Morris Park Ave, Bronx, NY 10461, USA
J Gen Physiol 122:161-76. 2003..Thus, the pathway for translocation is >/=26 A in diameter, or can stretch to this value. This is large enough for an alpha-helical hairpin to fit through... 
Anomalous proton selectivity in a large channel: colicin AStephen L Slatin
Department of Physiology and Biophysics, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 10461, USA
Biochemistry 47:1778-88. 2008..We are thus compelled to propose that an unorthodox mechanism is at work in this protein...- PA63 channel of anthrax toxin: an extended beta-barrelShilla Nassi
Department of Neuroscience and Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, New York 10461, USA
Biochemistry 41:1445-50. 2002..The implication is that major rearrangement of domains in the prepore cap region is required for membrane insertion of the beta-barrel stem... - Protein translocation through anthrax toxin channels formed in planar lipid bilayersSen Zhang
Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts, USA
Biophys J 87:3842-9. 2004.... - Protein translocation through the anthrax toxin transmembrane pore is driven by a proton gradientBryan A Krantz
Department of Microbiology and Molecular Genetics, Harvard Medical School 200 Longwood Ave, Boston, MA 02115, USA
J Mol Biol 355:968-79. 2006..In a sense, the channel functions as a proton/protein symporter... - A phenylalanine clamp catalyzes protein translocation through the anthrax toxin poreBryan A Krantz
Department of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA
Science 309:777-81. 2005..We conclude that the phi clamp serves a chaperone-like function, interacting with hydrophobic sequences presented by the protein substrate as it unfolds during translocation... - Evidence that translocation of anthrax toxin's lethal factor is initiated by entry of its N terminus into the protective antigen channelSen Zhang
Department of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA
Proc Natl Acad Sci U S A 101:16756-61. 2004....