| Year |
Citation |
Score |
| 2010 |
Slatin SL, Duché D, Baty D. Determinants of the proton selectivity of the colicin A channel. Biochemistry. 49: 4786-93. PMID 20459128 DOI: 10.1021/Bi100122G |
0.659 |
|
| 2008 |
Slatin SL, Finkelstein A, Kienker PK. Anomalous proton selectivity in a large channel: colicin A. Biochemistry. 47: 1778-88. PMID 18205407 DOI: 10.1021/Bi701900X |
0.826 |
|
| 2007 |
Cascales E, Buchanan SK, Duché D, Kleanthous C, Lloubès R, Postle K, Riley M, Slatin S, Cavard D. Colicin biology. Microbiology and Molecular Biology Reviews : Mmbr. 71: 158-229. PMID 17347522 DOI: 10.1128/MMBR.00036-06 |
0.379 |
|
| 2004 |
Slatin SL, Duché D, Kienker PK, Baty D. Gating movements of colicin A and colicin Ia are different. The Journal of Membrane Biology. 202: 73-83. PMID 15702371 DOI: 10.1007/S00232-004-0720-9 |
0.784 |
|
| 2002 |
Slatin SL, Nardi A, Jakes KS, Baty D, Duché D. Translocation of a functional protein by a voltage-dependent ion channel. Proceedings of the National Academy of Sciences of the United States of America. 99: 1286-91. PMID 11830660 DOI: 10.1073/Pnas.022480199 |
0.645 |
|
| 2001 |
Lakey JH, Slatin SL. Pore-forming colicins and their relatives. Current Topics in Microbiology and Immunology. 257: 131-61. PMID 11417119 |
0.526 |
|
| 2001 |
Nardi A, Slatin SL, Baty D, Duché D. The C-terminal half of the colicin A pore-forming domain is active in vivo and in vitro. Journal of Molecular Biology. 307: 1293-303. PMID 11292342 DOI: 10.1006/Jmbi.2001.4524 |
0.607 |
|
| 1998 |
Jakes KS, Kienker PK, Slatin SL, Finkelstein A. Translocation of inserted foreign epitopes by a channel-forming protein. Proceedings of the National Academy of Sciences of the United States of America. 95: 4321-6. PMID 9539735 DOI: 10.1073/Pnas.95.8.4321 |
0.818 |
|
| 1997 |
Kienker PK, Qiu X, Slatin SL, Finkelstein A, Jakes KS. Transmembrane insertion of the colicin Ia hydrophobic hairpin. The Journal of Membrane Biology. 157: 27-37. PMID 9141356 DOI: 10.1007/S002329900213 |
0.835 |
|
| 1996 |
Qiu XQ, Jakes KS, Kienker PK, Finkelstein A, Slatin SL. Major transmembrane movement associated with colicin Ia channel gating. The Journal of General Physiology. 107: 313-28. PMID 8868045 DOI: 10.1085/Jgp.107.3.313 |
0.84 |
|
| 1994 |
Qiu XQ, Jakes KS, Finkelstein A, Slatin SL. Site-specific biotinylation of colicin Ia. A probe for protein conformation in the membrane. The Journal of Biological Chemistry. 269: 7483-8. PMID 8125966 |
0.814 |
|
| 1994 |
Von Tersch MA, Slatin SL, Kulesza CA, English LH. Membrane-permeabilizing activities of Bacillus thuringiensis coleopteran-active toxin CryIIIB2 and CryIIIB2 domain I peptide. Applied and Environmental Microbiology. 60: 3711-7. PMID 7527203 DOI: 10.1128/Aem.60.10.3711-3717.1994 |
0.559 |
|
| 1994 |
Slatin SL, Qiu XQ, Jakes KS, Finkelstein A. Identification of a translocated protein segment in a voltage-dependent channel. Nature. 371: 158-61. PMID 7521016 DOI: 10.1038/371158A0 |
0.743 |
|
| 1994 |
English L, Robbins HL, Von Tersch MA, Kulesza CA, Ave D, Coyle D, Jany CS, Slatin SL. Mode of action of CryIIA: a Bacillus thuringiensis delta-endotoxin Insect Biochemistry and Molecular Biology. 24: 1025-1035. DOI: 10.1016/0965-1748(94)90140-6 |
0.406 |
|
| 1993 |
Walters FS, Slatin SL, Kulesza CA, English LH. Ion channel activity of N-terminal fragments from CryIA(c) delta-endotoxin. Biochemical and Biophysical Research Communications. 196: 921-6. PMID 7694582 DOI: 10.1006/Bbrc.1993.2337 |
0.678 |
|
| 1992 |
English L, Slatin SL. Mode of action of delta-endotoxins from Bacillus thuringiensis: A comparison with other bacterial toxins Insect Biochemistry and Molecular Biology. 22: 1-7. DOI: 10.1016/0965-1748(92)90093-T |
0.669 |
|
| 1991 |
Abrams CK, Jakes KS, Finkelstein A, Slatin SL. Identification of a translocated gating charge in a voltage-dependent channel. Colicin E1 channels in planar phospholipid bilayer membranes. The Journal of General Physiology. 98: 77-93. PMID 1719126 DOI: 10.1085/Jgp.98.1.77 |
0.842 |
|
| 1990 |
Andrews NW, Abrams CK, Slatin SL, Griffiths G. A T. cruzi-secreted protein immunologically related to the complement component C9: evidence for membrane pore-forming activity at low pH. Cell. 61: 1277-87. PMID 2194668 DOI: 10.1016/0092-8674(90)90692-8 |
0.71 |
|
| 1990 |
Slatin SL, Abrams CK, English L. Delta-endotoxins form cation-selective channels in planar lipid bilayers. Biochemical and Biophysical Research Communications. 169: 765-72. PMID 1694077 DOI: 10.1016/0006-291X(90)90397-6 |
0.828 |
|
| 1990 |
Jakes KS, Abrams CK, Finkelstein A, Slatin SL. Alteration of the pH-dependent ion selectivity of the colicin E1 channel by site-directed mutagenesis. The Journal of Biological Chemistry. 265: 6984-91. PMID 1691183 |
0.819 |
|
| 1988 |
Slatin SL. Colicin E1 in planar lipid bilayers. The International Journal of Biochemistry. 20: 737-44. PMID 3049178 DOI: 10.1016/0020-711X(88)90058-4 |
0.781 |
|
| 1986 |
Liu QR, Crozel V, Levinthal F, Slatin S, Finkelstein A, Levinthal C. A very short peptide makes a voltage-dependent ion channel: the critical length of the channel domain of colicin E1. Proteins. 1: 218-29. PMID 2453053 DOI: 10.1002/Prot.340010304 |
0.768 |
|
| 1986 |
Raymond L, Slatin SL, Finkelstein A, Liu QR, Levinthal C. Gating of a voltage-dependent channel (colicin E1) in planar lipid bilayers: translocation of regions outside the channel-forming domain. The Journal of Membrane Biology. 92: 255-68. PMID 2431149 DOI: 10.1007/Bf01869394 |
0.838 |
|
| 1986 |
Slatin SL, Raymond L, Finkelstein A. Gating of a voltage-dependent channel (colicin E1) in planar lipid bilayers: the role of protein translocation. The Journal of Membrane Biology. 92: 247-54. PMID 2431148 DOI: 10.1007/Bf01869393 |
0.809 |
|
| 1985 |
Raymond L, Slatin SL, Finkelstein A. Channels formed by colicin E1 in planar lipid bilayers are large and exhibit pH-dependent ion selectivity. The Journal of Membrane Biology. 84: 173-81. PMID 2582133 DOI: 10.1007/Bf01872215 |
0.806 |
|
| 1983 |
Cleveland MV, Slatin S, Finkelstein A, Levinthal C. Structure-function relationships for a voltage-dependent ion channel: properties of COOH-terminal fragments of colicin E1. Proceedings of the National Academy of Sciences of the United States of America. 80: 3706-10. PMID 6304732 DOI: 10.1073/Pnas.80.12.3706 |
0.743 |
|
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